Journal of Pharmacy And Bioallied Sciences
Journal of Pharmacy And Bioallied Sciences Login  | Users Online: 4255  Print this pageEmail this pageSmall font sizeDefault font sizeIncrease font size 
    Home | About us | Editorial board | Search | Ahead of print | Current Issue | Past Issues | Instructions | Online submission

 Table of Contents  
Year : 2013  |  Volume : 5  |  Issue : 1  |  Page : 21-29  

Chitinases: An update

1 Department of Biochemistry, Faculty of Science, Jamia Hamdard, New Delhi, India
2 Department of Biotechnology, Faculty of Science, Jamia Hamdard, New Delhi, India
3 Department of Microbiology, Faculty of Agricultural Sciences, AMU, Aligarh, India

Date of Submission21-Nov-2011
Date of Decision16-Mar-2012
Date of Acceptance21-May-2012
Date of Web Publication28-Jan-2013

Correspondence Address:
Saleem Javed
Department of Biochemistry, Faculty of Science, Jamia Hamdard, New Delhi
Login to access the Email id

Source of Support: Department of Science and Technology (DST), India, Conflict of Interest: None

DOI: 10.4103/0975-7406.106559

Rights and Permissions

Chitin, the second most abundant polysaccharide in nature after cellulose, is found in the exoskeleton of insects, fungi, yeast, and algae, and in the internal structures of other vertebrates. Chitinases are enzymes that degrade chitin. Chitinases contribute to the generation of carbon and nitrogen in the ecosystem. Chitin and chitinolytic enzymes are gaining importance for their biotechnological applications, especially the chitinases exploited in agriculture fields to control pathogens. Chitinases have a use in human health care, especially in human diseases like asthma. Chitinases have wide-ranging applications including the preparation of pharmaceutically important chitooligosaccharides and N-acetyl D glucosamine, preparation of single-cell protein, isolation of protoplasts from fungi and yeast, control of pathogenic fungi, treatment of chitinous waste, mosquito control and morphogenesis, etc. In this review, the various types of chitinases and the chitinases found in different organisms such as bacteria, plants, fungi, and mammals are discussed.

Keywords: Chitinases, chitinolytic enzymes, endochitinase, exochitinases

How to cite this article:
Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S. Chitinases: An update. J Pharm Bioall Sci 2013;5:21-9

How to cite this URL:
Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S. Chitinases: An update. J Pharm Bioall Sci [serial online] 2013 [cited 2022 Dec 7];5:21-9. Available from:

Chitin, a linear polymer of β-1, 4-N-acetylglucosamine (GlcNAC), is the second most abundant biopolymer on the planet. [1] Chitin is found in the outer skeleton of insects, fungi, yeasts, algae, crabs, shrimps, and lobsters, and in the internal structures of other invertebrates. [2] The overall weight of shellfish (e.g. crab, krill and shrimp), which is disposed as waste, is approximately 75%, and chitin consists of 20-58% of that dry weight. [3] Amid a broad array of applications, chitin has its use in order to boost up the formation of extracellular chitinase. Chitin and its associated materials have a broad usage in drug delivery, wound healing, dietary fiber, and in waste water treatment. [4] Chitin is a white, hard, inelastic polysaccharide, and is a major contribution to pollution in coastal areas. [5] Chitin has a high percentage of nitrogen (6.89%), which makes it a useful chelating agent. [6] Chitin exists in 2 allomorphic forms i.e. α-chitin and β-chitin. These 2 forms of chitin vary in packing and polarities of adjacent chains in the succeeding sheets. [7],[8] Chitin can be degraded by chitinase. The catabolism of chitin takes place in 2 steps, involving the initial cleavage of the chitin polymer by chitinases into chitin oligosaccharides and further cleavage to N-acetylglucosamine, and monosaccharides by chitobiases. [9]

Chitinases (E.C are glycosyl hydrolases with the sizes ranging from 20 kDa to about 90 kDa. [2] They are present in a wide range of organisms such as bacteria, fungi, yeasts, plants, actinomycetes, arthropods, and humans. Chitinases have the ability to degrade chitin directly to low molecular weight chitooligomers, which serve a broad range of industrial, agricultural, and medical functions such as elicitor action and anti-tumor activity. [10] N-acetylglucosamine (GlcNAc) has received special attention for the treatment of osteoarthritis. [11] Chitinases have been receiving an increased attention due to their role in the biocontrol of fungal phytopathogens [12] and harmful insects. [13] Of late, chitinases have also attained a lot of attention as they are thought to play a key role in mosquito control and plant defense systems against chitin-containing pathogens. [13] Chitin and chitinases are used by pathogens (mainly protozoan or metazoan) causing animal and human diseases. Several pathogens contain chitin coats, giving them protection against both external and internal (in a host) environment. Others attack their host using chitinase. In order to establish a successful infection or transmission from one vertebrate to another, they exploit the chitin-containing structures of the host. [14] A number of bacteria have the ability to produce chitinases, including Streptomyces, [15] Alteromonas, [16] Escherchia, [17] Aeromonas. [18] Chitinase-producing bacteria have been isolated from soil, shellfish waste, garden and park waste compost, and hot springs. [10]

Chitinases have been divided into 2 main groups: Endochitinases (E.C and exo-chitinases. The endochitinases randomly split chitin at internal sites, thereby forming the dimer di- cetylchitobiose and soluble low molecular mass multimers of GlcNAc such as chitotriose, and chitotetraose. [19] The exo- chitinases have been further divided into 2 subcategories: Chitobiosidases (E.C., [20] which are involved in catalyzing the progressive release of di-acetylchitobiose starting at the non-reducing end of the chitin microfibril, and 1-4-β-glucosaminidases (E.C., cleaving the oligomeric products of endochitinases and chitobiosidases, thereby generating monomers of GlcNAc. [19]

Based on this nomenclature, the identification of various chitinases in Serratia plymuthica has been carried out for the strains IC1270, IC14, and HRO-C48. It has been reported that, in the strains IC14 and HRO-C48, an endochitinase and a 100 kDa N-acetyl-β-1,4-D-hexosaminidase or chitobiase are produced, while the strain IC1270 produces N-acetyl- β-D- glucosaminidases of 89 and 67 kDa, a 50 kDa chitobiosidases, and an endochitinase with a molecular mass of 59 kDa. [21],[22] As far as the amino acid similarity of chitinases from various organisms is considered, 5 classes of chitinases have been proposed, and have been categorized into 2 families, which include families 18 and 19 of glycosyl hydrolases. [23] Family 18 chitinases have a large distribution in organisms, including plants, bacteria, fungi (classes III and V), mammals, and viruses. The sub-classification of chitinases is also based on N-terminal sequence, isoelectric pH, localization of the enzyme, signal peptide, and inducers. The class I chitinases have been found in plants, whereas class II enzymes are contained in plants, fungi, and bacteria. There is no sequence similarity of class III chitinases to enzymes of class I or II. Class I chitinases have similar characteristics to class IV chitinases, including immunological properties, but they are significantly smaller than class I chitinases. [24]

Chitinases are a huge and diverse group of enzymes that show differences in their molecular structure, substrate specificity, and catalytic mechanism. [25] It is vital to study the substrate specificity of chitinases as it not only reveals the relationship between the substrate specificity and physiological roles, but also allows one to degrade chitin into novel products having industrial applications. [26] It has been found that, individually, all chitinase classes exhibit different substrate specificities and reaction mechanisms. For example, in the case of tobacco class III chitinases, a considerable level of lysozyme as well as chitinase activity is possessed while class VI chitinases only show chitinase activity. [27] Class I and class II chitinases use an inverting mechanism in order to hydrolyze β-glycosidic linkage while class III chitinases do this through a retaining mechanism. [28],[29] It has been established by Sasaki et al. (2006)? [30] that class III chitinases do not act against GlcNAc oligomer or polymer, but could be active on an endogenous complex carbohydrate containing a GlcNAc residue, whereas a GlcNAc sequence was the most likely substrate of the class I enzyme.

The chitinases of the 2 different families do not share amino acid sequence similarity, and have completely different 3-dimensional (3D) structures and molecular mechanisms. Therefore, they are likely to have evolved from different ancestors. Family 18 consists of a number of conserved repeats of amino acids. It consists of an enzyme core, which has 8 strands of parallel β sheets, forming a barrel laid down α helices, which in turn forms a ring towards the outside. [31] GH family 18 chitinases have the ability to catalyze the transglycosylation reactions. The products formed due to transglycosylation have already been reported for T. harzianum Chit42 and Chit33, as well as for Aspergillus fumigatus ChiB1. [32]

A multidomain structure including catalytic domains and both a cysteine-rich chitin-binding domain (different from the catalytic domain) and a serine/threonine-rich glycosylated domain have been found as one of the structural characteristics of chitinases in various animals and microorganisms. [33] The resemblance shown by bacterial and fungal chitinases suggests that the catalytic domains are similar in all of these. [34]

A broad study of chitin-binding domains in plant proteins revealed that the 8 cysteins within the chitin-binding domain are greatly conserved. Moreover, plants also possess chitin-binding proteins (CBPs) having a cystein-rich chitin-binding domain, without chitinase activity. [35] As reported by Poole et al., 1993, [36] in bacteria, the chitin-binding domain is different than that found in plants, which contain 8 conserved cystein residues. On the contrary, some amino acids, mainly tryptophan, are amongst the residues that are conserved in their chitin-binding domain of bacteria, and their involvement in the binding of cellulase to cellulose has been revealed. The role of chitinases has also been implicated in the binding of a non-catalytic chitin-binding protein to chitin. [37] It has been identified by Watanabe et al., 1997 [38] that there are only 4 amino acids in the catalytic domain that are conserved between bacterial and plant class III chitinases.

It is thought that the fungal chitinases attach to their substrate or cell wall with the help of the chitin-binding domain. A 6-cystein conserved region present in the chitin-binding domain of CTS1 and K1Cts1p is probably involved in the protein-protein interaction or tertiary structure through the disulphide bond formation. According to Villagomez et al., 1996, [39] the C-terminal chitin-binding domain in insect chitinases binds to the substrate and it has a characteristic 6-cystein motif similar to nematode chitinases.

   Bacterial Chitinases Top

In bacterial chitinases, the chitin-binding domain can either be located in the amino terminal or in the carboxyl terminal domains of the enzyme. [40] Most of the bacterial chitinases, which have been isolated and sequenced so far, are included in family 18 of the glycosyl hydrolases; with the exception of a chitinase (C-1) isolated from S. griseus IIUT 6037 that belongs to the family 19 of the glycosyl hydrolases. [41] Unlike bacterial chitinases, this can hydrolyze only GlcNAc-GlcNAc and GlcNAc-glucosamine linkages; chitinase C-1 of S. griseus HUT 6037 has the capability to hydrolyze glucosamine-GlcNAc and GlcNAc-GlcNAc linkages. Thus, the catalytic site of chitinase C-1 is different from other microbial chitinases. The amino terminal region of chitinase C-1 share sequences similarity with non-catalytic domains of other bacterial lytic enzymes including chitinases, proteases, and cellulases, and it is postulated that this domain serves for chitin binding. [41] Some other species of bacteria that also produce high levels of chitinolytic enzymes are Serratia.[38],[42] Bacterial chitinases having a molecular weight range of 20-60 kDa are smaller than insect chitinases (40-85 kDa) while similar to that of plant chitinases (40-85 kDa). [2] Bacterial chitinases are active over a wide range of pH and temperatures, depending on the source of the bacteria from which they have been isolated. For example, endochitinase from Streptomyces violaceusniger[43] and thermostable chitinase from Streptomyces thermoviolaceus OPC-520 [16] have an optimum temperature of, respectively, 28°C and 80°C. Also, the last enzyme has high pH optima in the range of 8.0 to 10.075, while the chitinase isolated from Stenotrophomonas maltophilia C3 has a pH optima in the range of 4.5 to 5.0. Bacterial chitinases also show a broad range of isoelectric points (pI 4.5-8.5). [38]

It is considered that in order to supply nitrogen and carbon as a source of nutrients, bacteria mainly produce chitinases. [44] The production of chitinases in bacteria is mainly for the degradation of chitin and its utilization as an energy source. As reported by Chernin, 1997 [45] and Downing, 2000, [46] some chitinases of chitinolytic bacteria, such as the chiA gene products from Serratia marcescens and S. plymuthica, are potential agents for the biological control of plant diseases caused by various phytopathogenic fungi. The latter enzymes hydrolyze the chitin present in the fungal cell wall, thereby inhibiting fungal growth. Anti-fungal proteins such as chitinases have a great biotechnological aspect because of their potential use as food and seed preservative agents and for engineering plants for resistance to phytopathogenic fungi. [47] Ordentlich (1988) [48] reported the effectiveness of S. marcescens as a biocontrol agent against Sclerotium rolfsii via its chitinolytic culture filtrate. The vast majority of known bacterial chitinases are grouped into family 18. [49] Since most bacterial chitinases that have been characterized thus far have been classified into group A, it has been speculated that group A chitinase genes are more abundant in nature than enzymes in groups B or C. [50] Bacterial chitinases generally consist of multiple functional domains, such as chitin-binding domain (CBD) and Wibronectin type III-like domain (Fn3 domains), linked to the catalytic domain. The importance of the CBD in the degradation of insoluble chitin has been demonstrated for some bacterial chitinase. [51] In contrast, it has been found that family 19 chitinases are present only in some bacterial strains and plants. [52]

The presence of multiple chitinase producing enzymes have been described in various microorganisms such as Aeromonas sp. No. 10S-24, [53] Pseudomonas aeruginosa K-187, [3] Bacillus circulans WL-12. [54]

A synergistic action of Chi A, Chi B, and Chi C1 of S. marcescens 2170 has been reported by Suzuki et al. (2002) [42] on chitin degradation. In spite of having comparable catalytic domains, Chi A and Chi B were thought to digest chitin chains in reverse directions, i.e., Chi A from the reducing end and Chi B from the non-reducing end.

   Fungal Chitinases Top

Fungal chitinases, like bacterial chitinases, have multiple functions as they play an important role in nutrition, morphogenesis, and fungal development processes. Chitin is a major cell wall component of fungi. [19] Fungal chitinases show a high amino acid homology with class III plant chitinases. [55] Mostly, they belong to the family 18 of the glycosyl hydrolase superfamily. [56] The basic structure of family 18 fungal chitinases consists of 5 domains or regions: (1) catalytic domain, (2) N-terminal signal peptide region, (3) chitin-binding domain, (4) serine/threonine rich-region, and (5) C-terminal extension region. However, serine/threonine rich-region, chitin-binding domain, and C-terminal extension region is absent in most of the fungal chitinases, and these seem to be unnecessary for chitinase activity because naturally-occurring chitinases that lack these regions are still enzymatically active. Fungal chitinases are not as well-classified as the bacterial and plant chitinases, and are identified on the basis of their similarity to family 18 chitinases from bacteria or plants. [57] Therefore, fungal chitinases have been divided into fungal/plant chitinases, which correspond to class III chitinases and show similarity to class V chitinases from plants, fungi, and bacteria. [57] Group C fungal chitinases, which have not yet been characterized, is a novel group of fungal chitinases. It has been predicted that they are as large as 140-170 kDa, and consists of 2 LysM domains and a chitin-binding domain. They have shown resemblance to yeast killer toxins ( ). Chitinases have important physiological and biological roles, which include morphogenetic, autolytic, nutritional, and parasitic roles. For example, disruption of the chitinase gene (CTS1) in the yeast Saccharomyces cerevisiae results in failure of the cells to separate after division and cell clumping, while functional expression of chitosanase and chitinase have been reported to influence morphogenesis in the yeast (Schizosaccharomyces pombe). [58]

Lorito et al., 1994, [59] Ulhoa and Peberdy, 1991, [60] have reported the purification and characterization of 3 N-acetylglucosaminidaes (GlcNAcases) from different isolates of Trichoderma and that their molecular masses were similar, as shown by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, i.e., SDS-PAGE. Draborg et al., 1995 [61] and Peterbauer et al., 1996, [62] reported the cloning of 3 genes of GlcNAcases from Trichoderma sp.: exc1, exc2, and nag1. The genes exc1, exc2 were isolated from T25-1, thereby resulting in the conformation that Trichoderma has 2 different GlcNcases. Lorito et al., 1998, [63] reported the isolation of about 42 kDa endochitinase from Trichoderma. As reported by Yamanaka et al., 1994, [64] Sandor et al., 1998, [65] fungal cell wall chitinases have also been associated with their role in filamentous fungal sporulation since the chitinase inhibitors demethylallosamidin or allosamidin led to the inhibition of fragmentation of hyphae into arthroconidia. Trichoderma spp. have been given the most consideration as biocontrol agents in case of soil borne fungal pathogens amongst various chitinolytic fungi and bacteria. [66],[67],[68] The purification and characterisation of chitinases and β-1,3-glucanases from Talaromyces flavus and Trichoderma spp. has been reported and their function in mycoparasitism of soilborne pathogens i.e. Rhizoctonia solani, S. rolfsii and Fusarium sp. has also been emphasised. [20],[69],[70] Harman (2000) [71] and Yedidia et al., (2000) [72] reported that the valuable effect of Trichoderma on fungi is because of its direct mycoparasitism and it results in induced resistance and increased development in plants. It has been reported by Yaun and Crawford 1995 [73] that the antifungal biocontrol agent,  Streptomyces lydicus Scientific Name Search 8 has the capacity to damage the fungal cell wall hyphae and destroying germinating oospores of Phytium ultimum as well.

Earlier studies have shown that chitinase genes (such as ech42, chi33, nag1, chi18-13) from Trichoderma harzianum have a very important role in mycoparasitism. [74],[75] It has been reported that disruption of ech42 gene affects mycoparasitism in T. harzianum. [76] The isolation of a novel endochitinase called as CHIT36 from T. harzianum isolate TM was reported by Viterbo et al., 2001. [77]

Other important applications of fungal chitinases include the possibility for improving plant resistance with the help of genetic manipulation techniques. The chi42 gene of T. harzianum encodes a powerful endochitinase, which has a much stronger anti-fungal activity against a number of phytopathogenic fungi, and is expressed constitutively in apple, tobacco, and potato. These transgenic plants thereby show a high level of resistance against phytopathogenic fungi. [63] Fungal chitinases are also employed in insect control.

   Plant Chitinases Top

Chitinases are constitutively present in plants, stems, seeds, flowers, and tubers. They are developmentally regulated as well as tissue-specific. Taking into account the amino acid sequences, plant chitinases have been categorized into 5 or 6 classes. The key structure of the class I, II, and IV enzymes contains globular domains. While 8 α-helices and 8 β-strands form the class III and V plant chitinases. The former carries out the hydrolysis of the β-1, 4-glycosidic linkage by means of an inverting mechanism, and the latter through a retaining mechanism. [78] Plant chitinases are produced as pathogenesis-related proteins in plant self defense in response to the attack of phytopathogens, or by contact with elicitors such as chitooligosaccharides or growth regulators such as ethylene. [79] There are some chitinases, which are expressed in response to environmental stresses, (i.e., high salt concentration, cold, and drought). There are also reports of some chitinases, which take part in vital physiological processes of plants, like embryogenesis and ethylene synthesis. [78] Chitinase, which is a polypeptide and a major pathogenesis-related protein, accumulates in the infected plant tissue extracellularly. Garg and Gupta, 2010, [80],[81] reported the isolation and purification of chitinase from moth beans against the fungal pathogen Macrophomina Phaseolina strain 2165. The chitinases of plants can be detected during their development in the early stages of growth. The chitinases of plants are generally endochitinases of smaller molecular weight as compared to the chitinases of insects.

   Insect Chitinases Top

The chitinases found in the insects have been described from Manduca sexta and Bombyx mori. These enzymes have very important roles to play as degradative enzymes during ecdysis where endochitinases randomly break the cuticle to chitooligosaccharides, which are afterwards hydrolyzed by exoenzymes to N-acetyl-glucosamine. The monomer is reused for new cuticle synthesis. Insect chitinases also play defensive roles against their own parasites, and the enzyme production is regulated by hormones during the transformation of the larvae. Allosaminidin is the inhibitor of insect chitinases. [82] Chitinases are also found in crustaceans like shrimps, krills, and prawns.

   Mammalian Chitinases Top

Mammalian chitinases belong to the family 18 of glycosyl hydrolases (GH18), which can be divided into chitinase like proteins with no enzymatic activity, and enzymatically active true chitinases. [7] Chitotriosidase was the first mammalian chitinase to be identified. [83] The N-terminal catalytic domain of GH18 family members consists of triose-phosphate isomerase fold, which is characterized by the (β/α) 8 - barrel structure, and within this barrel, the β4 strand consists of a conserved sequence motif (DXXDXDXE, where D = aspartic acid, E = glutamic acid, and X = any amino acid) forming the active site of the enzyme. Glutamic acid is the key residue donating a proton required for hydrolyzing the β (1-4) glycosidic bond in chitin. [84] In chitinase-like proteins, it is the substitution of this essential glutamic acid to glutamine, leucine, and isoleucine that accounts for the lack of chitinolytic activity. However, as the conserved chitin-binding aromatic residues on the triose- phosphate isomerase barrel remain unaffected, they are still capable of binding to chitin with high affinity. [85]

   Methods of Production of Chitinase Top

A number of methods have been used for the production of microbial chitinases, which include "fed-batch fermentation, continuous fermentation, and liquid batch fermentation." As per the reports of Khan et al., 2010, [86] in the presence of chitin, MgSO4·7H2O and KH2PO4 has a positive effect on chitinase production, whereas yeast extract has a negative effect on chitinase production. It was also reported that there was an enhancement in chitinase secretion with an increase in maltose and chitin concentrations. The components like MgSO4·7H2O, KH2PO4, and yeast extract demonstrated highest chitinase secretion at lower concentration levels. As reported by Bhushan, 1998, [87] and Dahiya, 2005, [88] media constituents for nitrogen and carbon sources and agricultural remains (e.g., wheat bran, rice bran, etc.) influence extracellular chitinase production. He also reported the enhancing effect of glucose on chitinase production when glucose was used in the production medium along with chitin. However, Miyashita et al., 1991, reported that glucose has a repressing effect on the production of chitinase. [89]

Bhushan, 1998, [87] reported that chitinase production is also affected by some physical factors such as pH, aeration, and incubation temperature. He also reported that chitinase production was stimulated in Bacillus sp. BG-11 subsequent to addition of amino acids and their analogs, for example tryptophan, tyrosine, glutamine, and arginine in the growth medium at a concentration of (0.1 mM). In order to improve the production of chitinases from different organisms, several methods, such as biphasic cell systems, cell immobilization, solid-state fermentations, etc., have been used. [87],[90]

There are reports of both natural as well as general enzyme inhibitors, which include oxidizing/reducing agents and organic compounds as well. An antibiotic produced by Streptomyces sp., allosomadin, a competitive inhibitor, has been attained recognition as a specific inhibitor of yeast, insects, fungi, and human serum chitinases. Allosamidin acts as a non-hydrolysable analog of the oxazolinium ion intermediate, thereby exerting its inhibitory effect. [91],[92] Psammaplin A has gained recognition in the form of a non-competitive inhibitor of chitinase B from S. marcescens, which belongs to the family 18 chitinase and is a brominated tryrosine-derived compound. As suggested by crystallographic studies, a disordered Psammaplin A molecule binds in vicinity of the active site. [93] Argadin, which was isolated from Clonostachys sp. FO-7314, is another chitinase inhibitor. [94]

In order to carry out the cloning and expression of genes from diverse organisms into E. coli, several attempts have been made with S. plymuthica,[95] B. circulans WL-12. [54] ChiA, which is a chitinase gene from family 18, has been cloned from a thermophilic species Rhodothermus marinus and then expressed in E. coli. Hobel et al., 2005, [96] reported that the R. marinus chitinase is the most thermostable chitinase isolated from bacteria. Two chitinase genes of Bacillus, which encode ChiCW and ChiCH, have been cloned into pGEX-6P-1 and later expressed in E. coli in the form of soluble glutathione S-transferase chitinase fusion proteins. [97] Many Streptomyces and non-Streptomyces bacteria are renowned in chitin production and are antagonistic against Sclerotinia minor, the pathogen of the basal drop of lettuce. The two isolates; Streptomyces viridodiasticus and Micromonospora carbonacea have been recognised as high level chitinase producers and therefore, recognisably reduced the growth of S. minor in vitro and under controlled greenhouse conditions resulted in the reduced occurrence of disease. [98]

   Uses Top

Chitinases may be used to convert chitin-containing biomass into useful (depolymerized) components. Chitinases can be exploited for their use in control of fungal and insect pathogens of plants. [99],[100] Fungal protoplasts have been exploited as a very efficient experimental means to study the synthesis of cell wall, enzyme synthesis and secretion and strain improvement for biotechnological applications. [101] Chitinase activity also acts as an indicator showing the activity of fungi in soil. It has been reported that there is a strong association between chitinase activity and fungal population in the soil. Therefore, it appears that chitinases activity acts as a suitable indicator of the actively growing fungi in the soil. Miller et al., (1998) [102] by making use of specific methylumbelliferyl substrates reported the correlation of chitinase activity with the content of fungus-specific indicator molecules 18:2ωb phospholipid fatty acid and ergosterol.

   Medicinal Functions Top

Chitooligosaccharides have an enormous pharmaceutical potential. They are involved in the signaling for root nodule formation, act as elicitors of plant defense and also have a potential to be used in human medicines (e.g., anti-tumor activity is shown by chitohexaose and chitoheptaose). It was reported by Murao et al., 1999, [103] that chitotriose from colloidal chitin have been prepared using a chitinase from Vibrio alginolyticus. Kobayashi et al., 1997, [104] have reported the use of Bacillus chitinase for the production of chitobiose by combining GlcNAc and a sugar oxazoline derivative. GlcNAc itself is an anti-inflammatory drug, and in the human body, it is synthesized from glucose, then incorporated into glycoproteins and glycosaminoglycans. The GlcNAc administered by oral routes, intravenous (IV), and intramuscular (IM) has been reported to be effective as an anti-inflammatory drug, useful in the treatment of ulcerative colitis and other gastrointestinal inflammation disorders. [105] Horsch et al. (1997) [106] recommended that N-acetylhexosaminidase can be explored for its use as a target for designing antifungals with low molecular weight. According to Laine and Lo, (1996) [107] chitin and chitin binding proteins can be explored for the recognition of fungal infections in humans.

Chitinases have a significant function in human health care. An important medical use for chitinases has also been recommended in augmenting the activity of anti-fungal drugs in therapy for fungal diseases. [108] Due to their topical applications, they have a prospective use in anti-fungal creams and lotions. A number of artificial medical articles such as contact lenses, artificial skin, and surgical stitches have been formed from chitin derivatives. These derivatives have an extensive medical use because quite a few of these chitin derivatives are known to be non-toxic, non-allergic, biocompatible, and biodegradable. [109] Chitinases also have some other medical applications as well. For example, first discovery of the involvement of acidic mammalian chitinase (AMCase) in the pathogenesis of asthma was novel and unexpected because of the fact that mammals do not use chitin as an energy source, nor do they produce any chitinous structure. [110] Several lines of evidence have demonstrated the importance of chitinases as an effector of host defense in the mammalian immune system. For example, humans that are deficient in chitotriosidase show an increased rate of microfilarial infection due to suppressed chitinolytic activity, allowing the parasite to thrive within the host. Recombinant human chitotriosidase shows the inhibition of Candida albicans hyphae formation in vitro, thereby, showing anti-fungal activity, and reducing mortality in mouse models of neutropenic candidiasis and aspergillosis.

Zhu and co-workers, 1984, [110] reported the first clinically-significant finding related to the role of chitinase in asthma where exaggerated quantities of AMCase were detected in the epithelial cells and macrophages of lung biopsies taken from patients with asthma. Correspondingly, BAL fluid chitinase activity and the AMCase level have also been reported to be induced in the lungs of an ovalbumin-induced mouse asthma model. Moreover, it has been recently found that AMCase, serum, and lung tissue levels of a chitinase-like protein, YKL-40, are increased in patients with asthma. Furthermore, circulating YKL-40 levels correlated positively with thickening of the lung sub-epithelial basement membrane, incidence of use of rescue inhalers, asthma severity, and deterioration in pulmonary function in asthmatic subjects have been studied. [111]

Even though mammals cannot carry out the synthesis of chitin, some chitinolytic enzymes or true chitinases (-e.g., acidic mammalian chitinase AMCase and chitotriosidases, or chitinases like proteins (CLPs)) or CBPs (e.g., breast regression protein 39 (BRP-39, chondrocyte protein-39) and Ym-1, Ym-2) have been found in mammals. Mammalian chitinases do not have chitinase activity while AMCase and chitotriosidase have chitinase activity. [112] The enzymatic activity of mammalian chitinases is due to its chitin-binding domain, which consists of 6 cystein residues having chitin binding property. [113] On the contrary, no such typical chitin-binding domain is present in CLPs, but still they show a very high chitin-binding affinity. [114] CHI3L1 does not have chitinase activity because of substitution of an essential glutamic acid residue to leucine, [115] but it has a high affinity for chitooligosaccharides and chitin, which is due to conserved substrate binding cleft. [116] It has also been suggested that YKL-40/BRP-39 has a major role as an active pathogenic mediator in acute colitis during the generation of intestinal bowel disease (IBD). YKL-40 is supposed to play a role in tissue remodeling and inflammation and can bind to chitin, type I collagen, hyaluronan, and heparin even though it lacks chitinolytic activity. [117] Consisting of the body's first line of defense against external agents, which also includes chitin-containing pathogens, various chitinase family proteins have constitutively shown their expression in macrophages, digestive tract, and in epithelial cells of lungs. [110],[117] It has been reported that lungs show an increased expression of AMCases in the development of Th2 inflammation in the human asthmatic airway and in allergic animal models as well. [110] It has also been shown that AMCases have a very important role to play in the IL-13 effector pathway activation and in the pathogenesis of Th2 inflammation. It has been suggested from studies of cancer, arthritis, and liver fibrosis that chitinase 3-like protein 1 (CHI3L1) also has an important role in tissue remodeling and inflammation. [115],[118]

The chief components of solid waste from shellfish processing are CaCO 3 , chitin, and protein. Chitinase from S. marcescens was used by their group to hydrolyze the chitinous material and yeast, Pichia kudriavzevii, in order to produce SCP that was acceptable as aquaculture. Hensenula polymorpha, Candida tropicalis, S. cerevisiae, and M. verrucaria have been commonly used for the production of SCP. The chitinase from M. verrucaria and S. cerevisiae have been used to produce SCP from chitinous waste by Wang and Hwang, 2001. [119] These authors have also reported that M. verrucaria chitinase preparation could be used for chitin hydrolysis, and S. cerevisiae chitinase preparation for SCP. Chitinases find their use in other fields like agriculture and mosquito control. Chitinases can also be exploited as additives in order to supplement to the frequently used insecticides and fungicides so that they can be more potent and at the same time, the concentration of the chemically synthesised active agents in the ingredients can be minimised, which are otherwise harmful to health and environment. [120],[121] Chitinases also have applications in the bioconversion of chitin waste to fertiliser. [122] The utilization of microorganisms as biological control agents or their secretions to prevent plant pathogens and insect pests provides us with a striking choice in order to control the plant diseases. Therefore, biological control strategy has become a vital advance in order to make sustainable agriculture possible. [123] The organisms which produce chitinase could also be exploited for their use as biocontrol agents either directly or indirectly by making use of their purified proteins or via gene manipulation. [124]

   Future Prospects Top

In the future, there is a possibility of generating chitinases with novel functions. Chitinases can be exploited for their use as food preservatives, thereby increasing the shelf life of the foods. A vast understanding of the biological roles of different chitinases would help us to develop novel therapeutic approaches for several diseases including asthma, and chronic rhinosinusitis. There is a possibility of using chitinases as anti-tumor drugs since chitohexaose and chitoheptaose has shown an anti-tumor activity. These enzymes can be used for the enhancement of human the immune system. This research can be directed towards the identification of the active sites of chitinases and the novel functions associated with them. We can exploit protein engineering for the production of chitinases with exclusive functions.

   Acknowledgement Top

Saleem Javed is thankful to Department of Science and Technology (DST), India for financial support. Rifat Hamid and Mahboob Ahmad are thankful to UGC for fellowship.

   References Top

1.Shahidi F, Abozaytoun R. Chitin, chitosan and co-products: Chemistry, production, applications and health effects. Adv Food Nutr Res 2005;49:93-135.  Back to cited text no. 1
2.Bhattachrya D, Nagpure A, Gupta RK. Bacterial chitinase: Properties and potential. Crit Rev Biotechnol 2007;27:21-8.  Back to cited text no. 2
3.Wang SL, Chang WT. Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. Appl Environ Microbiol 1997;63:380-6.  Back to cited text no. 3
4.Muzzarelli RA. Clinical and biochemical evaluation of chitosan for hypercholesterolemia and overweight control. EXS 1999;87:293-304.  Back to cited text no. 4
5.Zikakis JP, editor. Chitin, Chitosan, and Related Enzymes. Academic Press Inc., Orlando, New York. 1984, P. XVII.  Back to cited text no. 5
6.Muzzarelli RA. Natural Chelating Polymers, per gives it the ability to bond chemically with negatively charged lipids, fats and bile acids. New York: The gamon Press; 1997. p. 83.  Back to cited text no. 6
7.Bussink AP, Speijer D, Aerts JM, Boot RG. Evolution of mammalian chitinase (-like) members of family 18 glycosyl hydrolases. Genetics 2007;177:959-70.  Back to cited text no. 7
8.Chen JK, Shen CR, Liu CL. N-acetylglucosamine: Production and applications. Mar Drugs 2010; 8:2493-516.  Back to cited text no. 8
9.Suginta W, Robertson PA, Austin B, Fry SC, Fothergill-Gillmore LA. Chitinases from vibrio: Activity screening and purification of chiA from V. carchariae. J Appl Microbiol 2000;89:76-84.  Back to cited text no. 9
10.Yuli PE, Suhartono MT, Rukayadi Y, Hwang JK, Pyunb YR. Characteristics of thermostable chitinase enzymes from the Indonesian Bacillus sp.13.26. Enzyme Microb Technol 2004;35:147-53.  Back to cited text no. 10
11.Shiro M, Ueda M, Kawaguchi T, Arai M. Cloning of a cluster of chitinase genes from Aeromonas sp. no. 10S-24. Biochim Biophys Acta 1996;1305:44-8.  Back to cited text no. 11
12.Mathivanan N, Kabilan V, Murugesan K. Purification, characterization and antifungal activity of chitinase from Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis. Can J Microbiol 1998;44:646-51.  Back to cited text no. 12
13.Mendonsa ES, Vartak PH, Rao JU, Deshpande MV. An enzyme from Myrothecium verrucaria that degrades insect cuticles for biocontrol of Aedes aegypti mosquito. Biotechnol Lett 1996;18:373-6.  Back to cited text no. 13
14.Shahabudin M, Vinetz JM. Chitinases of human parasites and their implications as antiparasitic targets. In: Jolles P, Muzzarelli RA, editors. Chitin and Chitinases. Switzerland: Birkhauser Verlag Basel; 1999. p. 223-8.  Back to cited text no. 14
15.Blaak H, Schrempf H. Binding and substrate specificities of a Streptomyces olivaceovirldis chitinase in comparison with its proteolytically processed form. Eur J Biochem 1995;229:132-9.  Back to cited text no. 15
16.Tsujibo II, Orikoshi II, Tanno H, Fujimoto K, MIyamoto IL, Imada C, et al. Cloning, sequence and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J Bacteriol 1993;175:176-81.  Back to cited text no. 16
17.West PA, Colwell RR. Identification and classification of Vibrionaceae: An overiew. In: Colweii RR, editors. Vibrios in the environment. New York: John Wiley and Sons, Inc.; 1984. p. 285-363.  Back to cited text no. 17
18.Sitrit Y, Vorgias CE, Chet I, Oppenheim AB. Cloning and primary structure of Chia gene from Aeromonas caviae. J Bacteriol 1995;177:4187-9.  Back to cited text no. 18
19.Sahai AS, Manocha MS. Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction. FEMS Microbiol Rev 1993;11:317-38.  Back to cited text no. 19
20.Harman GE, Hayes CK, Lorito M, Broadway RM, Di Pietro A, Peterbauer C, et al. Chitinolytic enzymes of Trichoderma harzianum: Purification of chitobiosidase and endochitinase. Phytopathol 1993;83:313-8.  Back to cited text no. 20
21.Frankowski J, Berg G, Bahl H. Purification and properties of two chitinolytic enzymes of the biocontrol agent Serratia plymuthica HRO C48. Arch Microbiol 2001;176:421-6.  Back to cited text no. 21
22.Kamensky M, Ovadis M, Chet I, Chernin L. Soil-borne strain IC14 of Serratia plymuthica with multiple mechanisms of antifungal activity provides biocontrol of Botrytis cinerea and Sclerotinia sclerotiorum diseases. Soil Biol Biochem 2003;35:323-31.  Back to cited text no. 22
23.Henrissat B, Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1993;293:781-8.  Back to cited text no. 23
24.Patil RS, Ghormade V, Deshpande MV. Chitinolytic enzymes: An exploration. Enzyme Microb Technol 2000;26:473-83.  Back to cited text no. 24
25.Kasprzewska A. Plant chitinases-regulation and function-a review. Cell Mol Bio Lett 2003;8:809-24.  Back to cited text no. 25
26.Matsumiya M, Kasasuda S, Miyauchi K, Mochizuki A. Substrate specificity and partial amino acid sequence of a Chitinase from the stomach of coelacanth Latimeria chalumnae. Fish Sci 2008;74:1360-2.  Back to cited text no. 26
27.Brunner F, Stintzi A, Fritig B, Legrand M. Substrate specificities of tobacco chitinases. Plant J 1998;14:225-34.  Back to cited text no. 27
28.Iseli B, Armand S, Boller T, Neuhaus JM, Henrissat B. Plant chitinases use two different hydrolytic mechanisms. FEBS Lett 1996;382:186-8.  Back to cited text no. 28
29.Sasaki C, Itoh Y, Takehara H, Kuhara S, Fukamizo T. Family 19 chitinase from rice (Oryza sativa L.): Substrate-binding subsites demonstrated by kinetic and molecular modeling studies. Plant Mol Biol 2003;52:43-52.  Back to cited text no. 29
30.Sasaki C, Vårum KM, Itoh Y, Tamoi M, Fukamizo T. Rice chitinases: Sugar recognition specificities of the individual subsites. Glycobiology 2006;16:1242-50.  Back to cited text no. 30
31.Gooday GW. Aggressive and defensive roles of chitinases. EXS 1999;87:157-69.  Back to cited text no. 31
32.Andres E, Boer H, Koivula A, Samain E, Driguez H, Armand S, Cottaz S. Engineering chitinases for the synthesis of chitin oligosaccharides: catalytic amino acid mutations convert the GHfamily 18 glycoside hydrolases into transglycosylases. J Mol Cat B: Enzym 2012;74:89-96.  Back to cited text no. 32
33.Tellam RL. Protein motifs in filarial chitinases: An alternative view. Parasitol Today 1996;12:291-2.  Back to cited text no. 33
34.Alam MM, Nikaidou N, Tanaka H, Watanabe T. Cloning and sequencing of chiC gene of Bacillus circulans WL-12 and relationship of its product to some other chitinases and chitinase-like proteins. J Ferment Bioeng 1995;80:454-61.  Back to cited text no. 34
35.Graham LS, Sticklen MS. Plant chitinases. Can J Bot 1994;721057-83.  Back to cited text no. 35
36.Poole DM, Hazelwood GP, Huskisson NS, Virden R, Gilbert H. The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand. FEMS Microbiol Lett 1993;106:77-84.  Back to cited text no. 36
37.Schnellmann J, Zeltins A, Blaak H, Schrempf H. The novel lectinlike protein CHBl is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline a-chitin of fungi and other organisms. Mol Microbiol 1994;13:807-19.  Back to cited text no. 37
38.Watanabe T, Kimura K, Sumiya T, Nikaidou N, Suzuki K, Suzuki M, et al. Genetic analysis of the chitinase system of Serratia marcescens 2170. J Bactriol 1997;179:7111-7.  Back to cited text no. 38
39.Venegas A, Goldstein JC, Beauregard K, Oles A, Abdulhayoglu N, Fuhrman JA. Expression of recombinant microfilarial chitinase and analysis of domain function. Mol Biochem Parasitol 1996;78:149-59.  Back to cited text no. 39
40.Watanabe T. Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J Bacteriol 1994;176:4465-72.  Back to cited text no. 40
41.Ohno T, Armand S, Hata T, Nikaidou N, Henrissat B, Mitsutomi M, et al. A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 603Z. J Bacteriol 1996;178:5065-70.  Back to cited text no. 41
42.Suzuki K, Sugawara N, Suzuki M, Uchiyama T, Katouno F, Nikaidou N, et al. Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: Enzymatic properties and synergism on chitin degradation. Biosci Biotechnol Biochem 2002;66:1075-83.  Back to cited text no. 42
43.Shekhar N, Bhattacharya D, Kumar D, Gupta RK. Biocontrol of wood- rotting fungi using Streptomyces violaceusniger XL-2. Can J Microbiol 2006; 52:805-8.  Back to cited text no. 43
44.Cohen-Kupiec R, Chet I. The molecular biology of chitin digestion. Curr Opin Biotechnol 1998;9:270-7.  Back to cited text no. 44
45.Chernin LS, De la Fuente L, Sobolev V. Molecular cloning structural analysis and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl Environ Microbiol 1997;63:834-9.  Back to cited text no. 45
46.Downing KJ, Thomson JA. Introduction of the Serratia marcescens chiA gene into an endophytic Pseudomonas fluorescens for the biocontrol of phytopathogenic fungi. Can J Microbiol 2000;46:363-9.  Back to cited text no. 46
47.Dempsey DA, Silva H, Klessig DF. Engineering disease and pest resistance in plants. Trends Microbiol 1998;6:54-61.  Back to cited text no. 47
48.Ordentlich A, Elad Y, Chet I. The role of chitinase of Serratia marcescens in biological control of Sclerotium rolfsii. Phytopathol 1988;78:84-8.  Back to cited text no. 48
49.Svitil AL, Kirchman DL. A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: Implications for the ecology and evolution of 1,4-beta-glycanases. Microbiology 1998;144:1299-308.  Back to cited text no. 49
50.Metcalfe AC, Krsek M, Gooday GW, Prosser JI, Wellington EM. Molecular analysis of a bacterial chitinolytic community in an upland pasture. Appl Environ Microbiol 2002;68:5042-50.  Back to cited text no. 50
51.Morimoto, K.S., Karita, T., Kimura, T., Sakka, K., Ohmiya, K., 1997. Cloning, sequencing, and expression of the gene encoding Clostridium paraprtrificum chitinase chiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol., 179(23):7306-7314  Back to cited text no. 51
52.Watanabe T, Kanai R, Kawase T, Tanabe T, Mitsutomi M, Sakuda M, et al. Family 19 chitinases of Streptomyces species: Characterization and distribution. Microbiology 1999;145:3353-63.  Back to cited text no. 52
53.Ueda M, Fujiwara A, Kawaguchi T, Arai M. Purification and some properties of six chitinases from Aeromonas sp. No. 10S-24. Biosci Biotechnol Biochem 1995;59:2162-4.  Back to cited text no. 53
54.Mitsutomi O, Isono M, Uchiyama A, Nikaidov N, Ikegami T, Watanabe T. Chitosanase activity of the enzyme previously reported as â-1,3-1,4-glucanase from Bacillus circulans WL 12. Biosci Biotechnol Biochem 1998;62:2107-14.  Back to cited text no. 54
55.Hayes CK, Klemsdal S, Lorito M, Di PA, Peterbauer C, Nakas JP, et al. Isolation and sequence of an endochitinase-encoding gene from a cDNA libray of Trichoderma harzianum. Gene 1994;138:143-8.  Back to cited text no. 55
56.Henrissat B. Classification of chitinase modules. In: Jolles P, Muzzarelli RA, editors. Chitin and Chitinases, Burkhauser Basel Switzerland, 1999. p. 137-56.  Back to cited text no. 56
57.Takaya N, Yamazaki D, Horiuchi H, Ohta A, Takagi M. Cloning and characterization of a chitinase-encoding gene (ChiA) from Aspergillus nidulans, disruption of that decreases germination frequency and hyphal growth. Biosci Biotechnol Biochem 1998a;62:60-5.  Back to cited text no. 57
58.Shimono K, Matsuda H, Kawamukai M. Functional expression of chitinase and chitosanase, and their effects on morphologies in the yeast Schizosaccharomyces pombe. Biosci Biotechnol Biochem 2002;66:1143-7.  Back to cited text no. 58
59.Lorito M, Hayes CK, Di Pietro A, Woo SL, Harman GE. Purification, characterization and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetylglucosaminidase from T. harzianum. Phytopathology 1994;84:398-405.  Back to cited text no. 59
60.Ulhoa CJ, Peberdy JF. Purification and characterization of an extracellular chitobiase from T. harzianum. Curr Microbiol 1991;23:285-9.  Back to cited text no. 60
61.Draborg H, Kauppinen S, Dalboge H, Christgau S. Molecular cloning and expression in S. cerevisiae of two exochitinases from T. harzianum. Biochem Molec Biol Int 1995;36:781-91.  Back to cited text no. 61
62.Peterbauer CK, Lorito M, Hayes CK, Harman GE, Kubicek CP. Molecular cloning and expression of the nag1 gene (N-acetylbeta-D-glucosaminidase-encod ing gene) from Trichoderma harzianum P1. Curr Genet 1996;30:325-31.  Back to cited text no. 62
63.Lorito M, Woo SL, Fernandez IG, Colucci G, Harman GE, Pintor-Toro JA, et al. Genes from mycoparisitic fungi as a source for improving resistance to fungal pathogens P. Natl Acad Sci USA 1998;95:7860-5.  Back to cited text no. 63
64.Yamanaka S, Tsuyoshi N, Kikuchi R, Takayama S, Sakuda S, Yamada Y. Effect of demethylallosamidin, a chitinase inhibitor, on morphology of fungus Geotrichum candidum. J Gen Appl Microbiol 1994;40:171-4.  Back to cited text no. 64
65.Sandor E, Pusztahelyi T, Karaffa L, Karanyi Z, Pocsi I, Biro S, et al. Allosamidin inhibits the fragmentation of Acremonium chrysogenum but does not influence the cephalosporin-C production of the fungus. FEMS Microbiol Lett 1998;164:231-6.  Back to cited text no. 65
66.Chérif M, Benhamou N. Cytochemical aspects of chitin breakdown during the parasitic action of a Trichoderma sp. on Fusarium oxysporum f. sp. radicis-lycopersici. Phytopathol 1990;80:1406-14.  Back to cited text no. 66
67.Chet I. Trichoderma- Application, mode of action, and potential as a biocontrol agent of soilborne plant pathogenic fungi. In: Chet I, editors. Innovative Approaches to Plant Disease Control. New York: John Wiley and Sons; 1987. p. 137-60.  Back to cited text no. 67
68.Lorito M, Harman GE, Hayes CK, Broadway RM, Tronsmo A, Woo SL, et al. Chitinolytic enzymes produced by Trichoderma harzianum: Antifungal activity of purified endochitinase and chitobiosidase. Phytopathology 1993;83:302-7.  Back to cited text no. 68
69.Haran S, Schickler H, Oppenheim A, Chet I. Differential expression of Trichoderma harzianum chitinases during mycoparasitism. Phytopathology 1996;86:980-5.  Back to cited text no. 69
70.Madi L, Katan T, Katan J, Henis Y. Biological control of Sclerotium rolfsii and Verticillium dahliae by Talaromyces flavus is mediated by different mechanisms. Phytopathology 1997;87:1054-60.  Back to cited text no. 70
71.Harman GE. Myths and dogmas of biocontrol. Plant Dis 2000;84:377-91.  Back to cited text no. 71
72.Yedidia I, Benhamou N, Kapulnik Y, Chet I. Induction and accumulation of PR proteins activity during early stages of root colonization by the mycoparasite T. harzianum strain T-203. Plant Physiol Biochem 2000;38:863-73.  Back to cited text no. 72
73.Yuan WM, Crawford DL. Characterization of Streptomyces lydicus WYEC108 as a potential biocontrol agent against fungal root and seed rots. Appl Environ Microbiol 1995;61:3119-28.  Back to cited text no. 73
74.Seidl V, Huemer B, Seiboth B, Kubicek CP. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J 2005;272:5923-39.  Back to cited text no. 74
75.Zeilinger S, Galhaup C, Payer K, Woo SL, Mach RL, Fekete C, et al. Chitinase gene expression during mycoparasitic interaction of Trichoderma harzianum with its host. Fungal Genet Biol 1999;26:131-40.  Back to cited text no. 75
76.Woo SL, Donzelli B, Scala F, Mach RL, Harman GE, Kubicek CP, et al. Disruption of ech42 (endochitinase-encoding) gene affects biocontrol activity in Trichoderma harzianum strain P1. Mol Plant Microbe Interact. 1998;12:419-29.  Back to cited text no. 76
77.Viterbo A, Haran S, Friesem D, Ramot O, Chet I. Antifungal activity of a novel endochitinase gene (chit36) from T. harzianum Rifai TM. FEMS Microbiol Lett 2001;200:169-74.  Back to cited text no. 77
78.Fukamizo T, Sakai C, Tamoi M. Plant Chitinases: Structure-function relationships and their physiology. Foods Food Ingredients J Jpn 2003;208:631-2.  Back to cited text no. 78
79.Gooday GW. Aggresive and Defensive Roles for Chitinases. In: Muzzarelli, RA, editors. Chitin Enzymology. Italia: Atec Edizioni; 1996. p. 125-133.  Back to cited text no. 79
80.Garg N, Gupta H. Isolation and purification of fungal pathogen (Macrophomina Phaseolina) induced chitinase from moth beans (Phaseolus aconitifolius). J Pharm Bioall Sci 2010;2:38-43.  Back to cited text no. 80
[PUBMED]  Medknow Journal  
81.Gupta R, Saxena R, Chaturvedi P, Virdi J. Chitinase production by Streptomyces viridificans: Its potential in fungal cell wall lysis. J Appl Bacteriol 1995;78:378-83.  Back to cited text no. 81
82.Koga D, Sasaki Y, Uchiumi Y, Hirai N, Arakane Y, Nagamatsu Y. Purification and Characterization of Bombyx mori Chitinases. Insect Biochem Mol Biol 1997;27:757-67.  Back to cited text no. 82
83.Bussink AP, van Eijk M, Renkema GH, Aerts JM, Boot RG. The biology of the Gaucher cell: The cradle of human chitinases. Int Rev Cytol 2006;252:71-128.  Back to cited text no. 83
84.Chou YT, Yao S, Czerwinski R, Fleming M, Krykbaev R, Xuan D, et al. Kinetic characterization of recombinant human acidic mammalian chitinase. Biochemistry 2006;45:4444-54.  Back to cited text no. 84
85.Webb DC, McKenzie AN, Foster PS. Expression of the Ym2 lectinbinding protein is dependent on interleukin (IL)-4 and IL-13 signal transduction: Identification of a novel allergy-associated protein. J Biol Chem 2001;276:41969-76.  Back to cited text no. 85
86.Khan MA, Hamid R, Ahmad M, Abdin MZ, Javed S. Optimization of culture media for enhanced chitinase production from a novel strain of Stenotrophomonas maltophilia using response surface methodology. J Microbiol Biotechnol 2010; 20:597-1602.  Back to cited text no. 86
87.Bhushan B. Isolation, purification, characterization and scale up production of a thermostable chitinase from an alkalophilic microorganism. Ph.D. thesis, Department of Microbiology 1998. Punjab University, Chandigarh.  Back to cited text no. 87
88.Dahiya N, Tewari R, Tiwari RP, Hoondal GS. Chitinase production in solid state fermentation by Enterobacter sp. NRG4 using statistical experimental design. Curr Microbiol 2005b;51:222-8.  Back to cited text no. 88
89.Miyashita K, Fujii T, Sawada Y. Molecular cloning and characterization of chitinase gene from Streptomyces lividans 66. J Microbiol 1991;137:2065-72.  Back to cited text no. 89
90.Chen JP, Lee MS. Enhanced production of Serratia marcescens chitinase in PEG/dextran aqueous two-phase system. Enzyme Microb Technol 1995;17:1021-7.  Back to cited text no. 90
91.Sakuda S. Studies on the chitinase inhibitors, allosamidins. In: Muzzarelli RA, editor. Chitin Enzymology. Eur. Chitin Soc, Grottammare. 1996; p. 203-12.  Back to cited text no. 91
92.Tews I, Scheltinga AC, Terwisscha V, Perrakis A, Wilson KS, Dijkstra BW. Substrate assisted catalysis unifies two families of chitinolytic enzymes. J Am Chem Soc 1997;119:7954-9.  Back to cited text no. 92
93.Tabudravu JN, Eijsink VA, Gooday GW, Jaspar M, Komander D, Legg M, et al. Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax. Bioorg Med Chem 2002;10:1123-8.  Back to cited text no. 93
94.Arai N, Shiomi K, Yamaguchi Y, Masuma R, Iwai Y, Turberg A, et al. Argadin, a new chitinase inhibitor, produced by Clonostachy sp. FO. 7314. Chem Pharm Bull 2000;48:1442-6.  Back to cited text no. 94
95.Ovadis M Liu XG, Gavriel S, Ismailov Z, Chet I, Chernin L. The global regulator genes from biocontrol strain Serratia plymuthica IC1270: Cloning, sequencing, and functional studies. J Bacteriol 2004;186:4986-93.  Back to cited text no. 95
96.Hobel CF, Hreggvidsson GO, Marteinsson VT, Bahrani-Mougeot F, Einarsson JM, Kristjansson JK. Cloning, expression and characterization of a highly thermostable family 18 chitinase from Rhodothermus marinus. Extremophiles 2005;9:53-64.  Back to cited text no. 96
97.Huang CJ, Chen CY. High level expression and characterization of two chitinases ChiCH and ChiCW of Bacillus cereus 28-9 in Escherichia coli. Biochem Biophys Res Commun 2005;327:8-17.  Back to cited text no. 97
98.El-Tarabily KA, Soliman M, Nassar A, Al-Hassani H, Sivasithamparam K, McKenna F, et al. Biological control of sclerotinia minor using a chitinolytic bacterium and actinomycetes. Plant Pathol 2000;49:573-83.  Back to cited text no. 98
99.Melchers LS, Stuiver MH. Novel genes for disease-resistance breeding. Curr Opin Plant Biol 2000;3:147-52.  Back to cited text no. 99
100.Roberts WK, Selitrennikoff CP. Plant and bacterial chitinases differ in antifungal activity. J Gen Microbiol 1988;134:169-76.  Back to cited text no. 100
101.Dahiya N, Tewari R, Tiwari RP, Hoondal GS. Production of an antifungal chitinase from Enterobacter sp. NRG4 and its application in protoplast production. World J Microbiol Biotechnol 2005a;21:1611-6.  Back to cited text no. 101
102.Miller M, Palojarvi A, Rangger A, Reeslev M, Kjoller A. The use of fluorogeic substrates to measure fungal presence and activity in soil. Appl Environ Microbiol 1998;64:613-7.  Back to cited text no. 102
103.Murao S, Kawada T, Itoh H, Oyama, H, Shin T. Purification and characterization of a novel type of chitinase from Vibrio alginolyticus. Biosci Biotech Biochem 1992;56:368-9.  Back to cited text no. 103
104.Kobayashi S, Kiyosada T, Shoda SI. A novel method for synthesis of chitobiose via enzymatic glycosylation using a sugar oxazoline as glycosyl donor. Tetrahedron Lett 1997;38:2111-2.  Back to cited text no. 104
105.Aloise PA, Lumme M, Haynes CA. N-Acetyl-D-glucosamine production from chitin-waste using chitinases from Serratia marcescens. In: Muzzarelli, RAA, editors. Chitin Enzymology. Grottammare: Eur. Chitin Soc; 1996. p. 581-94.  Back to cited text no. 105
106.Horsch M, Mayer C, Sennhauser U, Rast DM. β-N- acetylhexosaminidase: A target for the design of antifungal agents. Pharmacol Ther 1997;76:187-218.  Back to cited text no. 106
107.Laine LA, Lo CJ. Diagnosis of fungal infections with a chitinase. 1996 US patent 5587292.  Back to cited text no. 107
108.Orunsi NA, Trinci AP. Growth of bacteria on chitin, fungal cell walls and fungal biomass, and the effect of extracellular enzymes produced by these cultures on the antifungal activity of amphotericin B. Microbios 1985;43:17-30.  Back to cited text no. 108
109.Muzzarelli RA. Human enzymatic activities related to the therapeutical administration of chitin derivatives. Cell Mol Life Sci 1997;53:131-40.  Back to cited text no. 109
110.Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, et al. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science 2004;304:1678-82.  Back to cited text no. 110
111.Chupp GL, Lee CG, Jarjour N, Shim YM, Holm CT, He S, et al. A chitinase-like protein in the lung and circulation of patients with severe asthma. N Engl J Med 2007;357:2016-27.Chang NC, Hung SI, Hwa KY, Kato I, Chen JE, Liu CH, et al. A macrophage protein, Ym1, transiently expressed during inflammation is a novel mammalian lectin. J Biol Chem 2001;276:17497-506.  Back to cited text no. 111
112.Chang NC, Hung SI, Hwa KY, Kato I, Chen JE, Liu CH, Chang AC. A macrophage protein, Ym1, transiently expressed during in­flammation is a novel mammalian lectin. J Biol Chem 2001;276:17497-506.  Back to cited text no. 112
113.Tjoelker LW, Gosting L, Frey S, Hunter CL, Trong HL, Steiner B, et al. Structural and functional definition of the human chitinase chitin- binding domain. J Biol Chem 2000;275:514-20.  Back to cited text no. 113
114.Kzhyshkowska J, Mamidi S, Gratchev A, Kremmer E, Schmuttermaier C, Krusell L, et al. Novel stabilin-1 interacting chitinase-like protein (SICLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway. Blood 2006;107:3221-8.  Back to cited text no. 114
115.Hakala BE, White C, Recklies AD. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J Biol Chem 1993;268:25803-10.  Back to cited text no. 115
116.Renkema GH, Boot RG, Au FL, Donker-Koopman WE, Strijland A, Muijsers AO, et al. Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Eur J Biochem 1998;251:504-9.  Back to cited text no. 116
117.Kawada M, Hachiya Y, Arihiro A, Mizoguchi E. Role of mammalian chitinases in inflammatory conditions. Keio J Med 2007;56:21-7.  Back to cited text no. 117
118.Volck B, Price PA, Johansen JS, Sorensen O, Benfield TL, Nielsen HJ, et al. YKL-40, a mammalian member of the chitinase family, is a matrix protein of specific granules in human neutrophils. Proc Assoc Am Physicians 1998;110:351-60.  Back to cited text no. 118
119.Wang S, Hwang J. Microbial reclamation of shellfish wastes for the production of chitinases. Enzyme Microb Technol 2001;28:376-82.  Back to cited text no. 119
120.Giambattista RD, Federici F, Petruccioli M, Fence M. The chitinolytic activity of Penicillium janthinellum P9: Purification, partial characterization and potential application. J Appl Microbiol 2001;91:498-505.  Back to cited text no. 120
121.Govindsamy V, Gunaratna KR, Balasubramanian R. Properties of extracellular chitinase from Myrothecium verrucaria, an antagonist to the groundnut rust Puccinia arachidis. Can J Plant Pathol 1998;20:62-8.  Back to cited text no. 121
122.Sakai K, Yakota A, Kurokawa H, Wakayama M, Moriguchi M. Purification and characterization of three thermostable endochitinases of Bacillus noble strain MH-1 isolated from chitin containing compost. Appl Environ Microbiol 1998;64:3340-97.  Back to cited text no. 122
123.Wang SL, Yen YH, Tsiao WJ, Chang WT, Wang CL. Production of antimicrobial compounds by Monascus purpureus CCRC31499 using shrimp and crab shell powder as a carbon source. Enzyme Microb Technol 2002;31:337-44.  Back to cited text no. 123
124.Singh P, Shin Y, Park C, Chung Y. Biological control of Fusarium wilt of cucumber by chitinolytic bacteria. Phytopathology 1999;89:92-9.  Back to cited text no. 124

This article has been cited by
1 Antifungal Activity of Partially Purified Bacterial Chitinase Against Alternaria alternata
Neslihan Dikbas, Sevda Uçar, Elif Tozlu, Merve Senol Kotan, Recep Kotan
Erwerbs-Obstbau. 2022;
[Pubmed] | [DOI]
2 Bacterial chitinases: genetics, engineering and applications
Murugan Kumar, Hillol Chakdar, Kuppusamy Pandiyan, Shobit Thapa, Mohammad Shahid, Arjun Singh, Alok Kumar Srivastava, Anil Kumar Saxena
World Journal of Microbiology and Biotechnology. 2022; 38(12)
[Pubmed] | [DOI]
3 Morphological and structural characterization of chitin as a substrate for the screening, production, and molecular characterization of chitinase by Bacillus velezensis
Digvijay Dahiya, Akhil Pilli, Pratap Raja Reddy Chirra, Vinay Sreeramula, Nitish Venkateswarlu Mogili, Seenivasan Ayothiraman
Environmental Science and Pollution Research. 2022;
[Pubmed] | [DOI]
4 Increased production of chitinase by a Paenibacillus illinoisensis isolated from Brazilian coastal soil when immobilized in alginate beads
Francenya Kelley Lopes da Silva, Artur Ribeiro de Sa Alexandre, Ariadine Amorim Casas, Maycon Carvalho Ribeiro, Keili Maria Cardoso de Souza, Enio Saraiva Soares, Samuel Rodrigues Dos Santos Junior, Jose Daniel Gonçalves Vieira, Andre Correa Amaral
Folia Microbiologica. 2022;
[Pubmed] | [DOI]
5 Over-expression of PR proteins with chitinase activity in transgenic plants for alleviation of fungal pathogenesis
Rekha Chouhan, Sajad Ahmed, Sumit G. Gandhi
Journal of Plant Pathology. 2022;
[Pubmed] | [DOI]
6 Delineation of mechanistic approaches of rhizosphere microorganisms facilitated plant health and resilience under challenging conditions
Ajinath Dukare, Priyank Mhatre, Hemant S. Maheshwari, Samadhan Bagul, B. S. Manjunatha, Yogesh Khade, Umesh Kamble
3 Biotech. 2022; 12(3)
[Pubmed] | [DOI]
7 Impact of twenty pesticides on soil carbon microbial functions and community composition
Jowenna X.F. Sim, Barbara Drigo, Casey L. Doolette, Sotirios Vasileiadis, Dimitrios G. Karpouzas, Enzo Lombi
Chemosphere. 2022; 307: 135820
[Pubmed] | [DOI]
8 Myco-chitinases as versatile biocatalysts for translation of coastal residual resources to eco-competent chito-bioactives
Meenakshi Rajput, Manish Kumar, Nidhi Pareek
Fungal Biology Reviews. 2022;
[Pubmed] | [DOI]
9 Band gap tuning by Gd and Fe doping of LaNiO3 to boost solar light harvesting for photocatalytic application: A mechanistic approach
Shahid Iqbal, Ismat Bibi, Farzana Majid, Shagufta Kamal, Norah Alwadai, Munawar Iqbal
Optical Materials. 2022; 124: 111962
[Pubmed] | [DOI]
10 A synthesis of functional contributions of rhizobacteria to growth promotion in diverse crops
Silvina Brambilla, Margarita Stritzler, Gabriela Soto, Nicolas Ayub
Rhizosphere. 2022; 24: 100611
[Pubmed] | [DOI]
11 The potential of plant proteins as antifungal agents for agricultural applications
Tiffany Chiu, Theo Poucet, Yanran Li
Synthetic and Systems Biotechnology. 2022; 7(4): 1075
[Pubmed] | [DOI]
12 Characterization and biocontrol potential of Trichoderma longibrachiatum TL-RD-01 against plant pathogens
Priya R, Balachandar S, Murugesan N V, Prabhakaran N, RadheshKrishnan S, Latha K
Archives of Phytopathology and Plant Protection. 2022; : 1
[Pubmed] | [DOI]
13 A marine chitinase from Bacillus aryabhattai with antifungal activity and broad specificity toward crystalline chitin degradation
Arun Kumar Subramani, Ritu Raval, Subramaniam Sundareshan, Rashmi Sivasengh, Keyur Raval
Preparative Biochemistry & Biotechnology. 2022; : 1
[Pubmed] | [DOI]
14 Characterization of Chitinolytic and Antifungal Activities in Marine-Derived Trichoderma bissettii Strains
Dawoon Chung, Yong Min Kwon, Ji Yeon Lim, Seung Sub Bae, Grace Choi, Dae-Sung Lee
Mycobiology. 2022; : 1
[Pubmed] | [DOI]
15 Overexpression of 42 kDa chitinase genes from Trichoderma asperellum SH16 in peanut (Arachis hypogaea)
Phung Thi Bich Hoa, Nguyen Hoang Tue, Le Thi Thu Huyen, Luc Hoang Linh, Nguyen Thanh Nhan, Nguyen Quang Duc Tien, Nguyen Ngoc Luong, Nguyen Xuan Huy, Nguyen Hoang Loc
Journal of Crop Improvement. 2022; : 1
[Pubmed] | [DOI]
16 Computational identification and characterization of vascular wilt pathogen (Fusarium oxysporum f. sp. lycopersici) CAZymes in tomato xylem sap
Abhijeet Roy, Barsha Kalita, Aiswarya Jayaprakash, Amrendra Kumar, P. T. V. Lakshmi
Journal of Biomolecular Structure and Dynamics. 2022; : 1
[Pubmed] | [DOI]
17 Conserved molecular pathways underlying biting in two divergent mosquito genera
Alden Siperstein, Sarah Marzec, Megan L. Fritz, Christina M. Holzapfel, William E. Bradshaw, Peter A. Armbruster, Megan E. Meuti
Evolutionary Applications. 2022;
[Pubmed] | [DOI]
18 Comparative transcriptomic responses of European and Japanese larches to infection by Phytophthora ramorum
Heather F. Dun, Tin Hang Hung, Sarah Green, John J. MacKay
BMC Plant Biology. 2022; 22(1)
[Pubmed] | [DOI]
19 Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein
Patel Nilpa, Kapadia Chintan, R. Z. Sayyed, Hesham El Enshasy, Hala El Adawi, Alaa Alhazmi, Atiah H. Almalki, Shafiul Haque, Rahul Datta
PLOS ONE. 2022; 17(4): e0265969
[Pubmed] | [DOI]
20 Salmonella enterica serovar Typhimurium chitinases modulate the intestinal glycome and promote small intestinal invasion
Jason R. Devlin, William Santus, Jorge Mendez, Wenjing Peng, Aiying Yu, Junyao Wang, Xiomarie Alejandro-Navarreto, Kaitlyn Kiernan, Manmeet Singh, Peilin Jiang, Yehia Mechref, Judith Behnsen, Andreas J. Baumler
PLOS Pathogens. 2022; 18(4): e1010167
[Pubmed] | [DOI]
21 Genome-wide characterization of the chitinase gene family in wild apple (Malus sieversii) and domesticated apple (Malus domestica) reveals its role in resistance to Valsa mali
Yakupjan Haxim, Gulnaz Kahar, Xuechun Zhang, Yu Si, Abdul Waheed, Xiaojie Liu, Xuejing Wen, Xiaoshuang Li, Daoyuan Zhang
Frontiers in Plant Science. 2022; 13
[Pubmed] | [DOI]
22 Biochemical Analyses of Ten Cyanobacterial and Microalgal Strains Isolated from Egyptian Habitats, and Screening for Their Potential against Some Selected Phytopathogenic Fungal Strains
Hoda H. Senousy, Mostafa M. El-Sheekh, Abdullah A. Saber, Hanan M. Khairy, Hanan A. Said, Wardah. A. Alhoqail, Abdelghafar M. Abu-Elsaoud
Agronomy. 2022; 12(6): 1340
[Pubmed] | [DOI]
23 Antioxidants, Antimicrobial, and Anticancer Activities of Purified Chitinase of Talaromyces funiculosus Strain CBS 129594 Biosynthesized Using Crustacean Bio-Wastes
Hossam S. El-Beltagi, Omima M. El-Mahdy, Heba I. Mohamed, Abeer E. El-Ansary
Agronomy. 2022; 12(11): 2818
[Pubmed] | [DOI]
24 Nepenthes mirabilis Fractionated Pitcher Fluid Use for Mixed Agro-Waste Pretreatment: Advocacy for Non-Chemical Use in Biorefineries
Justine O. Angadam, Mahomet Njoya, Seteno K. O. Ntwampe, Boredi S. Chidi, Jun-Wei Lim, Vincent I. Okudoh, Peter L. Hewitt
Catalysts. 2022; 12(7): 726
[Pubmed] | [DOI]
25 Trichoderma: The Current Status of Its Application in Agriculture for the Biocontrol of Fungal Phytopathogens and Stimulation of Plant Growth
Renata Tyskiewicz, Artur Nowak, Ewa Ozimek, Jolanta Jaroszuk-Scisel
International Journal of Molecular Sciences. 2022; 23(4): 2329
[Pubmed] | [DOI]
26 Structure–Function Insights into the Fungal Endo-Chitinase Chit33 Depict its Mechanism on Chitinous Material
Elena Jiménez-Ortega, Peter Elias Kidibule, María Fernández-Lobato, Julia Sanz-Aparicio
International Journal of Molecular Sciences. 2022; 23(14): 7599
[Pubmed] | [DOI]
27 Genome-Wide Identification and Expression Analyses of the Chitinase Gene Family in Response to White Mold and Drought Stress in Soybean (Glycine max)
Peiyun Lv, Chunting Zhang, Ping Xie, Xinyu Yang, Mohamed A. El-Sheikh, Daniel Ingo Hefft, Parvaiz Ahmad, Tuanjie Zhao, Javaid Akhter Bhat
Life. 2022; 12(9): 1340
[Pubmed] | [DOI]
28 Optimization of Bacillus amyloliquefaciens BLB369 Culture Medium by Response Surface Methodology for Low Cost Production of Antifungal Activity
Imen Zalila-Kolsi, Sameh Kessentini, Slim Tounsi, Kaïs Jamoussi
Microorganisms. 2022; 10(4): 830
[Pubmed] | [DOI]
29 Genomic Analysis of Prophages from Klebsiella pneumoniae Clinical Isolates
Andreia T. Marques, Luís Tanoeiro, Aida Duarte, Luisa Gonçalves, Jorge M. B. Vítor, Filipa F. Vale
Microorganisms. 2021; 9(11): 2252
[Pubmed] | [DOI]
30 Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles’ Heel in Protein Structure and Industrial Utilization
Dale L. Ang, Mubasher Zahir Hoque, Md. Abir Hossain, Gea Guerriero, Roberto Berni, Jean-Francois Hausman, Saleem A Bokhari, Wallace J. Bridge, Khawar Sohail Siddiqui
Molecules. 2021; 26(3): 707
[Pubmed] | [DOI]
31 The Interactions among Isolates of Lactiplantibacillus plantarum and Dairy Yeast Contaminants: Towards Biocontrol Applications
Miloslava Kavková, Jaromír Cihlár, Vladimír Dráb, Olga Bazalová, Zuzana Dlouhá
Fermentation. 2021; 8(1): 14
[Pubmed] | [DOI]
32 Characterization of the Chitinase Gene Family in Mulberry (Morus notabilis) and MnChi18 Involved in Resistance to Botrytis cinerea
Youchao Xin, Donghao Wang, Shengmei Han, Suxia Li, Na Gong, Yiting Fan, Xianling Ji
Genes. 2021; 13(1): 98
[Pubmed] | [DOI]
33 Inclusion of Oat and Yeast Culture in Sow Gestational and Lactational Diets Alters Immune and Antimicrobial Associated Proteins in Milk
Barry Donovan, Aridany Suarez-Trujillo, Theresa Casey, Uma K. Aryal, Dawn Conklin, Leonard L. Williams, Radiah C. Minor
Animals. 2021; 11(2): 497
[Pubmed] | [DOI]
34 Essential Oil of Foeniculum vulgare Mill. as a Green Fungicide and Defense-Inducing Agent against Fusarium Root Rot Disease in Vicia faba L.
Mona M. Khaleil, Maryam M. Alnoman, Elsayed S. Abd Elrazik, Hayat Zagloul, Ahmed Mohamed Aly Khalil
Biology. 2021; 10(8): 696
[Pubmed] | [DOI]
35 Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications
Vikram Poria, Anuj Rana, Arti Kumari, Jasneet Grewal, Kumar Pranaw, Surender Singh
Biology. 2021; 10(12): 1319
[Pubmed] | [DOI]
36 Genome-Wide Identification and Analysis of Chitinase GH18 Gene Family in Mycogone perniciosa
Yang Yang, Frederick Leo Sossah, Zhuang Li, Kevin D. Hyde, Dan Li, Shijun Xiao, Yongping Fu, Xiaohui Yuan, Yu Li
Frontiers in Microbiology. 2021; 11
[Pubmed] | [DOI]
37 Rapamycin Promotes ROS-Mediated Cell Death via Functional Inhibition of xCT Expression in Melanoma Under ?-Irradiation
Yunseo Woo, Hyo-Ji Lee, Jeongyeon Kim, Seung Goo Kang, Sungjin Moon, Jeong A. Han, Young Mee Jung, Yu-Jin Jung
Frontiers in Oncology. 2021; 11
[Pubmed] | [DOI]
38 Biotechnological Eminence of Chitinases: A Focus on Thermophilic Enzyme Sources, Production Strategies and Prominent Applications
Fatima Akram, Rabia Akram, Ikram ul Haq, Ali Nawaz, Zuriat Jabbar, Zeeshan Ahmed
Protein & Peptide Letters. 2021; 28(9): 1009
[Pubmed] | [DOI]
39 Expression and Refolding of the Plant Chitinase From Drosera capensis for Applications as a Sustainable and Integrated Pest Management
Igor G. Sinelnikov, Niklas E. Siedhoff, Andrey M. Chulkin, Ivan N. Zorov, Ulrich Schwaneberg, Mehdi D. Davari, Olga A. Sinitsyna, Larisa A. Shcherbakova, Arkady P. Sinitsyn, Aleksandra M. Rozhkova
Frontiers in Bioengineering and Biotechnology. 2021; 9
[Pubmed] | [DOI]
40 Genetic Variation in Antimicrobial Activity of Honey Bee (Apis mellifera) Seminal Fluid
Shannon Holt, Naomi Cremen, Julia Grassl, Paul Schmid-Hempel, Boris Baer
Frontiers in Ecology and Evolution. 2021; 9
[Pubmed] | [DOI]
41 Chitinases production: A robust enzyme and its industrial applications
Rahul Vikram Singh, Krishika Sambyal, Anjali Negi, Shubham Sonwani, Ritika Mahajan
Biocatalysis and Biotransformation. 2021; 39(3): 161
[Pubmed] | [DOI]
42 Diversification of Fungal Chitinases and Their Functional Differentiation in Histoplasma capsulatum
Kristie D Goughenour, Janice Whalin, Jason C Slot, Chad A Rappleye, Barlow Miriam
Molecular Biology and Evolution. 2021; 38(4): 1339
[Pubmed] | [DOI]
43 Dioscorea Alata Tuber Proteome Analysis Uncovers Differentially Regulated Growth-associated Pathways of Tuber Development
Shruti Sharma, Renu Deswal
Plant and Cell Physiology. 2021; 62(1): 191
[Pubmed] | [DOI]
44 Comparative Transcriptome Analysis of Two Contrasting Maize Inbred Lines Provides Insights on Molecular Mechanisms of Stalk Rot Resistance
Andres Salcedo, Jameel Al-Haddad, C. Robin Buell, Frances Trail, Elsa Góngora-Castillo, Lina Quesada-Ocampo
PhytoFrontiers™. 2021;
[Pubmed] | [DOI]
45 Bacillus cereus MH778713 elicits tomato plant protection against Fusarium oxysporum
Verónica Ramírez, Javier Martínez, María del Rocio Bustillos-Cristales, Dolores Catañeda-Antonio, José-Antonio Munive, Antonino Baez
Journal of Applied Microbiology. 2021;
[Pubmed] | [DOI]
46 Endophytic Colletotrichum siamense for Biocontrol and Resistance Induction in Guarana Seedlings
Luana L. Casas, José O. Pereira, Pedro Q. Costa-Neto, José F. Silva, Lucas N. Almeida, Roberto A. Bianco, João L. Azevedo, Clemencia Chaves Lopez
International Journal of Microbiology. 2021; 2021: 1
[Pubmed] | [DOI]
47 A Helminth-Derived Chitinase Structurally Similar to Mammalian Chitinase Displays Immunomodulatory Properties in Inflammatory Lung Disease
Friederike Ebner, Katja Lindner, Katharina Janek, Agathe Niewienda, Piotr H. Malecki, Manfred S. Weiss, Tara E. Sutherland, Arnd Heuser, Anja A. Kühl, Jürgen Zentek, Andreas Hofmann, Susanne Hartmann, Yolanda González
Journal of Immunology Research. 2021; 2021: 1
[Pubmed] | [DOI]
48 Chitin, Chitin Oligosaccharide, and Chitin Disaccharide Metabolism of Escherichia coli Revisited: Reassignment of the Roles of ChiA, ChbR, ChbF, and ChbG
Axel Walter, Simon Friz, Christoph Mayer
Microbial Physiology. 2021; 31(2): 178
[Pubmed] | [DOI]
49 Biochemical characterization of two chitinases from Bacillus cereus sensu lato B25 with antifungal activity against Fusarium verticillioides P03
Estefanía Morales-Ruiz, Ricardo Priego-Rivera, Alejandro Miguel Figueroa-López, Jesús Eduardo Cazares-Álvarez, Ignacio E Maldonado-Mendoza
FEMS Microbiology Letters. 2021; 368(2)
[Pubmed] | [DOI]
50 Expression of 42 kDa chitinase of Trichoderma asperellum (Ta-CHI42) from a synthetic gene in Escherichia coli
Nguyen Ngoc Luong, Nguyen Quang Duc Tien, Nguyen Xuan Huy, Nguyen Hoang Tue, Le Quang Man, Duong Duc Hoang Sinh, Dang Van Thanh, Duong Thi Kim Chi, Phung Thi Bich Hoa, Nguyen Hoang Loc
FEMS Microbiology Letters. 2021; 368(16)
[Pubmed] | [DOI]
51 Recent Developments in Industrial Mycozymes: A Current Appraisal
Suresh Nath, Naveen Kango
Mycology. 2021; : 1
[Pubmed] | [DOI]
52 Multifaceted production strategies and applications of glucosamine: a comprehensive review
Twinkle Soni, Mengchuan Zhuang, Manish Kumar, Venkatesh Balan, Bryan Ubanwa, Vivekanand Vivekanand, Nidhi Pareek
Critical Reviews in Biotechnology. 2021; : 1
[Pubmed] | [DOI]
53 Perspectives on Expanding the Repertoire of Novel Microbial Chitinases for Biological Control
Thiago Machado Pasin, Tássio Brito de Oliveira, Ana Sílvia de Almeida Scarcella, Maria de Lourdes Teixeira de Moraes Polizeli, María-Eugenia Guazzaroni
Journal of Agricultural and Food Chemistry. 2021; 69(11): 3284
[Pubmed] | [DOI]
54 Recent developments in valorisation of bioactive ingredients in discard/seafood processing by-products
Fatih Ozogul, Martina Cagalj, Vida Šimat, Yesim Ozogul, Joanna Tkaczewska, Abdo Hassoun, Abderrahmane Ait Kaddour, Esmeray Kuley, Nikheel Bhojraj Rathod, Girija Gajanan Phadke
Trends in Food Science & Technology. 2021; 116: 559
[Pubmed] | [DOI]
55 Crystal structure of breast regression protein 39 (BRP39), a signaling glycoprotein expressed during mammary gland apoptosis, at 2.6 Å resolution
Ashok K. Mohanty, Suman Choudhary, Jai K. Kaushik, Andrew J. Fisher
Journal of Structural Biology. 2021; 213(2): 107737
[Pubmed] | [DOI]
56 Chitinase involved in immune regulation by mediated the toll pathway of crustacea Procambarus clarkii
Min Liu, Chen Chen, Qi-Cheng Wu, Jia-Le Chen, Li-Shang Dai, Sheng Hui Chu, Qiu-Ning Liu
Fish & Shellfish Immunology. 2021; 110: 67
[Pubmed] | [DOI]
57 Therapeutic enzymes: Discoveries, production and applications
Siddhi Tandon, Anjali Sharma, Shikha Singh, Sumit Sharma, Saurabh Jyoti Sarma
Journal of Drug Delivery Science and Technology. 2021; 63: 102455
[Pubmed] | [DOI]
58 Sclerotinia stem rot in tomato: a review on biology, pathogenicity, disease management and future research priorities
Purabi Mazumdar
Journal of Plant Diseases and Protection. 2021; 128(6): 1403
[Pubmed] | [DOI]
59 Chemoenzymatic production of chitooligosaccharides employing ionic liquids and Thermomyces lanuginosus chitinase
Manish Kumar, Jogi Madhuprakash, Venkatesh Balan, Amit Kumar Singh, V. Vivekanand, Nidhi Pareek
Bioresource Technology. 2021; 337: 125399
[Pubmed] | [DOI]
60 Genotoxic and cytotoxic effect of chitinase against Corcyra cephalonica larvae under laboratory conditions
Nithin Vijayakumar, Madanagopal Nalini, Chandrasekaran Rajkuberan, Lukmanul Hakkim Faruck, Hamid Bakshi, Alagar Yadav Sangilimuthu
International Journal of Tropical Insect Science. 2021; 41(4): 2937
[Pubmed] | [DOI]
61 Maize Endochitinase Expression in Response to Fall Armyworm Herbivory
Yang Han, Erin B. Taylor, Dawn Luthe
Journal of Chemical Ecology. 2021; 47(7): 689
[Pubmed] | [DOI]
62 Activity-Based Protein Profiling of Chitin Catabolism
Elias K. Zegeye, Natalie C. Sadler, Gerard X. Lomas, Isaac K. Attah, Janet K. Jansson, Kirsten S. Hofmockel, Christopher R. Anderton, Aaron T. Wright
ChemBioChem. 2021; 22(4): 717
[Pubmed] | [DOI]
63 Potential applications of extracellular enzymes from Streptomyces spp. in various industries
Munendra Kumar, Prateek Kumar, Payal Das, Renu Solanki, Monisha Khanna Kapur
Archives of Microbiology. 2020; 202(7): 1597
[Pubmed] | [DOI]
64 Comparative bioefficacy of Bacillus and Pseudomonas chitinase against Helopeltis theivora in tea (Camellia sinensis (L.) O.Kuntze
M. Suganthi, S. Arvinth, P. Senthilkumar
Physiology and Molecular Biology of Plants. 2020; 26(10): 2053
[Pubmed] | [DOI]
65 Functional Display of an Amoebic Chitinase in Escherichia coli Expressing the Catalytic Domain of EhCHT1 on the Bacterial Cell Surface
Ricardo Torres-Bañaga, Rosa E. Mares-Alejandre, Celina Terán-Ramírez, Ana L. Estrada-González, Patricia L.A. Muñoz-Muñoz, Samuel G. Meléndez-López, Ignacio A. Rivero, Marco A. Ramos-Ibarra
Applied Biochemistry and Biotechnology. 2020; 192(4): 1255
[Pubmed] | [DOI]
66 Enhanced virulence of Beauveria bassiana against Diatraea saccharalis using a soluble recombinant enzyme with endo- and exochitinase activity
Andrea Lovera, Mariano Belaich, Laura Villamizar, Manuel A. Patarroyo, Gloria Barrera
Biological Control. 2020; 144: 104211
[Pubmed] | [DOI]
67 Simple, functional, inexpensive cell extract for in vitro prototyping of proteins with disulfide bonds
Jared L. Dopp, Nigel F. Reuel
Biochemical Engineering Journal. 2020; 164: 107790
[Pubmed] | [DOI]
68 Antibacterial activities of microwave-assisted synthesized polypyrrole/chitosan and poly (pyrrole-N-(1-naphthyl) ethylenediamine) stimulated by C-dots
Moorthy Maruthapandi, Kusha Sharma, John H.T. Luong, Aharon Gedanken
Carbohydrate Polymers. 2020; 243: 116474
[Pubmed] | [DOI]
69 Functional expression of recombinant hybrid enzymes composed of bacterial and insect’s chitinase domains in E. coli
Aron Paek, Min Jae Kim, Hee Yun Park, Je Geun Yoo, Seong Eun Jeong
Enzyme and Microbial Technology. 2020; 136: 109492
[Pubmed] | [DOI]
70 Sequence analysis and docking performance of extracellular chitinase from Bacillus pumilus MCB-7, a novel mangrove isolate
Rishad K.S, Sherin Varghese, Jisha M.S
Enzyme and Microbial Technology. 2020; 140: 109624
[Pubmed] | [DOI]
71 Potential use of Bacillus genus to control of bananas diseases: Approaches toward high yield production and sustainable management
Arezoo Dadrasnia, Mohammed Maikudi Usman, Rahmat Omar, Salmah Ismail, Rosazlin Abdullah
Journal of King Saud University - Science. 2020; 32(4): 2336
[Pubmed] | [DOI]
72 Expression and biochemical characterization of a novel chitinase ChiT-7 from the metagenome in the soil of a mangrove tidal flat in China
Ren Kuan Li, Ya Juan Hu, Tzi Bun Ng, Bing Qi Guo, Zi He Zhou, Jing Zhao, Xiu Yun Ye
International Journal of Biological Macromolecules. 2020; 158: 1125
[Pubmed] | [DOI]
73 Partial purification and characterization of chitinase produced by Bacillus licheniformis B307
Yasser Akeed, Faiza Atrash, Walid Naffaa
Heliyon. 2020; 6(5): e03858
[Pubmed] | [DOI]
74 Enzymatic characterization and structure-function relationship of two chitinases, LmChiA and LmChiB, from Listeria monocytogenes
Wasinee Churklam, Ratchaneewan Aunpad
Heliyon. 2020; 6(7): e04252
[Pubmed] | [DOI]
75 Enhanced glucosamine production through synergistic action of Aspergillus terreus chitozymes
Manish Kumar, Pragati Dangayach, Nidhi Pareek
Journal of Cleaner Production. 2020; 262: 121363
[Pubmed] | [DOI]
76 Ultrasound enhanced the binding ability of chitinase onto chitin: From an AFM insight
Furong Hou, Liang He, Xiaobin Ma, Danli Wang, Tian Ding, Xingqian Ye, Donghong Liu
Ultrasonics Sonochemistry. 2020; 67: 105117
[Pubmed] | [DOI]
77 Seed priming with Pseudomonas putida isolated from rhizosphere triggers innate resistance against Fusarium wilt in tomato through pathogenesis-related protein activation and phenylpropanoid pathway
Nellickal Subramanyan JAYAMOHAN, Savita Veeranagouda PATIL, Belur Satyan KUMUDINI
Pedosphere. 2020; 30(5): 651
[Pubmed] | [DOI]
78 A Plumieridine-Rich Fraction From Allamanda polyantha Inhibits Chitinolytic Activity and Exhibits Antifungal Properties Against Cryptococcus neoformans
Eden Silva e Souza, Vanessa de Abreu Barcellos, Nicolau Sbaraini, Júlia Catarina Vieira Reuwsaat, Rafael de Oliveira Schneider, Adriana Corrêa da Silva, Ane Wichine Acosta Garcia, Gilsane Lino von Poser, Euzébio Guimarães Barbosa, João Paulo Matos Santos Lima, Marilene Henning Vainstein
Frontiers in Microbiology. 2020; 11
[Pubmed] | [DOI]
79 Chemoenzymatic Production and Engineering of Chitooligosaccharides and N-acetyl Glucosamine for Refining Biological Activities
Manish Kumar, Meenakshi Rajput, Twinkle Soni, Vivekanand Vivekanand, Nidhi Pareek
Frontiers in Chemistry. 2020; 8
[Pubmed] | [DOI]
80 Cockroaches: Allergens, Component-Resolved Diagnosis (CRD) and Component-Resolved Immunotherapy
Nitat Sookrung, Anchalee Tungtrongchitr, Wanpen Chaicumpa
Current Protein & Peptide Science. 2020; 21(2): 124
[Pubmed] | [DOI]
81 Genome-wide analysis of the transcriptional response to drought stress in root and leaf of common bean
Wendell Jacinto Pereira, Arthur Tavares de Oliveira Melo, Alexandre Siqueira Guedes Coelho, Fabiana Aparecida Rodrigues, Sujan Mamidi, Sérgio Amorim de Alencar, Anna Cristina Lanna, Paula Arielle Mendes Ribeiro Valdisser, Claudio Brondani, Ivanildo Ramalho do Nascimento-Júnior, Tereza Cristina de Oliveira Borba, Rosana Pereira Vianello
Genetics and Molecular Biology. 2020; 43(1)
[Pubmed] | [DOI]
82 A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization
Andrea Sánchez-Vallet, Hui Tian, Luis Rodriguez-Moreno, Dirk-Jan Valkenburg, Raspudin Saleem-Batcha, Stephan Wawra, Anja Kombrink, Leonie Verhage, Ronnie de Jonge, H. Peter van Esse, Alga Zuccaro, Daniel Croll, Jeroen R. Mesters, Bart P. H. J. Thomma, Hui-Shan Guo
PLOS Pathogens. 2020; 16(6): e1008652
[Pubmed] | [DOI]
83 A salivary chitinase of Varroa destructor influences host immunity and mite’s survival
Andrea Becchimanzi, Rosarita Tatè, Ewan M. Campbell, Silvia Gigliotti, Alan S. Bowman, Francesco Pennacchio, Leonard Foster
PLOS Pathogens. 2020; 16(12): e1009075
[Pubmed] | [DOI]
84 Genes Involved in Stress Response and Especially in Phytoalexin Biosynthesis Are Upregulated in Four Malus Genotypes in Response to Apple Replant Disease
Stefanie Reim, Annmarie-Deetja Rohr, Traud Winkelmann, Stefan Weiß, Benye Liu, Ludger Beerhues, Michaela Schmitz, Magda-Viola Hanke, Henryk Flachowsky
Frontiers in Plant Science. 2020; 10
[Pubmed] | [DOI]
85 The CaChiVI2 Gene of Capsicum annuum L. Confers Resistance Against Heat Stress and Infection of Phytophthora capsici
Muhammad Ali, Izhar Muhammad, Saeed ul Haq, Mukhtar Alam, Abdul Mateen Khattak, Kashif Akhtar, Hidayat Ullah, Abid Khan, Gang Lu, Zhen-Hui Gong
Frontiers in Plant Science. 2020; 11
[Pubmed] | [DOI]
86 Putative Antimicrobial Peptides of the Posterior Salivary Glands from the Cephalopod Octopus vulgaris Revealed by Exploring a Composite Protein Database
Daniela Almeida, Dany Domínguez-Pérez, Ana Matos, Guillermin Agüero-Chapin, Hugo Osório, Vitor Vasconcelos, Alexandre Campos, Agostinho Antunes
Antibiotics. 2020; 9(11): 757
[Pubmed] | [DOI]
87 Melatonin Mitigates the Infection of Colletotrichum gloeosporioides via Modulation of the Chitinase Gene and Antioxidant Activity in Capsicum annuum L.
Muhammad Ali, Anthony Tumbeh Lamin-Samu, Izhar Muhammad, Mohamed Farghal, Abdul Mateen Khattak, Ibadullah Jan, Saeed ul Haq, Abid Khan, Zhen-Hui Gong, Gang Lu
Antioxidants. 2020; 10(1): 7
[Pubmed] | [DOI]
88 Extracellular Enzymes and Bioactive Compounds from Antarctic Terrestrial Fungi for Bioprospecting
Laura Zucconi, Fabiana Canini, Marta Elisabetta Temporiti, Solveig Tosi
International Journal of Environmental Research and Public Health. 2020; 17(18): 6459
[Pubmed] | [DOI]
89 Abalone Viral Ganglioneuritis
Serge Corbeil
Pathogens. 2020; 9(9): 720
[Pubmed] | [DOI]
90 Activation of Early Defense Signals in Seedlings of Nicotiana benthamiana Treated with Chitin Nanoparticles
Miguel López, Elisa Miranda, Cecilia Ramos, Héctor García, Andrónico Neira-Carrillo
Plants. 2020; 9(5): 607
[Pubmed] | [DOI]
91 Gene Cloning, Characterization, and Molecular Simulations of a Novel Recombinant Chitinase from Chitinibacter Tainanensis CT01 Appropriate for Chitin Enzymatic Hydrolysis
Yeng-Tseng Wang, Po-Long Wu
Polymers. 2020; 12(8): 1648
[Pubmed] | [DOI]
92 Two Highly Similar Chitinases from Marine Vibrio Species have Different Enzymatic Properties
Xinxin He, Min Yu, Yanhong Wu, Lingman Ran, Weizhi Liu, Xiao-Hua Zhang
Marine Drugs. 2020; 18(3): 139
[Pubmed] | [DOI]
93 Isolation and Molecular Identification of Two Chitinase Producing Bacteria from Marine Shrimp Shell Wastes
Maaly H. Ali, Saja Aljadaani, Jehan Khan, Ikhlas Sindi, Majdah Aboras, Magda M. Aly
Pakistan Journal of Biological Sciences. 2020; 23(2): 139
[Pubmed] | [DOI]
94 Transcriptomic Analysis Reveals Candidate Genes Responsive to Sclerotinia scleroterum and Cloning of the Ss-Inducible Chitinase Genes in Morus laevigata
Huanhuan Jiang, Xiaoyun Jin, Xiaofeng Shi, Yufei Xue, Jiayi Jiang, Chenglong Yuan, Youjie Du, Xiaodan Liu, Ruifang Xie, Xuemei Liu, Lejing Li, Lijuan Wei, Chunxing Zhang, Liangjing Tong, Yourong Chai
International Journal of Molecular Sciences. 2020; 21(21): 8358
[Pubmed] | [DOI]
95 Cloning, expression and characterization of a chitinase from Paenibacillus chitinolyticus strain UMBR 0002
Cong Liu, Naikun Shen, Jiafa Wu, Mingguo Jiang, Songbiao Shi, Jinzi Wang, Yanye Wei, Lifang Yang
PeerJ. 2020; 8: e8964
[Pubmed] | [DOI]
96 Identification and Expression Analysis of Genes Induced in Response to Tomato chlorosis virus Infection in Tomato
Mehtap Sahin-Çevik, Emine Dogus Sivri, Bayram Çevik
The Plant Pathology Journal. 2019; 35(3): 257
[Pubmed] | [DOI]
97 Crystal Structures of Protein-Bound Cyclic Peptides
Alpeshkumar K. Malde, Timothy A. Hill, Abishek Iyer, David P. Fairlie
Chemical Reviews. 2019; 119(17): 9861
[Pubmed] | [DOI]
98 Microbial metabolomics: essential definitions and the importance of cultivation conditions for utilizing Bacillus species as bionematicides
I. Horak, G. Engelbrecht, P.J. Jansen Rensburg, S. Claassens
Journal of Applied Microbiology. 2019; 127(2): 326
[Pubmed] | [DOI]
99 Changes in the secretome of Vitis vinifera cv. Monastrell cell cultures treated with cyclodextrins and methyl jasmonate
S. Belchí-Navarro, L. Almagro, R. Bru-Martínez, M.A. Pedreño
Plant Physiology and Biochemistry. 2019; 135: 520
[Pubmed] | [DOI]
100 Synthesis, homology modeling, molecular docking, dynamics, and antifungal screening of new 4-hydroxycoumarin derivatives as potential chitinase inhibitors
Rasha Z. Batran, Mohammed A. Khedr, Nehad A. Abdel Latif, Abeer A. Abd El Aty, Abeer N. Shehata
Journal of Molecular Structure. 2019; 1180: 260
[Pubmed] | [DOI]
101 Pesticidal prospectives of chitinolytic bacteria in agricultural pest management
A.R.N.S. Subbanna,H. Rajasekhara,J. Stanley,K.K. Mishra,A. Pattanayak
Soil Biology and Biochemistry. 2018; 116: 52
[Pubmed] | [DOI]
102 Suppression of Plant Immunity by Fungal Chitinase-like Effectors
Gabriel Lorencini Fiorin, Andrea Sanchéz-Vallet, Daniela Paula de Toledo Thomazella, Paula Favoretti Vital do Prado, Leandro Costa do Nascimento, Antonio Vargas de Oliveira Figueira, Bart P.H.J. Thomma, Gonçalo Amarante Guimarães Pereira, Paulo José Pereira Lima Teixeira
Current Biology. 2018; 28(18): 3023
[Pubmed] | [DOI]
103 Characterization and expression analysis of chitinase genes (CHIT1, CHIT2 and CHIT3) in turbot ( Scophthalmus maximus L.) following bacterial challenge
Chengbin Gao,Xin Cai,Yu Zhang,Baofeng Su,Huanhuan Song,Wang Wenqi,Chao Li
Fish & Shellfish Immunology. 2017; 64: 357
[Pubmed] | [DOI]
104 Chitin and chitinase: Role in pathogenicity, allergenicity and health
Seema Patel,Arun Goyal
International Journal of Biological Macromolecules. 2017; 97: 331
[Pubmed] | [DOI]
105 Expression of chitinase gene in BL21 pET system and investigating the biocatalystic performance of chitinase-loaded AlgSep nanocomposite beads
Reza Mohammadzadeh,Maryam Agheshlouie,Gholam Reza Mahdavinia
International Journal of Biological Macromolecules. 2017;
[Pubmed] | [DOI]
106 Biochemical characterization of a novel thermostable chitinase from Hydrogenophilus hirschii strain KB-DZ44
Khelifa Bouacem,Hassiba Laribi-Habchi,Sondes Mechri,Hocine Hacene,Bassem Jaouadi,Amel Bouanane-Darenfed
International Journal of Biological Macromolecules. 2017;
[Pubmed] | [DOI]
107 Bactericidal and fungistatic activity of peptide derived from GH18 domain of prawn chitinase 3 and its immunological functions during biological stress
Gayathri Ravichandran,Venkatesh Kumaresan,Arun Mahesh,Arunkumar Dhayalan,Aziz Arshad,Mariadhas Valan Arasu,Naif Abdullah Al-Dhabi,Mukesh Pasupuleti,Jesu Arockiaraj
International Journal of Biological Macromolecules. 2017;
[Pubmed] | [DOI]
108 Spatio-temporal patterns of enzyme activities after manure application reflect mechanisms of niche differentiation between plants and microorganisms
Shibin Liu,Bahar S. Razavi,Xu Su,Menuka Maharjan,Mohsen Zarebanadkouki,Evgenia Blagodatskaya,Yakov Kuzyakov
Soil Biology and Biochemistry. 2017; 112: 100
[Pubmed] | [DOI]
109 The endochitinase VDECH from Verticillium dahliae inhibits spore germination and activates plant defense responses
Xiao-Xiao Cheng,Li-Hong Zhao,Steven J. Klosterman,Hong-Jie Feng,Zi-Li Feng,Feng Wei,Yong-Qiang Shi,Zhi-Fang Li,He-Qin Zhu
Plant Science. 2017; 259: 12
[Pubmed] | [DOI]
110 Towards a sustainable biobased industry – Highlighting the impact of extremophiles
Anna Krüger,Christian Schäfers,Carola Schröder,Garabed Antranikian
New Biotechnology. 2017;
[Pubmed] | [DOI]
111 In silico analysis of ChtBD3 domain to find its role in bacterial pathogenesis and beyond
Seema Patel,Abdur Rauf,Biswa Ranjan Meher
Microbial Pathogenesis. 2017; 110: 519
[Pubmed] | [DOI]
112 Crop molds and mycotoxins: Alternative management using biocontrol
Phuong-Anh Nguyen,Caroline Strub,Angélique Fontana,Sabine Schorr-Galindo
Biological Control. 2017; 104: 10
[Pubmed] | [DOI]
113 Improved fluorescent labeling of chitin oligomers: Chitinolytic properties of acidic mammalian chitinase under somatic tissue pH conditions
Satoshi Wakita,Masahiro Kimura,Naoki Kato,Akinori Kashimura,Shunsuke Kobayashi,Naoto Kanayama,Misa Ohno,Shotaro Honda,Masayoshi Sakaguchi,Yasusato Sugahara,Peter O. Bauer,Fumitaka Oyama
Carbohydrate Polymers. 2017;
[Pubmed] | [DOI]
114 A critical review on serine protease: Key immune manipulator and pathology mediator
S. Patel
Allergologia et Immunopathologia. 2017;
[Pubmed] | [DOI]
115 Diversity and functional annotation of chitinolytic Bacillus and associated chitinases from north western Indian Himalayas
R.N.S. Subbanna Avupati,M.S. Khan,Stanley Johnson,Stanley Shivashankara,Manish Kumar Yogi
Applied Soil Ecology. 2017; 119: 46
[Pubmed] | [DOI]
116 Identification of candidate infection genes from the model entomopathogenic nematode Heterorhabditis bacteriophora
Jonathan Vadnal,Ramesh Ratnappan,Melissa Keaney,Eric Kenney,Ioannis Eleftherianos,Damien O’Halloran,John M. Hawdon
BMC Genomics. 2017; 18(1)
[Pubmed] | [DOI]
117 Floral nectar of the obligate outcrossing Canavalia gladiata (Jacq.) DC. (Fabaceae) contains only one predominant protein, a class III acidic chitinase
X. L. Ma,R. I. Milne,H. X. Zhou,J. Y. Fang,H. G. Zha,H. P. Mock
Plant Biology. 2017;
[Pubmed] | [DOI]
118 Optimizing the expression of a Heterologous chitinase: A study of different promoters
Abigail F. da Silva,Belén García-Fraga,Jacobo López-Seijas,Carmen Sieiro
Bioengineered. 2017; 8(4): 428
[Pubmed] | [DOI]
119 Molecular dynamics simulation of chitinase I from Thermomyces lanuginosus SSBP to ensure optimal activity
Faez Iqbal Khan,Krishna Bisetty,Ke-Ren Gu,Suren Singh,Kugen Permaul,Md. Imtaiyaz Hassan,Dong-Qing Wei
Molecular Simulation. 2017; 43(7): 480
[Pubmed] | [DOI]
120 Complete genome of Arthrobacter alpinus strain R3.8, bioremediation potential unraveled with genomic analysis
Wah-Seng See-Too,Robson Ee,Yan-Lue Lim,Peter Convey,David A. Pearce,Taznim Begam Mohd Mohidin,Wai-Fong Yin,Kok Gan Chan
Standards in Genomic Sciences. 2017; 12(1)
[Pubmed] | [DOI]
121 Polysaccharide Degradation Capability of Actinomycetales Soil Isolates from a Semiarid Grassland of the Colorado Plateau
Chris M. Yeager, La Verne Gallegos-Graves, John Dunbar, Cedar N. Hesse, Hajnalka Daligault, Cheryl R. Kuske, Alfons J. M. Stams
Applied and Environmental Microbiology. 2017; 83(6)
[Pubmed] | [DOI]
122 The Role of Plant Innate Immunity in the Legume-Rhizobium Symbiosis
Yangrong Cao,Morgan K. Halane,Walter Gassmann,Gary Stacey
Annual Review of Plant Biology. 2017; 68(1): 535
[Pubmed] | [DOI]
123 Complete Genome Sequence Analysis of Enterobacter sp. SA187, a Plant Multi-Stress Tolerance Promoting Endophytic Bacterium
Cristina Andrés-Barrao,Feras F. Lafi,Intikhab Alam,Axel de Zélicourt,Abdul A. Eida,Ameerah Bokhari,Hanin Alzubaidy,Vladimir B. Bajic,Heribert Hirt,Maged M. Saad
Frontiers in Microbiology. 2017; 8
[Pubmed] | [DOI]
124 Purification and molecular characterization of chitinases from soil actinomycetes
Das Payal,Kumar Prateek,Kumar Munendra,Solanki Renu,Khanna Kapur Monisha
African Journal of Microbiology Research. 2017; 11(27): 1086
[Pubmed] | [DOI]
125 Sequence/structural analysis of xylem proteome emphasizes pathogenesis-related proteins, chitinases andß-1, 3-glucanases as key players in grapevine defense againstXylella fastidiosa
Sandeep Chakraborty,Rafael Nascimento,Paulo A. Zaini,Hossein Gouran,Basuthkar J. Rao,Luiz R. Goulart,Abhaya M. Dandekar
PeerJ. 2016; 4: e2007
[Pubmed] | [DOI]
126 Isolation and Characterization of Chitinolytic Bacteria for Chitinase Production from the African Catfish, Clarias gariepinus (Burchell, 1822)
A.A. Ajayi,E.A. Onibokun,F.O.A. George,O.M. Atolagbe
Research Journal of Microbiology. 2016; 11(4): 119
[Pubmed] | [DOI]
127 Feces Derived Allergens of Tyrophagus putrescentiae Reared on Dried Dog Food and Evidence of the Strong Nutritional Interaction between the Mite and Bacillus cereus Producing Protease Bacillolysins and Exo-chitinases
Tomas Erban,Dagmar Rybanska,Karel Harant,Bronislava Hortova,Jan Hubert
Frontiers in Physiology. 2016; 7
[Pubmed] | [DOI]
128 A pH based molecular dynamics simulations of chitinase II isolated from Thermomyces lanuginosus SSBP
Faez Iqbal Khan,Krishna Bisetty,Dong-Qing Wei,Md. Imtaiyaz Hassan,Rajni Hatti Kaul
Cogent Biology. 2016; 2(1)
[Pubmed] | [DOI]
129 A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus
Ayumi Horiuchi, Mehwish Aslam, Tamotsu Kanai, Haruyuki Atomi, V. Müller
Applied and Environmental Microbiology. 2016; 82(12): 3554
[Pubmed] | [DOI]
130 A complete chitinolytic system in the atherinopsid pike silversideChirostoma estor: gene expression and activities
P. Pohls,L. González-Dávalos,O. Mora,A. Shimada,A. Varela-Echavarria,E. M. Toledo-Cuevas,C. A. Martínez-Palacios
Journal of Fish Biology. 2016;
[Pubmed] | [DOI]
131 Treatment with rhDNase in patients with cystic fibrosis altersin-vitroCHIT-1 activity of isolated leucocytes
M. Weckmann,C. Schultheiss,A. Hollaender,I. Bobis,J. Rupp,M.V. Kopp
Clinical & Experimental Immunology. 2016; 185(3): 382
[Pubmed] | [DOI]
132 Strategic tillage increased the relative abundance of Acidobacteria but did not impact on overall soil microbial properties of a 19-year no-till Solonetz
Hongwei Liu,Lilia C. Carvalhais,Mark Crawford,Yash P. Dang,Paul G. Dennis,Peer M. Schenk
Biology and Fertility of Soils. 2016;
[Pubmed] | [DOI]
133 Secretome analysis of virulentPyrenophora teresf. teresisolates
Ismail A. Ismail,Amanda J. Able
[Pubmed] | [DOI]
134 Expression of MfAvr4 in banana leaf sections with black leaf streak disease caused by Mycosphaerella fijiensis: a technical validation
Cecilia Mónica Rodríguez-García,Abril Diane Canché-Gómez,Luis Sáenz-Carbonell,Leticia Peraza-Echeverría,Blondy Canto-Canché,Ignacio Islas-Flores,Santy Peraza-Echeverría
Australasian Plant Pathology. 2016;
[Pubmed] | [DOI]
135 Antagonist effects of Bacillus spp. strains against Fusarium graminearum for protection of durum wheat (Triticum turgidum L. subsp. durum)
Imen Zalila-Kolsi,Afif Ben Mahmoud,Hacina Ali,Sameh Sellami,Zina Nasfi,Slim Tounsi,Kaïs Jamoussi
Microbiological Research. 2016; 192: 148
[Pubmed] | [DOI]
136 First insights into the diversity and functional properties of chitinases of the latex of Calotropis procera
Cleverson D.T. Freitas,Carolina A. Viana,Ilka M. Vasconcelos,Frederico B.B. Moreno,José V. Lima-Filho,Hermogenes D. Oliveira,Renato A. Moreira,Ana Cristina O. Monteiro-Moreira,Márcio V. Ramos
Plant Physiology and Biochemistry. 2016; 108: 361
[Pubmed] | [DOI]
137 Activity, stability and folding analysis of the chitinase from Entamoeba histolytica
Patricia L.A. Muñoz,Alexis Z. Minchaca,Rosa E. Mares,Marco A. Ramos
Parasitology International. 2016; 65(1): 70
[Pubmed] | [DOI]
138 Molecular Cloning and Characterization of ech46 Endochitinase From Trichoderma harzianum
Vivek Sharma,Richa Salwan,P.N. Sharma,S.S. Kanwar
International Journal of Biological Macromolecules. 2016;
[Pubmed] | [DOI]
139 Complete genome sequence of the fish pathogen Aeromonas veronii TH0426 with potential application in biosynthesis of pullulanase and chitinase
Yuanhuan Kang,Xiaoyi Pan,Yang Xu,Shahrood A. Siddiqui,Chunfeng Wang,Xiaofeng Shan,Aidong Qian
Journal of Biotechnology. 2016;
[Pubmed] | [DOI]
140 The flexible feedstock concept in Industrial Biotechnology: Metabolic engineering of Escherichia coli, Corynebacterium glutamicum, Pseudomonas, Bacillus and yeast strains for access to alternative carbon sources
Volker F. Wendisch,Luciana Fernandes Brito,Marina Gil Lopez,Guido Hennig,Johannes Pfeifenschneider,Elvira Sgobba,Kareen H. Veldmann
Journal of Biotechnology. 2016; 234: 139
[Pubmed] | [DOI]
141 Complete genome sequence of Serratia multitudinisentens RB-25T, a novel chitinolytic bacterium
Yan-Lue Lim,Delicia Yong,Robson Ee,Kok-Keng Tee,Wai-Fong Yin,Kok-Gan Chan
Journal of Biotechnology. 2015; 207: 32
[Pubmed] | [DOI]
142 Thermostable chitinase II from Thermomyces lanuginosus SSBP: Cloning, structure prediction and molecular dynamics simulations
Faez Iqbal Khan,Algasan Govender,Kugen Permaul,Suren Singh,Krishna Bisetty
Journal of Theoretical Biology. 2015; 374: 107
[Pubmed] | [DOI]
143 Isolation and characterization of endochitinase and exochitinase of Setaria cervi
Piyush Dravid,Deep C. Kaushal,Jitendra K. Saxena,Nuzhat A. Kaushal
Parasitology International. 2015; 64(6): 579
[Pubmed] | [DOI]
144 In silico characterization, homology modeling of Camellia sinensis chitinase and its evolutionary analyses with other plant chitinases
Swarnendu Chandra,Arun Kumar Dutta,Krishnappa Nagarathana Chandrashekara,Krishnendu Acharya
Proceedings of the National Academy of Sciences, India Section B: Biological Sciences. 2015;
[Pubmed] | [DOI]
145 Purification and characterisation of an acidic and antifungal chitinase produced by a Streptomyces sp.
Narayanan Karthik,Parameswaran Binod,Ashok Pandey
Bioresource Technology. 2015; 188: 195
[Pubmed] | [DOI]
146 Evolutionary analysis of the global landscape of protein domain types and domain architectures associated with family 14 carbohydrate-binding modules
Ti-Cheng Chang,Ioannis Stergiopoulos
FEBS Letters. 2015; 589(15): 1813
[Pubmed] | [DOI]
147 Purification and biochemical characterization of chitinase of Aeromonas hydrophila SBK1 biosynthesized using crustacean shell
Suman Kumar Halder,Arijit Jana,Tanmay Paul,Arpan Das,Kuntal Ghosh,Bikas Ranjan Pati,Keshab Chandra Mondal
Biocatalysis and Agricultural Biotechnology. 2015;
[Pubmed] | [DOI]
148 Synergistic Action of a Metalloprotease and a Serine Protease from Fusarium oxysporum f. sp. lycopersici Cleaves Chitin-Binding Tomato Chitinases, Reduces Their Antifungal Activity, and Enhances Fungal Virulence
Mansoor Karimi Jashni, Ivo H. M. Dols, Yuichiro Iida, Sjef Boeren, Henriek G. Beenen, Rahim Mehrabi, Jérôme Collemare, Pierre J. G. M. de Wit
Molecular Plant-Microbe Interactions®. 2015; 28(9): 996
[Pubmed] | [DOI]
149 Computational analysis of difenoconazole interaction with soil chitinases
D L Vladoiu,M N Filimon,V Ostafe,A Isvoran
Journal of Physics: Conference Series. 2015; 574: 012012
[Pubmed] | [DOI]
150 Genome Sequence, Comparative Analysis, and Evolutionary Insights into Chitinases of Entomopathogenic Fungus Hirsutella thompsonii
Yamini Agrawal,Indu Khatri,Srikrishna Subramanian,Belle Damodara Shenoy
Genome Biology and Evolution. 2015; 7(3): 916
[Pubmed] | [DOI]
151 Novel Protease-Resistant Exochitinase (Echi47) from Pig Fecal Environment DNA with Application Potentials in the Food and Feed Industries
Yuchun Liu,Qiaojuan Yan,Shaoqing Yang,Zhengqiang Jiang
Journal of Agricultural and Food Chemistry. 2015; 63(27): 6262
[Pubmed] | [DOI]
152 Functional Properties of the Catalytic Domain of Mouse Acidic Mammalian Chitinase Expressed in Escherichia coli
Akinori Kashimura,Masahiro Kimura,Kazuaki Okawa,Hirotaka Suzuki,Atsushi Ukita,Satoshi Wakita,Kana Okazaki,Misa Ohno,Peter Bauer,Masayoshi Sakaguchi,Yasusato Sugahara,Fumitaka Oyama
International Journal of Molecular Sciences. 2015; 16(2): 4028
[Pubmed] | [DOI]
153 The Correlation between Chitin and Acidic Mammalian Chitinase in Animal Models of Allergic Asthma
Chia-Rui Shen,Horng-Heng Juang,Hui-Shan Chen,Ching-Jen Yang,Chia-Jen Wu,Meng-Hua Lee,Yih-Shiou Hwang,Ming-Ling Kuo,Ya-Shan Chen,Jeen-Kuan Chen,Chao-Lin Liu
International Journal of Molecular Sciences. 2015; 16(12): 27371
[Pubmed] | [DOI]
154 Purification, characteristics and identification of chitinases synthesized by the bacterium Serratia plymuthica MP44 antagonistic against phytopathogenic fungi
U. Jankiewicz,M. Swiontek Brzezinska
Applied Biochemistry and Microbiology. 2015; 51(5): 560
[Pubmed] | [DOI]
155 Identification of Differentially Expressed Genes in Leaf of Reaumuria soongorica under PEG-Induced Drought Stress by Digital Gene Expression Profiling
Yubing Liu,Meiling Liu,Xinrong Li,Bo Cao,Xiaofei Ma,Cynthia Gibas
PLoS ONE. 2014; 9(4): e94277
[Pubmed] | [DOI]
156 Novel mode of action of plant defense peptides - hevein-like antimicrobial peptides from wheat inhibit fungal metalloproteases
Anna A. Slavokhotova,Todd A. Naumann,Neil P. J. Price,Eugene A. Rogozhin,Yaroslav A. Andreev,Alexander A. Vassilevski,Tatyana I. Odintsova
FEBS Journal. 2014; : n/a
[Pubmed] | [DOI]
157 Isolation and characterization of chitin-degrading micro-organisms from the faeces of Goeldiæs monkey,Callimico goeldii
C. Macdonald,S. Barden,S. Foley
Journal of Applied Microbiology. 2014; 116(1): 52-59
[Pubmed] | [DOI]
158 A Novel Family 19 Chitinase from the Marine-Derived Pseudoalteromonas tunicata CCUG 44952T: Heterologous Expression, Characterization and Antifungal Activity
Belén García-Fraga,Abigail F. da Silva,Jacobo López-Seijas,Carmen Sieiro
Biochemical Engineering Journal. 2014;
[Pubmed] | [DOI]
159 Purification and characterization of an antifungal chitinase from Citrobacter freundii str. nov. haritD11
Meruvu, H., Donthireddy, S.R.R.
Applied Biochemistry and Biotechnology. 2014; 172(1): 196-205
160 Extremozymes—biocatalysts with unique properties from extremophilic microorganisms
Skander Elleuche,Carola Schröder,Kerstin Sahm,Garabed Antranikian
Current Opinion in Biotechnology. 2014; 29: 116
[Pubmed] | [DOI]
161 Chitinolytic assay for Trichoderma species isolated from different geographical locations of Uttar Pradesh
Pandey Sonika,Shahid Mohammad,Srivastava Mukesh,Sharma Antima,Singh Anuradha,Kumar Vipul,Jee Gupta Shyam
African Journal of Biotechnology. 2014; 13(45): 4246
[Pubmed] | [DOI]
162 Efficient biosynthesis of a chitinase fromHalobacterium salinarumexpressed inEscherichia coli
Fatima Moscoso,Myriam Sieira,Alberto Domínguez,Francisco J. Deive,Maria A. Longo,Maria A. Sanromán
Journal of Chemical Technology & Biotechnology. 2013; : n/a
[Pubmed] | [DOI]
163 A Review of the Applications of Chitin and Its Derivatives in Agriculture to Modify Plant-Microbial Interactions and Improve Crop Yields
Russell Sharp
Agronomy. 2013; 3(4): 757
[Pubmed] | [DOI]


    Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
 Related articles
    Access Statistics
    Email Alert *
    Add to My List *
* Registration required (free)  

  In this article
   Bacterial Chitinases
   Fungal Chitinases
   Plant Chitinases
   Insect Chitinases
   Mammalian Chitinases
    Methods of Produ...
   Medicinal Functions
   Future Prospects

 Article Access Statistics
    PDF Downloaded1710    
    Comments [Add]    
    Cited by others 163    

Recommend this journal