Microbial chitinases and their relevance in various industries

. 2023 Feb ; 68 (1) : 29-53. [epub] 20220816

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, přehledy

Perzistentní odkaz   https://www.medvik.cz/link/pmid35972681
Odkazy

PubMed 35972681
DOI 10.1007/s12223-022-00999-w
PII: 10.1007/s12223-022-00999-w
Knihovny.cz E-zdroje

Chitin, the second most abundant biopolymer on earth after cellulose, is composed of β-1,4-N-acetylglucosamine (GlcNAc) units. It is widely distributed in nature, especially as a structural polysaccharide in the cell walls of fungi, the exoskeletons of crustaceans, insects, and nematodes. However, the principal commercial source of chitin is the shells of marine or freshwater invertebrates. Microbial chitinases are largely responsible for chitin breakdown in nature, and they play an important role in the ecosystem's carbon and nitrogen balance. Several microbial chitinases have been characterized and are gaining prominence for their applications in various sectors. The current review focuses on chitinases of microbial origin, their diversity, and their characteristics. The applications of chitinases in several industries such as agriculture, food, the environment, and pharmaceutical sectors are also highlighted.

Zobrazit více v PubMed

Ahmed AS, Ezziyyani M, Sanchez CP, Candela ME (2003) Effect of chitin on biological control activity of Bacillus spp. and Trichoderma harzianum against root rot disease in pepper (Capsicum annuum) plants. Eur J Plant Pathol 109:633–637. https://doi.org/10.1023/A:1024734216814 DOI

Ajayi AA, Onibokun EA, George FOA, Atolagbe OM (2016) Isolation and characterization of chitinolytic bacteria for chitinase production from the African catfish, Clarias gariepinus (Burchell, 1822). Res J Microbiol 11:119–125. https://doi.org/10.3923/jm.2016.119.125 DOI

Akagi K, Watanabe J, Hara M, Kezuka Y, Chikaishi E, Yamaguchi T, Akutsu H, Nonaka T, Watanabe T, Ikegami T (2006) Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C. J Biochem 139:483–493. https://doi.org/10.1093/jb/mvj062 PubMed DOI

Akeed Y, Atrash F, Naffaa W (2020) Partial purification and characterization of chitinase produced by Bacillus licheniformis B307. Heliyon. https://doi.org/10.1016/j.heliyon.2020.e03858 PubMed DOI PMC

Ali M, Li QH, Zou T, Wei AM, Gombojav G, Lu G, Gong ZH (2020) Chitinase gene positively regulates hypersensitive and defense responses of pepper to Colletotrichum acutatum infection. Int J Mol Sci. https://doi.org/10.3390/ijms21186624 PubMed DOI PMC

Ali S, Wu J, Huang Z, Ren SX (2010) Production and regulation of extracellular chitinase from the entomopathogenic fungus Isaria fumosorosea. Biocontrol Sci Technol 20:723–738. https://doi.org/10.1080/09583151003714091 DOI

Aliabadi N, Aminzadeh S, Karkhane AA, Haghbeen K (2016) Thermostable chitinase from Cohnella sp. A01: isolation and product optimization. Braz J Microbiol 47:931–940. https://doi.org/10.1016/j.bjm.2016.07.009 PubMed DOI PMC

Alias N, Mahadi NM, Murad AMA, Bakar FDA, Mahmood NAN, Illias MR (2009) Expression and characterization of Trichoderma virens UKM-1 endochitinase in Escherichia coli. World J Microbiol Biotechnol 25:561–572. https://doi.org/10.1007/s11274-008-9924-y DOI

Al-qwabah AA, Al-Limoun MO, Al-Mustafa AH, Al-Zereini WA (2018) Bacillus atrophaeus A7 crude chitinase: characterization and potential role against Drosophila melanogaster larvae. Jordan J Biol Sci 11:451–459

Al-Rashed SAA, Bakar FDA, Said M, Hassan O, Rabu A, Illias RM, Murad AMA (2010) Expression and characterization of the recombinant Trichoderma virens endochitinase Cht2. Afr J Microbiol Res 4:1758–1767

Alves TB, de Oliveira Ornela PH, de Oliveira AHC, Jorge JA, Guimaraes LHS (2018) Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation. 3 Biotech. https://doi.org/10.1007/s13205-018-1397-6

Aly MM, Tork S, Al-Garni SM, Kabli SA (2011) Chitinolytic enzyme production and genetic improvement of a new isolate belonging to Streptomyces anulatus. Ann Microbiol 61:453–461. https://doi.org/10.1007/s13213-010-0158-5 DOI

Andreini C, Bertini I, Cavallaro G, Holliday GL, Thornton JM (2008) Metal ions in biological catalysis: from enzyme databases to general principles. J Biol Inorg Chem 13:1205–1218. https://doi.org/10.1007/s00775-008-0404-5 PubMed DOI

Annamalai N, Giji S, Arumugam M, Balasubramanian T (2010) Purification and characterization of chitinase from Micrococcus sp. AG84 isolated from marine environment. Afr J Microbiol Res 4:2822–2827

Arai N, Shiomi K, Yamaguchi Y, Masuma R, Iwai Y, Tuberg A, Kolbl H, Omura S (2000) Argadin, a new chitinase inhibitor, produced by Clonostachys sp. FO-7314. Chem Pharm Bull 48:1442–1446 DOI

Arakane Y, Muthukrishnan S (2010) Insect chitinase and chitinase-like proteins. Cell Mol Life Sci 67:201–216. https://doi.org/10.1007/s00018-009-0161-9 PubMed DOI

Asril M, Mubarik NR, Wahyudi AT (2014) Partial purification of bacterial chitinase as biocontrol of leaf blight disease on oil palm. Res J Microbiol 9:265–277. https://doi.org/10.3923/jm.2014.265.277 DOI

Atalla SM, Gamal NGE, Awad HM (2020) Chitinase of marine Penicillium chrysogenum MH745129: isolation, identification, production and characterization as controller for citrus fruits postharvest pathogens. Jordan J Biol Sci 13:19–28

Aunpad R, Panbangred W (2003) Cloning and characterization of the constitutively expressed chitinase C gene from a marine bacterium, Salinivibrio costicola strain 5SM-1. J Biosci Bioeng 96:529–536. https://doi.org/10.1016/S1389-1723(04)70145-0 PubMed DOI

Awad GEA, Abdel Wahab WA, Hussein M, El-Diwany A, Esawy MA (2017) Sequential optimizations of Aspergillus awamori EM66 exochitinase and its application as biopesticide. J App Pharm Sci 7:67–75. https://doi.org/10.7324/JAPS.2017.70208 DOI

Barboza-Corona JE, Nieto-Mazzocco E, Velazquez-Robledo R, Salcedo-Hernandez R, Bautista M, Jimenez B, Ibarra JE (2003) Cloning, sequencing, and expression of the chitinase gene chiA74 from Bacillus thuringiensis. Appl Environ Microbiol 69:1023–1029. https://doi.org/10.1128/AEM.69.2.1023-1029.2003 PubMed DOI PMC

Beier S, Bertilsson S (2013) Bacterial chitin degradation-mechanisms and ecophysiological strategies. Front Microbiol 4:1–12. https://doi.org/10.3389/fmicb.2013.00149 DOI

Berini F, Caccia S, Franzetti E, Congiu T, Marinelli F, Casartelli M, Tettamanti G (2016) Effects of Trichoderma viride chitinases on the peritrophic matrix of Lepidoptera. Pest Manag Sci 72:980–989. https://doi.org/10.1002/ps.4078 PubMed DOI

Bhattacharya S, Das A, Samadder S, Rajan SS (2016) Biosynthesis and characterization of a thermostable, alkali-tolerant chitinase from Bacillus pumilus JUBCH08 displaying antagonism against phytopathogenic Fusarium oxysporum. 3 Biotech. https://doi.org/10.1007/s13205-016-0406-x

Binod P, Pusztahelyi T, Nagy V, Sandhya C, Szakacs G, Pocsi I, Pandey A (2005) Production and purification of extracellular chitinases from Penicillium aculeatum NRRL 2129 under solid-state fermentation. Enzyme Microb Technol 36:880–887. https://doi.org/10.1016/j.enzmictec.2004.12.031 DOI

Binod P, Sukumaran RK, Shirke SV, Rajput JC, Pandey A (2007) Evaluation of fungal culture filtrate containing chitinase as a biocontrol agent against Helicoverpa armigera. J Appl Microbiol 103:1845–1852. https://doi.org/10.1111/j.1365-2672.2007.03428.x PubMed DOI

Blackwell J, Parker KD, Rudall KM (1965) Chitin in pogonophore tubes. J Mar Biol Assoc UK 45:659–661. https://doi.org/10.1017/S0025315400016489 DOI

Blackwell J, Parker KD, Rudall KM (1967) Chitin fibers of the diatoms Thalassiosira fluviatilis and Cyclotella cryptica. J Mol Biol 28:383–385. https://doi.org/10.1016/s0022-2836(67)80018-4 PubMed DOI

Bo M, Bavestrello G, Kurek D, Paasch S, Brunner E, Born R, Galli R, Stelling AL, Sivkov VN, Petrova OV, Vyalikh D, Kummer K, Molodtsov SL, Nowak D, Nowak J, Ehrlich H (2012) Isolation and identification of chitin in the black coral Parantipathes larix (Anthozoa: Cnidaria). Int J Biol Macromol 51:129–137. https://doi.org/10.1016/j.ijbiomac.2012.04.016 PubMed DOI

Boldo JT, Junges A, do Amaral KB, Staats CC, Vainstein MH, Schrank A (2009) Endochitinase CHI2 of the biocontrol fungus Metarhizium anisopliae affects its virulence toward the cotton stainer bug Dysdercus peruvianus. Curr Genet 55:551–560. https://doi.org/10.1007/s00294-009-0267-5 PubMed DOI

Braconnot H (1811) De la fongine, ou analyse des champignons. Journal de Physique, de Chimie, d’Histoire Naturelle et des Arts. Paris: chez Courcier, Imprimeur-Libraire pour les mathématiques, tome LXXIII, pp 130–135

Braconnot H (1813) Nouvelles recherches analytiques sur la nature des champignons, pour servir de suite à celles qui ont été insérés dans les tomes LXXIX et LXXX des Annales de chimie. Annales de Chimie. In: Recueil de Mémoires concernant la chimie et les arts qui en dépendent et spécialement la pharmacie.odier Librairie des Ecoles Impériales Polytechnique et des Ponts et Chaussées, Paris. Klostermann J (ed) Annales de Chimie, tome soixante-dix-neuf, pp 237–270

Broadway RM, Wllllams DL, Kaln WC, Harman GE, Lorito M, Labeda DP (1995) Partial characterization of chitinolytic enzymes from Streptomyces albidoflavus. Lett Appl Microbiol 20:271–276. https://doi.org/10.1111/j.1472-765X.1995.tb00444.x PubMed DOI

Brzezinska MS, Donderski W (2001) Occurrence and activity of the chitinolytic bacteria of Aeromonas genus. Pol J Environ Stud 10:27–31

Brzezinska MS, Jankiewicz U (2012) Production of antifungal chitinase by Aspergillus niger LOCK 62 and its potential role in the biological control. Curr Microbiol 65:666–672. https://doi.org/10.1007/s00284-012-0208-2 PubMed DOI PMC

Brzezinska MS, Jankiewicz U, Kalwasinska A, Swiatczak J, Zero K (2019) Characterization of chitinase from Streptomyces luridiscabiei U05 and its antagonist potential against fungal plant pathogens. J Phytopathol 167:404–412. https://doi.org/10.1111/jph.12809 DOI

Brzezinska MS, Jankiewicz U, Lisiecki K (2013) Optimization of cultural conditions for the production of antifungal chitinase by Streptomyces sporovirgulis. Appl Biochem Microbiol 49:154–159. https://doi.org/10.1134/S0003683813020014 DOI

Carroad PA, Tom RA (1978) Bioconversion of shellfish chitin wastes: process conception and selection of microorganisms. J Food Sci 43:1158–1161. https://doi.org/10.1111/j.1365-2621.1978.tb15259.x DOI

Casadidio C, Peregrina DV, Gigliobianco MR, Deng S, Censi R, Di Martino P (2019) Chitin and chitosans: characteristics, eco-friendly processes, and applications in cosmetic science. Mar Drugs 17:369. https://doi.org/10.3390/md17060369 PubMed DOI PMC

Castillo BM, Dunn MF, Navarro KG, Melendez FH, Ortiz MH, Guevara SE, Palacios GH (2016) Antifungal performance of extracellular chitinases and culture supernatants of Streptomyces galilaeus CFFSUR-B12 against Mycosphaerella fijiensis Morelet. World J Microbiol Biotechnol. https://doi.org/10.1007/s11274-015-1993-0 PubMed DOI

Chandrasekaran R, Revathi K, Nisha S, Kirubakaran SA, Sathish-Narayanan S, Senthil-Nathan S (2012) Physiological effect of chitinase purified from Bacillus subtilis against the tobacco cutworm Spodoptera litura Fab. Pestic Biochem Physiol 104:65–71. https://doi.org/10.1016/j.pestbp.2012.07.002 DOI

Chang WT, Chen CS, Wang SL (2003) An antifungal chitinase produced by Bacillus cereus with shrimp and crab shell powder as a carbon source. Curr Microbiol 47:102–108. https://doi.org/10.1007/s00284-002-3955-7 PubMed DOI

Chang WT, Chen ML, Wang SL (2010) An antifungal chitinase produced by Bacillus subtilis using chitin waste as a carbon source. World J Microbiol Biotechnol 26:945–950. https://doi.org/10.1007/s11274-009-0244-7 DOI

Chen CC, Kumar HGA, Kumar S, Tzean SS, Yeh KW (2007) Molecular cloning, characterization, and expression of a chitinase from the entomopathogenic fungus Paecilomyces javanicus. Curr Microbiol 55:8–13. https://doi.org/10.1007/s00284-006-0405-y PubMed DOI

Chen W, Chen Q, Kumar A, Jiang X, Zhang KYJ, Yang Q (2021) Structure-based virtual screening of highly potent inhibitors of the nematode chitinase CeCht1. J Enzyme Inhib Med Chem 36:1198–1204. https://doi.org/10.1080/14756366.2021.1931862 PubMed DOI PMC

Chernin LS, De La Fuente L, Sobolev V, Haran S, Vorgias CE, Oppenheim AB, Chet I (1997) Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl Environ Microbiol 63:834–839 PubMed DOI PMC

Chigaleichik AG, Pirieva DA, Rylkin SS, Tiunova NA (1976) Biosynthesis of chitinase by Achromobacter liquefaciens. Mikrobiologiia 45:475–480 PubMed

Chrisnasari R, Verina D, Tapatfeto AC, Pranata S, Patjajani T, Wahjudi M, Purwanto MGM (2018) Isolating and characterising chitinolytic thermophilic bacteria from Cangar Hot Spring, East Java. Pertanika J Trop Agric Sci 41:1457–1468

Chu HH, Hoang V, Hofemeister J, Schrempf H (2001) A Bacillus amyloliquefaciens ChbB protein binds β- and α-chitin and has homologues in related strains. Microbiology 147:1793–1803. https://doi.org/10.1099/00221287-147-7-1793 PubMed DOI

Chung D, Baek K, Bae SS, Jung J (2019) Identification and characterization of a marine-derived chitinolytic fungus, Acremonium sp. YS2–2. J Microbiol 57:1–9. https://doi.org/10.1007/s12275-019-8469-0 DOI

Cronin D, Moenne-Loccoz Y, Dunne C, O’Gara F (1997) Inhibition of egg hatch of the potato cyst nematode Globodera rostochiensis by chitinase-producing bacteria. Eur J Plant Pathol 103:433–440. https://doi.org/10.1023/A:1008662729757 DOI

Cuong HN, Minh NC, Hoa NV, Trung TS (2016) Preparation and characterization of high purity β-chitin from squid pens (Loligo chenisis). Int J Biol Macromol 93:442–447. https://doi.org/10.1016/j.ijbiomac.2016.08.085 PubMed DOI

Dahiya N, Tewari R, Tiwari RP, Hoondal GS (2005) Production of an antifungal chitinase from Enerobacter sp. NRG4 and its application in protoplast production. World J Microbiol Biotechnol 21:1611–1616. https://doi.org/10.1007/s11274-005-8343-6 DOI

Danismazoglu M, Demir I, Sezen K, Muratoglu H, Nalcacioglu R (2015) Cloning and expression of chitinase A, B, and C (chiA, chiB, chiC) genes from Serratia marcescens originating from Helicoverpa armigera and determining their activities. Turk J Biol 39:78–87. https://doi.org/10.3906/biy-1404-31 DOI

Davies G, Henrissat B (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3:853–859. https://doi.org/10.1016/S0969-2126(01)00220-9 PubMed DOI

de Freitas Soares FE, de Queiroz JH, de Araujo JV, Queiroz PV, de Souza GA, Hiura E, Braga FR (2015) Nematicidal action of chitinases produced by the fungus Monacrosporium thaumasium under laboratorial conditions. Biocontrol Sci Technol 25:337–344. https://doi.org/10.1080/09583157.2014.979133 DOI

De Marco JL, Lima LHC, de Sousa MV, Felix CR (2000) A Trichoderma harzianum chitinase destroys the cell wall of the phytopathogen Crinipellis perniciosa, the causal agent of witches’ broom disease of cocoa. World J Microbiol Biotechnol 16:383–386. https://doi.org/10.1023/A:1008964324425 DOI

Draborg H, Christgau S, Halkier T, Rasmussen G, Dalboge H, Kauppinen S (1996) Secretion of an enzymatically active Trichoderma harzianum endochitinase by Saccharomyces cerevisiae. Curr Genet 29:404–409. https://doi.org/10.1007/BF02208622 PubMed DOI

Ehrlich H (2010) Chitin and collagen as universal and alternative templates in biomineralization. Int Geol Rev 52:661–699. https://doi.org/10.1080/00206811003679521 DOI

Ehrlich H, Krautter M, Hanke T, Simon P, Knieb C, Heinemann S, Worch H (2007) First evidence of the presence of chitin in skeletons of marine sponges. Part II. Glass sponges (Hexactinellida: Porifera). J Exp Zool (mol and Develop Evol) 308B:473–483. https://doi.org/10.1002/jez.b.21174 DOI

Ekundayo EA, Ekundayo FO, Bamidele F (2016) Production, partial purification and optimization of a chitinase produced from Trichoderma viride, an isolate of maize cob. Mycosphere 7:786–793. https://doi.org/10.5943/mycosphere/7/6/9 DOI

Ekundayo FO, Folorunsho AE, Ibisanmi TA, Olabanji OB (2022) Antifungal activity of chitinase produced by Streptomyces species isolated from grassland soils in Futa Area. Akure Bull Natl Res Cent 46:95. https://doi.org/10.1186/s42269-022-00782-4 DOI

Elieh-Ali-Komi D, Hamblin MR (2016) Chitin and chitosan: production and application of versatile biomedical nanomaterials. Int J Adv Res (indore) 4:411–427 PubMed

El-Katatny MH, Gudelj M, Robra KH, Elnaghy MA, Gubitz GM (2001) Appl Microbiol Biotechnol 56:137–143. https://doi.org/10.1007/s002530100646 PubMed DOI

El-Sayed ESA, Ezzat SM, Ghaly MF, Mansour M, El-Bohey MA (2000) Purification and characterization of two chitinases from Streptomyces albovinaceus S-22. World J Microbiol Biotechnol 16:87–89. https://doi.org/10.1023/A:1008926214392 DOI

El-Tarabily KA (2003) An endophytic chitinase-producing isolate of Actinoplanes missouriensis, with potential for biological control of root rot of lupin caused by Plectosporium tabacinum. Aust J Bot 51:257–266. https://doi.org/10.1071/BT02107 DOI

Escott GM, Adams DJ (1995) Chitinase activity in human serum and leucocytes. Infect Immun 63:4770–4773. https://doi.org/10.1128/iai.63.12.4770-4773.1995 PubMed DOI PMC

Evvyernie D, Morimoto K, Karita S, Kimura T, Sakka K, Ohmiya K (2001) Conversion of chitinous wastes to hydrogen gas by Clostridium paraputrificum M-21. J Biosci Bioeng 91:339–343. https://doi.org/10.1016/s1389-1723(01)80148-1 PubMed DOI

Farag AM, Abd-Elnabey HM, Ibrahim HAH, El-Shenawy M (2016) Purification, characterization and antimicrobial activity of chitinase from marine-derived Aspergillus terreus. Egyptian J Aquat Res 42:185–192. https://doi.org/10.1016/j.ejar.2016.04.004 DOI

Faramarzi MA, Fazeli M, Yazdi MT, Adrangi S, Al Ahmadi KJ, Tasharrofi N, Mohseni FA (2009) Optimization of cultural conditions for production of chitinase by a soil isolate of Massilia timonae. Biotechnol 8:93–99. https://doi.org/10.3923/biotech.2009.93.99 DOI

Fernandez-de Castro L, Mengibar M, Sanchez A, Arroyo L, Villaran MC, de Apodaca ED, Heras A (2016) Films of chitosan and chitosan-oligosaccharide neutralized and thermally treated: effects on its antibacterial and other activities. LWT-Food Sci Technol 73:368–374. https://doi.org/10.1016/j.lwt.2016.06.038 DOI

Fleuri LF, Kawaguti HY, Sato HH (2009) Production, purification and application of extracellular chitinase from Cellulosimicrobium cellulans 191. Braz J Microbiol 40:623–630. https://doi.org/10.1590/S1517-838220090003000026 PubMed DOI PMC

Frandberg E, Schnurer J (1994) Chitinolytic properties of Bacillus pabuli K1. J Appl Bacteriol 76:361–367. https://doi.org/10.1111/j.1365-2672.1994.tb01641.x PubMed DOI

Frankowski J, Lorito M, Scala F, Schmid R, Berg G, Bahl H (2001) Purification and properties of two chitinolytic ekolbenzymes of Serratia plymuthica HRO-C48. Arch Microbiol 176:421–426. https://doi.org/10.1007/s002030100347 PubMed DOI

Frederiksen RF, Paspaliari DK, Larsen T, Storgaard BG, Larsen MH, Ingmer H, Palcic MM, Leisner JJ (2013) Bacterial chitinases and chitin-binding proteins as virulence factors. Microbiology 159:833–847. https://doi.org/10.1099/mic.0.051839-0 PubMed DOI

Fu X, Yan Q, Wang J, Yang S, Jiang Z (2016) Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii. Int J Biol Macromol 91:973–979. https://doi.org/10.1016/j.ijbiomac.2016.06.050 PubMed DOI

Fuchs RL, McPherson SA, Drahos DJ (1986) Cloning of a Serratia marcescens gene encoding chitinase. Appl Environ Microbiol 51:504–509. https://doi.org/10.1128/aem.51.3.504-509.1986 PubMed DOI PMC

Furuhashi T, Schwarzinger C, Miksik I, Smrz M, Beran A (2009) Molluscan shell evolution with review of shell calcification hypothesis. Comp Biochem Physiol Part B 154:351–371. https://doi.org/10.1016/j.cbpb.2009.07.011 DOI

Gadelhak GG, El-Tarabily KA, Al-Kaabi FK (2005) Insect control using chitinolytic soil actinomycetes as biocontrol agents. Int J Agric Biol 7:627–633

Gan Z, Yang J, Tao N, Liang L, Mi Q, Li J, Zhang KQ (2007) Cloning of the gene Lecanicillium psalliotae chitinase Lpchi1 and identification of its potential role in the biocontrol of root-knot nematode Meloidogyne incognita. Appl Microbiol Biotechnol 76:1309–1317. https://doi.org/10.1007/s00253-007-1111-9 PubMed DOI

Gangwar M, Singh V, Pandey AK, Tripathi CKM, Mishra BN (2016) Purification and characterization of chitinase from Streptomyces violascens NRRL B2700. Indian J Exp Biol 54:64–71 PubMed

Gao J, Bauer MW, Shockley KR, Pysz MA, Kelly RM (2003) Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases. Appl Environ Microbiol 69:3119–3128. https://doi.org/10.1128/AEM.69.6.3119-3128.2003 PubMed DOI PMC

Gao L, Sun J, Secundo F, Gao X, Xue C, Mao X (2018) Cloning, characterization and substrate degradation mode of a novel chitinase from Streptomyces albolongus ATCC 27414. Food Chem 261:329–336. https://doi.org/10.1016/j.foodchem.2018.04.068 PubMed DOI

Garcia-Fraga B, Da Silva AF, Lopez-Seijas J, Sieiro C (2014) Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli. Appl Microbiol Biotechnol 98:2133–2143. https://doi.org/10.1007/s00253-013-5124-2 PubMed DOI

Gardner KH, Blackwell J (1975) Refinement of the structure of β-chitin. Biopolymers 14:1581–1595. https://doi.org/10.1002/bip.1975.360140804 PubMed DOI

Gautam SP, Gupta AK, Shrivastava R, Awasthi M (1996) Protoplast formation from the thermophilic fungus Malbranchea sulfurea, using the thermostable chitinase and laminarinase of Paecilomyces varioti. World J Microbiol Biotechnol 12:99–100. https://doi.org/10.1007/BF00327811 PubMed DOI

Ghanem KM, Al-Fassi FA, Farsi RM (2011) Statistical optimization of cultural conditions for chitinase production from shrimp shellfish waste by Alternaria alternata. Afr J Microbiol Res 5:1649–1659. https://doi.org/10.5897/AJMR11.255 DOI

Ghasemi S, Ahmadian G, Jelodar NB, Rahimian H, Ghandili S, Dehestani A, Shariati P (2010) Antifungal chitinases from Bacillus pumilus SG2: preliminary report. World J Microbiol Biotechnol 26:1437–1443. https://doi.org/10.1007/s11274-010-0318-6 DOI

Ghasemi Y, Dehdari Z, Mohkam M, Kargar M (2013) Isolation and optimization of cultivation conditions for production of chitinase by Aeromonas sp. ZD_05 from the Persian Gulf. J Pure Appl Micro 7:913–918

Gohel V, Chaudhary T, Vyas P, Chhatpar HS (2004) Isolation and identification of marine chitinolytic bacteria and their potential in antifungal biocontrol. Indian J Exp Biol 42:715–720 PubMed

Gomes RC, Semedo LTAS, Soares RMA, Linhares LF, Ulhoa CJ, Alviano CS, Coelho RRR (2001) Purication of a thermostable endochitinase from Streptomyces RC1071 isolated from a cerrado soil and its antagonism against phytopathogenic fungi. J Appl Microbiol 90:653–661. https://doi.org/10.1046/j.1365-2672.2001.01294.x PubMed DOI

Govindsamy V, Gunaratna KR, Balasubramanian R (1998) Properties of extracellular chitinase from Myrothecium verrucaria, an antagonist to the groundnut rust Puccinia arachidis. Can J Plant Pathol 20:62–68. https://doi.org/10.1080/07060669809500446 DOI

Gueye N, Kumar GK, Ndiaye M, Sall SYD, Ndiaye MAF, Diop TA, Ram MR (2020) Factors affecting the chitinase activity of Trichoderma asperellum isolated from agriculture field soils. J App Biol Biotech 8:41–44. https://doi.org/10.7324/JABB.2020.80207 DOI

Gunaratna KR, Balasubramanian R (1994) Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to the groundnut rust, Puccinia arachidis. World J Microbiol Biotechnol 10:342–345. https://doi.org/10.1007/BF00414876 PubMed DOI

Guo SH, Chen JK, Lee WC (2004) Purification and characterization of extracellular chitinase from Aeromonas schubertii. Enzyme Microb Technol 35:550–556. https://doi.org/10.1016/j.enzmictec.2004.08.025 DOI

Gupta CP, Kumar B, Dubey RC, Maheshwari DK (2006) Chitinase-mediated destructive antagonistic potential of Pseudomonas aeruginosa GRC DOI

Gupta R, Sxena RK, Chaturvedi P, Virdi JS (1995) Chitinase production by Streptomyces viridificans: its potential in fungal cell wall lysis. J Appl Bacteriol 78:378–383. https://doi.org/10.1111/j.1365-2672.1995.tb03421.x PubMed DOI

Gutierrez-Roman MI, Holguin-Melendez F, Dunn MF, Guillen-Navarro K, Huerta-Palacios G (2015) Antifungal activity of Serratia marcescens CFFSUR-B2 purified chitinolytic enzymes and prodigiosin against Mycosphaerella fijiensis, causal agent of black sigatoka in banana (Musa spp.). BioControl. https://doi.org/10.1007/s10526-015-9655-6

Hammami I, Siala R, Jridi M, Ktari N, Nasri M, Triki MA (2013) Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8. J Appl Microbiol 115:358–366. https://doi.org/10.1111/jam.12242 PubMed DOI

Han B, Zhou K, Li Z, Sun B, Ni Q, Meng X, Pan G, Li C, Long M, Li T, Zhou C, Li W, Zhou Z (2016) Characterization of the first fungal glycosyl hydrolase family 19 chitinase (NbchiA) from Nosema bombycis (Nb). J Eukaryot Microbiol 63:37–45. https://doi.org/10.1111/jeu.12246 PubMed DOI

Han Y, Yang B, Zhang F, Miao X, Li Z (2009) Characterization of antifungal chitinase from marine Streptomyces sp. DA11 associated with South China sea sponge Craniella australiensis. Mar Biotechnol 11:132–140. https://doi.org/10.1007/s10126-008-9126-5 DOI

Hao Z, Cai Y, Liao X, Zhang X, Fang Z, Zhang D (2012) Optimization of nutrition factors on chitinase production from a newly isolated Chitiolyticbacter meiyuanensis SYBC-H1. Braz J Microbiol 43:177–186. https://doi.org/10.1590/S1517-838220120001000019 PubMed DOI PMC

Harighi MJ, Zamani MR, Motallebi M (2007) Evaluation of antifungal activity of purified chitinase 42 from Trichoderma atroviride PTCC5220. Biotechnol 6:28–33. https://doi.org/10.3923/biotech.2007.28.33 DOI

Hashimoto M, Ikegami T, Seino S, Ohuchi N, Fukada H, Sugiyama J, Shirakawa M, Watanabe T (2000) Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J Bacteriol 182:3045–3054. https://doi.org/10.1128/JB.182.11.3045-3054.2000 PubMed DOI PMC

Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280:309–316. https://doi.org/10.1042/bj2800309 PubMed DOI PMC

Hiraga K, Shou L, Kitazawa M, Takahashi S, Shimada M, Sato R, Oda K (1997) Isolation and characterization of chitinase from a flake-chitin degrading marine bacterium, Aeromonas hydrophila H-2330. Biosci Biotech Biochem 61:174–176. https://doi.org/10.1271/bbb.61.174 DOI

Hoell IA, Klemsdal SS, Vaaje-Kolstad G, Horn SJ, Eijsink VGH (2005) Overexpression and characterization of a novel chitinase from Trichoderma atroviride strain P1. Biochem Biophys Acta 1748:180–190. https://doi.org/10.1016/j.bbapap.2005.01.002 PubMed DOI

Homthong M, Kubera A, Srihuttagum M, Hongtrakul V (2016) Isolation and characterization of chitinase from soil fungi, Paecilomyces sp. Agric Nat Resour 50:232–242. https://doi.org/10.1016/j.anres.2015.09.005 DOI

Horn SJ, Sorlie M, Vaaje-Kolstad G, Norberg AL, Synstad B, Varum KM, Eijsink VGH (2006) Comparative studies of chitinases A, B and C from Serratia marcescens. Biocatal Biotransfor 24:39–53. https://doi.org/10.1080/10242420500518482 DOI

Huang L, Shizume A, Nogawa M, Taguchi G, Shimosaka M (2012) Heterologus expression and functional charaterization of a novel chitinase from the chitinolytic bacteria Chitiniphilus shinanonensis. Biosci Biotechnol Biochem 76:517–522. https://doi.org/10.1271/bbb.110822 PubMed DOI

Ike M, Nagamatsu K, Shioya A, Nogawa M, Ogasawara W, Okada H, Morikawa Y (2006) Purification, characterization, and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli. Appl Microbiol Biotechnol 71:294–303. https://doi.org/10.1007/s00253-005-0171-y PubMed DOI

Iseli B, Armand S, Boller T, Neuhaus JM, Henrissat B (1996) Plant chitinases use two different hydrolytic mechanisms. FEBS Lett 382:186–188. https://doi.org/10.1016/0014-5793(96)00174-3 PubMed DOI

Islam SMA, Cho KM, Hong SJ, Math RK, Kim JM, Yun MG, Cho JJ, Heo JY, Lee YH, Kim H, Yun HD (2010) Chitinase of Bacillus licheniformis from oyster shell as a probe to detect chitin in marine shells. Appl Microbiol Biotechnol 86:119–129. https://doi.org/10.1007/s00253-009-2215-1 PubMed DOI

Itoh T, Kimoto H (2019) Bacterial chitinase system as a model of chitin biodegradation. In: Yang Q, Fukamizo T (eds) Targeting chitin-containing organisms, advances in experimental medicine and biology. Springer Nature Singapore Pte Ltd, pp 131–151

Jabeen F, Hussain A, Manzoor M, Younis T, Rasul A, Qazi JI (2018) Potential of bacterial chitinolytic, Stenotrophomonas maltophilia, in biological control of termites. Egypt J Biol Pest Control. https://doi.org/10.1186/s41938-018-0092-6 DOI

Jagadeeswari S, Selvam KP (2012) Optimization of chitinase production by soil Streptomyces sp. SJKP9. J Acad Indus Res 1:332–336

Jenin GA, Babu MM, Murugan M, Murugan T (2016) Isolation and identification of chitinase producing native fungi from saltpan of Puthalam, Kanyakumari District, Tamil Nadu, India. J Appl Biol Biotechnol 4:1–5. https://doi.org/10.7324/JABB.2016.40301 DOI

Jha S, Modi HA, Jha CK (2016) Characterization of extracellular chitinase produced from Streptomyces rubiginosus isolated from rhizosphere of Gossypium sp. Cogent Food Agric. https://doi.org/10.1080/23311932.2016.1198225 DOI

Jog R, Nareshkumar G, Rajkumar S (2012) Plant growth promoting potential and soil enzyme production of the most abundant Streptomyces spp. from wheat rhizosphere. J Appl Microbiol 113:1154–1164. https://doi.org/10.1111/j.1365-2672.2012.05417.x PubMed DOI

Joo GJ (2005) Purification and characterization of an extracellular chitinase from the antifungal biocontrol agent Streptomyces halstedii. Biotechnol Lett 27:1483–1486. https://doi.org/10.1007/s10529-005-1315-y PubMed DOI

Jung WJ, Jung SJ, An KN, Jin YL, Park RD, Kim KY, Shon BK, Kim TH (2002) Effect of chitinase-producing Paenibacillus illinoisensis KJA-424 on egg hatching of root-knot nematode (Meloidogyne incognita). J Microbiol Biotechnol 12:865–871

Kavitha A, Vijayalakshmi M (2011) Partial purification and antifungal profile of chitinase produced by Streptomyces tendae TK-VL_333. Ann Microbiol 61:597–603. https://doi.org/10.1007/s13213-010-0178-1 DOI

Kaya M, Mujtaba M, Ehrlich H, Salaberria AM, Baran T, Amemiya CT, Galli R, Akyuz L, Sargin I, Labidi J (2017) On chemistry of γ-chitin. Carbohydr Polym 176:177–186. https://doi.org/10.1016/j.carbpol.2017.08.076 PubMed DOI

Khan A, Williams KL, Nevalainen HKM (2004) Effects of Paecilomyces lilacinus protease and chitinase on the eggshell structures and hatching of Meloidogyne javanica juveniles. Biol Control 31:346–352. https://doi.org/10.1016/j.biocontrol.2004.07.011 DOI

Khatri DK, Tiwari DN, Bariya HS (2017) Chitinolytic efficacy and secretion of cell wall-degrading enzymes from Trichoderma spp. in response to phytopathological fungi. J Appl Biol Biotechnol 5:1–8. https://doi.org/10.7324/JABB.2017.50601 DOI

Kim KJ, Yang YJ, Kim JG (2003) Purification and characterization of chitinase from Streptomyces sp. M-20. J Biochem Mol Bio 36:185–189. https://doi.org/10.5483/bmbrep.2003.36.2.185 DOI

Kishore GK, Pande S (2007) Chitin-supplemented foliar application of chitinolytic Bacillus cereus reduces severity of Botrytis gray mold disease in chickpea under controlled conditions. Lett Appl Microbiol 44:98–105. https://doi.org/10.1111/j.1472-765X.2006.02022.x PubMed DOI

Kishore GK, Pande S, Podile AR (2005) Biological control of late leaf spot of peanut (Arachis hypogaea) with chitinolytic bacteria. Phytopathol 95:1157–1165. https://doi.org/10.1094/PHYTO-95-1157 DOI

Kolbe S, Fischer S, Becirevic A, Hinz P, Schrempf H (1998) The Streptormyces reticuli α-chitin-binding protein CHB2 and its gene. Microbiology 144:1291–1297 PubMed DOI

Kong H, Shimosaka M, Ando Y, Nishiyama K, Fujii T, Miyashita K (2001) Species-specific distribution of a modular family 19 chitinase gene in Burkholderia gladioli. FEMS Microbiol Ecol 37:135–141. https://doi.org/10.1111/j.1574-6941.2001.tb00861.x DOI

Korany SM, Mansour AN, El-Hendawy HH, Kobisi ANA, Aly HH (2019) Entomopathogenic efficacy of the chitinolytic bacteria: Aeromonas hydrophila isolated from Siwa Oasis, Egypt. Egypt J Biol Pest Control. https://doi.org/10.1186/s41938-019-0116-x

Kramer KJ, Koga D (1986) Insect chitin: physical state, synthesis, degradation and metabolic regulation. Insect Biochem 16:851–877. https://doi.org/10.1016/0020-1790(86)90059-4 DOI

Krishnaveni B, Ragunathan R (2014) Chitinase production from marine wastes by Aspergillus terreus and its application in degradation studies. Int J Curr Microbiol App Sci 3:76–82

Kuddus SM, Ahmad RIZ (2013) Isolation of novel chitinolytic bacteria and production optimization of extracellular chitinase. J Genet Eng Biotechnol 11:39–46. https://doi.org/10.1016/j.jgeb.2013.03.001 DOI

Lacombe-Harvey ME, Brzezinski R, Beaulieu C (2018) Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution. Appl Microbiol Biotechnol 102:7219–7230. https://doi.org/10.1007/s00253-018-9149-4 PubMed DOI PMC

Langner T, Gohre V (2016) Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions. Curr Genet 62:243–254. https://doi.org/10.1007/s00294-015-0530-x PubMed DOI

Lee HJ, Lee YS, Choi YL (2018) Cloning, purifcation, and characterization of an organic solvent-tolerant chitinase, MtCh509, from Microbulbifer thermotolerans DAU221. Biotechnol Biofuels. https://doi.org/10.1186/s13068-018-1299-1 PubMed DOI PMC

Lee YS, Kim KY (2015) Statistical optimization of medium components for chitinase production by Pseudomonas fluorescens strain HN1205: role of chitinase on egg hatching inhibition of root-knot nematode. Biotechnol Biotechnol Equip 29:470–478. https://doi.org/10.1080/13102818.2015.1010702 DOI

Lee YS, Nguyen XH, Naing KW, Park YS, Kim KY (2014) Role of lytic enzymes secreted by Lysobacter capsici YS1215 in the control of root-knot nematode of tomato plants. Indian J Microbiol. https://doi.org/10.1007/s12088-014-0499-z PubMed DOI PMC

Li S, Zhang B, Zhu H, Zhu T (2018) Cloning and expression of the chitinase encoded by ChiKJ406136 from Streptomyces Sampsonii (Millard & Burr) Waksman KJ40 and its antifungal effect. Forests. https://doi.org/10.3390/f9110699 DOI

Liaqat F, Eltem R (2018) Chitooligosaccharides and their biological activities: a comprehensive review. Carbohydr Polym 184:243–259. https://doi.org/10.1016/j.carbpol.2017.12.067 PubMed DOI

Lima LHC, Ulhoa CJ, Fernandes AP, Felix CR (1997) Purification of a chitinase from Trichoderma sp. and its action on Sclerotium rolfsii and Rhizoctonia solani cell walls. J Gen Appl Microbiol 43:31–37. https://doi.org/10.2323/jgam.43.31 PubMed DOI

Liu CL, Shen CR, Hsu FF, Chen JK, Wu PT, Guo SH, Lee WC, Yu FW, Mackey ZB, Turk J, Gross ML (2009) Isolation and identification of two novel SDS-resistant secreted chitinases from Aeromonas schubertii. Biotechnol Prog 25:124–131. https://doi.org/10.1002/btpr.100 PubMed DOI PMC

Liu K, Ding H, Yu Y, Chen B (2019) A cold-adapted chitinase-producing bacterium from Antarctica and its potential in biocontrol of plant pathogenic fungi. Mar Drugs. https://doi.org/10.3390/md17120695 PubMed DOI PMC

Liu P, Cheng D, Miao L (2015) Characterization of thermotolerant chitinases encoded by a Brevibacillus laterosporus strain isolated from a suburban wetland. Genes 6:1268–1282. https://doi.org/10.3390/genes6041268 PubMed DOI PMC

Liu ZH, Yang Q, Hu S, Zhang JD, Ma J (2008) Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity. Appl Microbiol Biotechnol 80:241–252. https://doi.org/10.1007/s00253-008-1543-x PubMed DOI

Loc NH, Hoa NTQ, Cuc PTK, Quang HT (2013) Expression of chitinase (chi42) gene from Trichoderma asperellum in Saccharomyces cerevisiae. Ann Biol Res 4:15–19

Lonhienne T, Mavromatis K, Vorgias CE, Buchon L, Gerday C, Bouriotis V (2001) Cloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes. J Bacteriol 183:1773–1779. https://doi.org/10.1128/JB.183.5.1773-1779.2001 PubMed DOI PMC

Loni PP, Patil JU, Phugare SS, Bajekal SS (2014) Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis NCIM 5434. J Basic Microbiol 53:1–10. https://doi.org/10.1002/jobm.201300533 DOI

Lu Y, Wang N, He J, Li Y, Gao X, Huang L, Yan X (2018) Expression and characterization of a novel chitinase with antifungal activity from a rare actinomycete, Saccharothrix yanglingensis Hhs. 015. Protein Expr Purif 143:45–51. https://doi.org/10.1016/j.pep.2017.10.013 PubMed DOI

Makhdoumi A, Dehghani-Joybari Z, Mashreghi M, Jamialahmadi K, Asoodeh A (2015) A novel halo-alkali-tolerant and thermo-tolerant chitinase from Pseudoalteromonas sp. DC14 isolated from the Caspian Sea. Int J Environ Sci Technol 12:3895–3904. https://doi.org/10.1007/s13762-015-0848-4 DOI

Mander P, Cho SS, Choi YH, Panthi S, Choi YS, Kim HM, Yoo JC (2016) Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242. Arch Pharm Res. https://doi.org/10.1007/s12272-016-0747-3 PubMed DOI

Mansour SH, Abdel-Fattah AM, Esawy M, Ahmed EF, Haroun AA, Hussein MA, Hassanien NM, Khater HM (2019) Immobilization, thermodynamic studies and application of chitinase enzyme from Penicillium chrysogenum. Egypt J Aquat Biol Fish 23:527–544. https://doi.org/10.21608/EJABF.2019.48698 DOI

Mathivanan N, Kabilan V, Murugesan K (1998) Purification, characterization, and antifungal activity of chitinase from Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis. Can J Microbiol 44:646–651 PubMed DOI

Mathur A, Rawat A, Bhatt G, Baweja S, Ahmad F, Grover A, Madhav K, Dhand M, Mathur D, Verma SK, Singh SK, Dua VK (2011) Isolation of Bacillus producing chitinase from soil: production and purification of chito-oligosaccharides from chitin extracted from fresh water crustaceans and antimicrobial activity of chitinase. Recent Res Sci Technol 3:1–6

Mehmood MA, Gai Y, Zhuang Q, Wang F, Xiao X, Wang F (2010) Aeromonas caviae CB101 contains four chitinases encoded by a single Gene chi1. Mol Biotechnol 44:213–220. https://doi.org/10.1007/s12033-009-9227-z PubMed DOI

Mehmood MA, Xiao X, Hafeez FY, Gai Y, Wang F (2011) Molecular characterization of the modular chitin binding protein Cbp50 from Bacillus thuringiensis serovar konkukian. Antonie Van Leeuwenhoek 100:445–453. https://doi.org/10.1007/s10482-011-9601-2 PubMed DOI

Meng H, Wang Z, Meng X, Xie L, Huang B (2015) Cloning and expression analysis of the chitinase gene Ifu-chit2 from Isaria fumosorosea. Genet Mol Biol 38:381–389. https://doi.org/10.1590/S1415-475738320150003 PubMed DOI PMC

Mercer CF, Greenwood DR, Grant JL (1992) Effect of plant and microbial chitinases on the eggs and juveniles of Meloidogyne hapla Chitwood (Nematoda: Tylenchida). Nematologica 38:227–236 DOI

Merzendorfer H, Zimoch L (2003) Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J Exp Biol 206:4393–4412. https://doi.org/10.1242/jeb.00709 PubMed DOI

Mishra P, Kshirsagar PR, Nilegaonkar SS, Singh SK (2012) Statistical optimization of medium components for production of extracellular chitinase by Basidiobolus ranarum: a novel biocontrol agent against plant pathogenic fungi. J Basic Microbiol 52:1–10. https://doi.org/10.1002/jobm.201100446 DOI

Mohamed S, Bouacem K, Mechri S, Addou NA, Laribi-Habchi H, Fardeau ML, Jaouadi B, Bouanane-Darenfed A, Hacene H (2019) Purification and biochemical characterization of a novel acido-halotolerant and thermostable endochitinase from Melghiribacillus thermohalophilus strain Nari2A PubMed DOI

Mohan K, Muralisankar T, Jayakumar R, Rajeevgandhi C (2021) A study on structural comparisons of α-chitin extracted from marine crustacean shell waste. Carbohydr Polym Technol App. https://doi.org/10.1016/j.carpta.2021.100037 DOI

Mondal S, Baksi S, Koris A, Vatai G (2016) Journey of enzymes in entomopathogenic fungi. Pac Sci Rev a: Nat Sci Eng 18:85–99. https://doi.org/10.1016/j.psra.2016.10.001 DOI

Monreal J, Reese ET (1969) The chitinase of Serratia marcescens. Can J Microbiol 15:689–696 PubMed DOI

Morimoto K, Karita S, Kimura T, Sakka K, Ohimya K (1997) Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J Bacteriol 179:7306–7314. https://doi.org/10.1128/jb.179.23.7306-7314.1997 PubMed DOI PMC

Morrissey RF, Dugan EP, Koths JS (1976) Chitinase production by an Arthrobacter sp. lysing cells of Fusarium roseum. Soil Biol Biochem 8:23–28 DOI

Mubarik NR, Mahagiani I, Anindyaputri A, Santoso S, Rusmana I (2010) Chitinolytic bacteria isolated from chili rhizosphere: chitinase characterization and its application as biocontrol for whitefly (Bemisia tabaci Genn.). Am J Agri & Biol Sci 5:430–435 DOI

Mukherjee G, Sen SK (2006) Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P PubMed DOI

Nagpure A, Gupta RK (2012) Purification and characterization of an extracellular chitinase from antagonistic Streptomyces violaceusniger. J Basic Microbiol 52:1–11. https://doi.org/10.1002/jobm.201100648 DOI

Narayana KJP, Vijayalakshmi M (2009) Chitinase production by Streptomyces sp. ANU 6277. Bra J Microbiol 40:725–733. https://doi.org/10.1590/S1517-83822009000400002 DOI

Naveed M, Phil L, Sohail M, Hasnat M, Baig MMFA, Ihsan AU, Shumzaid M, Kakar MU, Khan TM, Akabar MD, Hussain MI, Zhou QG (2019) Chitosan oligosaccharide (COS): an overview. Int J Biol Macromol 129:827–843. https://doi.org/10.1016/j.ijbiomac.2019.01.192 PubMed DOI

Nawani NN, Kapadnis BP, Das AD, Rao AS, Mahajan SK (2002) Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2. J Appl Microbiol 93:965–975. https://doi.org/10.1046/j.1365-2672.2002.01766.x PubMed DOI

Nayak SK, Nayak S, Mohanty S, Sundaray JK, Mishra BB (2021) Microbial chitinases and their applications: an overview. Mishra BB, Nayak SK, Mohapatra S, Samantaray D (eds) Environmental and agricultural microbiology: applications for sustainability. Scrivener Publishing LLC, Wiley Online Library, pp 313–340

Nguyen NV, Kim YJ, Oh KT, Jung WJ, Park RD (2007) The role of chitinase from Lecanicillium antillanum B-3 in parasitism to root-knot nematode Meloidogyne incognita eggs. Biocontrol Sci Technol 17:1047–1058. https://doi.org/10.1080/09583150701668658 DOI

Odier A (1823) Mémoire sur la composition chimique des parties cornées des insectes. Mémoires de la Société d’Histoire Naturelle de Paris. Paris: Baudouin Frères Libraires-Éditeurs, tome premier, pp 29–42

Ogawa K, Yoshida N, Kariya K, Ohnishi C, Ikeda R (2002) Purification and characterization of a novel chitinase from Burkholderia cepacia strain KH2 isolated from the bed log of Lentinus edodes, Shiitake mushroom. J Gen Appl Microbiol 48:25–33. https://doi.org/10.2323/jgam.48.25 PubMed DOI

Ohishi K, Yamagishi M, Ohta T, Suzuki M, Izumida H, Sano H, Nishijima M, Miwa T (1996) Purification and properties of two chitinases from Vibrio alginolyticus H-8. J Ferment Bioeng 82:598–600. https://doi.org/10.1016/S0922-338X(97)81260-3 DOI

Ohno T, Armand S, Hata T, Nikaidou N, Henrissat B, Mitsutomi M, Watanabe T (1996) A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. J Bacteriol 178:5065–5070. https://doi.org/10.1128/jb.178.17.5065-5070.1996 PubMed DOI PMC

Okazaki K, Tagawa K (1991) Purification and properties of chitinase from Streptomyces cinereoruber. J Ferment Bioeng 71:237–241. https://doi.org/10.1016/0922-338X(91)90274-K DOI

Oku T, Ishikawa K (2006) Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: activity towrds crystalline chitin. Biosci Biotechnol Biochem 70:1696–1701. https://doi.org/10.1271/bbb.60031 PubMed DOI

Omura S, Arai N, Yamaguchi Y, Masuma R, Iwai Y, Namikoshi M, Turberg A, Kolbl H, Shiomi K (2000) Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668. J Antibiot 53:603–608. https://doi.org/10.7164/antibiotics.53.603 DOI

Ordentlich A, Elad Y, Chet I (1988) The role of chitinase of Serretia marcescens in biocontrol of Sclerotium rolfsii. Phytopathology 78:84–88

Orikoshi H, Baba N, Nakayama S, Kashu H, Miyamoto K, Yasuda M, Inamori Y, Tsujibo H (2003) Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7. J Bacteriol 185:1153–1160. https://doi.org/10.1128/JB.185.4.1153-1160.2003 PubMed DOI PMC

Pandya U, Saraf M (2015) Purification and characterization of antifungal chitinase from Bacillus safensis MBCU6 and its application for production of chito-oligosaccharides. Biologia 70:863–868. https://doi.org/10.1515/biolog-2015-0112 DOI

Paoletti MG, Norberto L, Damini R, Musumeci S (2007) Human gastric juice contains chitinase that can degrade chitin. Ann Nutr Metab 51:244–251. https://doi.org/10.1159/000104144 PubMed DOI

Park HJ, Kim D, Kim IH, Lee CE, Kim IC, Kim JY, Kim SJ, Lee HK, Yim JH (2009) Characteristics of cold-adaptive endochitinase from Antarctic bacterium Sanguibacter antarcticus KOPRI 21702. Enzyme Microb Technol 45:391–396. https://doi.org/10.1016/j.enzmictec.2009.07.002 DOI

Park JK, Morita K, Fukumoto I, Yamasaki Y, Nakagawa T, Kawamukai M, Matsuda H (1997) Purification and characterization of the chitinase (ChiA) from Enterobacter sp. G-1. Biosci Biotech Biochem 61:684–689. https://doi.org/10.1271/bbb.61.684 DOI

Park JO, El-Tarabily KA, Ghisalberti EL, Sivasithamparam K (2002) Pathogenesis of Streptoverticillium albireticuli on Caenorhabditis elegans and its antagonism to soil-borne fungal pathogens. Lett Appl Microbiol 35:361–365. https://doi.org/10.1046/j.1472-765x.2002.01194.x PubMed DOI

Pasqualetti M, Barghini P, Giovannini V, Fenice M (2019) High production of chitinolytic activity in halophilic conditions by a new marine strain of Clonostachys rosea. Molecules. https://doi.org/10.3390/molecules24101880 PubMed DOI PMC

Patidar P, Agrawal D, Banerjee T, Patil S (2005) Optimisation of process parameters for chitinase production by soil isolates of Penicillium chrysogenum under solid substrate fermentation. Process Biochem 40:2962–2967. https://doi.org/10.1016/j.procbio.2005.01.013 DOI

Patil NS, Jadhav JP (2014) Single cell protein production using Penicillium ochrochloron chitinase and its evaluation in fish meal formulations. J Microbial Biochem Technol. https://doi.org/10.4172/1948-5948.S4-005 DOI

Patil NS, Waghmare SR, Jadhav JP (2013) Purification and characterization of an extracellular antifungal chitinase from Penicillium ochrochloron MTCC 517 and its application in protoplast formation. Process Biochem 48:176–183. https://doi.org/10.1016/j.procbio.2012.11.017 DOI

Pattanapipitpaisal P, Kamlandharn R (2012) Screening of chitinolytic actinomycetes for biological control of Sclerotium rolfsii stem rot disease of chilli. Songklanakarin J Sci Technol 34:387–393

Percot A, Viton C, Domard A (2003) Optimization of chitin extraction from shrimp shells. Biomacromol 4:12–18 DOI

Pleban S, Chernin L, Chet I (1997) Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett Appl Microbiol 25:284–288. https://doi.org/10.1046/j.1472-765x.1997.00224.x PubMed DOI

Ploydee E, Chaiyanan S (2014) Production of high viscosity chitosan from biologically purified chitin isolated by microbial fermentation and deproteinization. Int J Polym Sci 2014:1–8 DOI

Prasad M, Palanivelu P (2012) Overexpression of a chitinase gene from the thermophilic fungus, Thermomyces lanuginosus in Saccharomyces cerevisiae and characterization of the recombinant chitinase. J Microb Biochem Technol. https://doi.org/10.4172/1948-5948.1000076

Prasanna L, Eijsink VGH, Meadow R, Gaseidnes S (2013) A novel strain of Brevibacillus laterosporus produces chitinases that contribute to its biocontrol potential. Appl Microbiol Biotechnol 97:1601–1611. https://doi.org/10.1007/s00253-012-4019-y PubMed DOI

Proespraiwong P, Tassanakajon A, Rimphanitchayakit V (2010) Chitinases from the black tiger shrimp Penaeus monodon: phylogenetics, expression and activities. Comp Biochem Physiol Part B 156:86–96. https://doi.org/10.1016/j.cbpb.2010.02.007 DOI

Purushotham P, Arun PVPS, Prakash JSS, Podile AR (2012) Chitin binding proteins act synergistically with chitinases in Serratia proteamaculans 568. PLoS ONE. https://doi.org/10.1371/journal.pone.0036714 PubMed DOI PMC

Pusztahelyi T (2018) Chitin and chitin-related compounds in plant-fungal interactions. Mycology. https://doi.org/10.1080/21501203.2018.1473299 PubMed DOI PMC

Rabeeth M, Anitha A, Srikanth G (2011) Purification of an antifungal endochitinase from a potential biocontrol agent Streptomyces griseus. Pak J Biol Sci 14:788–797. https://doi.org/10.3923/pjbs.2011.788.797 PubMed DOI

Rahman MA, Halfar J (2014) First evidence of chitin in calcified coralline algae: new insights into the calcification process of Clathromorphum compactum. Sci Rep. https://doi.org/10.1038/srep06162 PubMed DOI PMC

Rajan LA, Dharini J, Singh KHP, Sivvaswaamy SN, Sheela JS, Sundar N (2010) Identification, cloning and sequence analysis of chitinase gene in Bacillus halodurans isolated from salted fish. Biotechnol 9:229–233. https://doi.org/10.3923/biotech.2010.229.233 DOI

Ramli ANM, Mahadi NM, Rabu A, Murad AMA, Bakar FDA, Illias RM (2011) Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12. Microb Cell Fact 10:94. https://doi.org/10.1186/1475-2859-10-94 PubMed DOI PMC

Rashad YM, Al-Askar AA, Ghoneem KM, Saber WIA, Hafez EE (2017) Chitinolytic Streptomyces griseorubens E44G enhances the biocontrol efficacy against Fusarium wilt disease of tomato. Phytoparasitica 45:227–237. https://doi.org/10.1007/s12600-017-0580-3 DOI

Rawway M, Beltagy EA, Abdul-Raouf UM, Elshenawy MA, Kelany MS (2018) Optimization of process parameters for chitinase production by a marine Aspergillus flavus MK20. J Eco Heal Env 6:1–8. https://doi.org/10.18576/jehe/060101 DOI

Ray L, Panda AN, Mishra SR, Pattanaik AK, Adhya TK, Suar M, Raina V (2019) Purification and characterization of an extracellular thermo-alkali stable, metal tolerant chitinase from Streptomyces chilikensis RC1830 isolated from a brackish water lake sediment. Biotechnol Rep. https://doi.org/10.1016/j.btre.2019.e00311 DOI

Reguera G, Leschine SB (2003) Biochemical and genetic characterization of ChiA, the major enzyme component for the solubilization of chitin by Cellulomonas uda. Arch Microbiol 180:434–443. https://doi.org/10.1007/s00203-003-0611-y PubMed DOI

Reisert PS (1972) Studies of the chitinase system of Chytriomyces hyalinus using a C PubMed DOI

Ren XB, Dang YR, Liu SS, Huang KX, Qin QL, Chen XL, Zhang YZ, Wang YJ, Li PY (2022) Identification and characterization of three chitinases with potential in direct conversion of crystalline chitin into N, N′-diacetylchitobiose. Mar Drugs 20:165. https://doi.org/10.3390/md20030165 PubMed DOI PMC

Revah-Moiseev S, Carroad PA (1981) Conversion of the enzymatic hydrolysate of shellfish waste chitin to single-cell protein. Biotechnol Bioeng 23:1067–1078. https://doi.org/10.1002/bit.260230514 DOI

Reyes-Ramirez A, Escudero-Abarca BI, Aguilar-Uscanga G, Hayward-Jones PM, Barboza-Corona JE (2004) Antifungal activity of Bacillus thuringiensis chitinase and its potential for the biocontrol of phytopathogenic fungi in soybean seeds. J Food Sci 69:131–134. https://doi.org/10.1111/j.1365-2621.2004.tb10721.x DOI

Rishad KS, Rebello S, Shabanamol PS, Jisha MS (2017) Biocontrol potential of halotolerant bacterial chitinase from high yielding novel Bacillus pumilus MCB-7 autochthonous to mangrove ecosystem. Pest Biochem Physiol 137:36–41. https://doi.org/10.1016/j.pestbp.2016.09.005 DOI

Rodriguez-Kabana R, Godoy G, Morgan-Jones G, Shelby RA (1983) The determination of soil chitinase activity: conditions for assay and ecological studies. Plant Soil 75:95–106. https://doi.org/10.1007/BF02178617 DOI

Roy JC, Salaun F, Giraud S, Ferri A, Chen G, Guan J (2017) Solubility of chitin: solvents, solution behaviors and their related mechanisms. In: Xu Z (ed) Solubility of polysaccharides. IntechOpen, Vienna, Austria, pp 109–127

Rudall KM (1969) Chitin and its association with other molecules. J Polymer Sci Part C 28:83–102. https://doi.org/10.1002/polc.5070280110 DOI

Saadoun I, Al-Omari R, Jaradat Z, Ababneh Q (2009) Influence of culture conditions of Streptomyces sp. (strain S PubMed

Sakuda S, Inoue H, Nagasawa H (2013) Novel biological activities of allosamidins. Molecules 18:6952–6968. https://doi.org/10.3390/molecules18066952 PubMed DOI PMC

Sakuda S, Isogai A, Matsumoto S, Suzuki A, Koseki K (1986) The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett 27:2475–2478. https://doi.org/10.1016/S0040-4039(00)84560-8 DOI

Sakurada M, Morgavi DP, Komatani K, Tomita Y, Onodera R (1997) Purification and characteristics of an autolytic chitinase of Piromyces communis OTS1 from culture medium. Curr Microbiol 35:48–51. https://doi.org/10.1007/s002849900210 PubMed DOI

Salam M, Dahiya N, Sharma R, Soni SK, Hoondal GS, Tewari R (2008) Cloning, characterization and expression of the chitinase gene of Enterobacter sp. NRG4. Indian J Microbiology 48:358–364. https://doi.org/10.1007/s12088-008-0044-z DOI

Sampson MN, Gooday GW (1998) Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects. Microbiology 144:2189–2194. https://doi.org/10.1099/00221287-144-8-2189 PubMed DOI

Seidl V (2008) Chitinases of filamentous fungi: a large group of diverse proteins with multiple physiological functions. Fungal Biol Rev 22:36–42. https://doi.org/10.1016/j.fbr.2008.03.002 DOI

Seidl V, Huemer B, Seiboth B, Kubicek CP (2005) A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J 272:5923–5939. https://doi.org/10.1111/j.1742-4658.2005.04994.x PubMed DOI

Seidl-Seiboth V, Zach S, Frischmann A, Spadiut O, Dietzsch C, Herwig C, Ruth C, Rodler A, Jungbauer A, Kubicek CP (2013) Spore germination of Trichoderma atroviride is inhibited by its LysM protein TAL6. FEBS J 280:1226–1236. https://doi.org/10.1111/febs.12113 PubMed DOI

Senol M, Nadaroglu H, Dikbas N, Kotan R (2014) Purification of chitinase enzymes from Bacillus subtilis bacteria TV-125, investigation of kinetic properties and antifungal activity against Fusarium culmorum. Ann Clin Microbiol Antimicrob 13:35. https://doi.org/10.1186/s12941-014-0035-3 PubMed DOI PMC

Seo DJ, Lee YS, Kim KY, Jung WJ (2016) Antifungal activity of chitinase obtained from Paenibacillus ehimensis MA2012 against conidial of Collectotrichum gloeosporioides in vitro. Microb Pathog 96:10–14. https://doi.org/10.1016/j.micpath.2016.04.016 PubMed DOI

Shaikh SS, Wani SJ, Sayyed RZ, Thakur R, Gulati A (2018) Production, purification and kinetics of chitinase of Stenotrophomonas maltophilia isolated from rhizospheric soil. Indian J Exp Biol 56:274–278

Shali A, Ghasemi S, Ahmadian G, Ranjbar G, Dehestani A, Khalesi N, Motallebi E, Vahed M (2010) Bacillus pumilus SG2 chitinases induced and regulated by chitin, show inhibitory activity against Fusarium graminearum and Bipolaris sorokiniana. Phytoparasitica 38:141–147. https://doi.org/10.1007/s12600-009-0078-8 DOI

Shanmugaiah V, Mathivanan N, Balasubramanian N, Manoharan PT (2008) Optimization of cultural conditions for production of chitinase by Bacillus laterosporous MML2270 isolated from rice rhizosphere soil. Afr J Biotechnol 7:2562–2568

Shapira R, Ordentlich A, Chet I, Oppenheim AB (1989) Control of plant diseases by chitinase expressed from cloned DNA in Escherichia coli. Phytopathology 79:1246–1249. https://doi.org/10.1094/Phyto-79-1246 DOI

Sharaf EF (2005) A potent chitinolytic activity of Alternaria alternata isolated from Egyptian black sand. Pol J Microbiol 54:145–151 PubMed

Sharma S, Kumar S, Khajuria A, Ohri P, Kaur R, Kaur R (2020) Biocontrol potential of chitinases produced by newly isolated Chitinophaga sp. S167. World J Microbiol Biotechnol. https://doi.org/10.1007/s11274-020-02864-9

Sharma V, Shanmugam V (2011) Purification and characterization of an extracellular 24 kDa chitobiosidase from the mycoparasitic fungus Trichoderma saturnisporum. J Basic Microbiol 51:1–8. https://doi.org/10.1002/jobm.201100145 DOI

Shehata AN, Abd El Aty AA, Darwish DA, Abdel Wahab WA, Mostafa FA (2018) Purification, physicochemical and thermodynamic studies of antifungal chitinase with production of bioactive chitosan-oligosaccharide from newly isolated Aspergillus griseoaurantiacus KX010988. Int J Biol Macromol 107:990–999. https://doi.org/10.1016/j.ijbiomac.2017.09.071 PubMed DOI

Shimosaka M, Fukumori Y, Narita T, Zhang XY, Kodaira R, Nogawa M, Okazaki M (2001) The bacterium Burkholderia gladioli strain CHB101 produces two different kinds of chitinases belonging to families 18 and 19 of the glycosyl hydrolases. J Biosci Bioeng 91:103–105. https://doi.org/10.1263/jbb.91.103 PubMed DOI

Shivalee A, Lingappa K, Mahesh D (2018) Influence of bioprocess variables on the production of extracellular chitinase under submerged fermentation by Streptomyces pratensis strain KLSL55. J Genet Eng Biotechnol 16:421–426. https://doi.org/10.1016/j.jgeb.2017.12.006 PubMed DOI PMC

Simunek J, Kopecny J, Hodrova B, Bartonova H (2002) Identification and characterization of Clostridium paraputrificum, a chitinolytic bacterium of human digestive tract. Folia Microbiol 47:559–564. https://doi.org/10.1007/BF02818798 DOI

Sonawane KD, Dandagal NR, Naikwadi AG, Gurav PT, Anapat SV, Nadaf NH, Jadhav DB, Waghmare SR (2016) Intergeneric fusant development using chitinase preparation of Rhizopus stolonifer NCIM 880. AMB Expr 6:114. https://doi.org/10.1186/s13568-016-0287-8 DOI

Song YS, Seo DJ, Jung WJ (2017) Identification, purification, and expression patterns of chitinase from psychrotolerant Pedobacter sp. PR-M6 and antifungal activity in vitro. Microb Pathog 107:62–68. https://doi.org/10.1016/j.micpath.2017.03.018 PubMed DOI

Songsiriritthigul C, Lapboonrueng S, Pechsrichuang P, Pesatcha P, Yamabhai M (2010) Bioresour Technol 101:4096–4103. https://doi.org/10.1016/j.biortech.2010.01.036 PubMed DOI

Sousa AJS, Silva CFB, Sousa JS, Monteiro-Junior JE, Freire JEC, Sousa BL, Lobo MDP, Monteiro-Moreira ACO, Grangeiro TB (2019) A thermostable chitinase from the antagonistic Chromobacterium violaceum that inhibits the development of phytopathogenic fungi. Enzyme Microb Technol 126:50–61. https://doi.org/10.1016/j.enzmictec.2019.03.009 PubMed DOI

Staats CC, Kmetzsch L, Lubeck I, Junges A, Vainstein MH, Schrank A (2013) Metarhizium anisopliae chitinase CHIT30 is involved in heat-shock stress and contributes to virulence against Dysdercus peruvianus. Fungal Biol 117:137–144. https://doi.org/10.1016/j.funbio.2012.12.006 PubMed DOI

Stefanidi E, Vorgias CE (2008) Molecular analysis of the gene encoding a new chitinase from the marine psychrophilic bacterium Moritella marina and biochemical characterization of the recombinant enzyme. Extremophiles 12:541–552. https://doi.org/10.1007/s00792-008-0155-9 PubMed DOI

Subramaniam S, Ravi V, Narayanan GK (2012) Studies on production of enzyme chitinase from Streptomyces sp. and its anti-fungal activity. J Pharma Res 5:1409–1413

Suganthi M, Senthilkumar P, Arvinth S, Chandrashekara KN (2017) Chitinase from Pseudomonas fluorescens and its insecticidal activity against Helopeltis theivora. J Gen Appl Microbiol. https://doi.org/10.2323/jgam.2016.11.001 PubMed DOI

Suginta W, Vongsuwan A, Songsiriritthigul C, Prinz H, Estibeiro P, Duncan RR, Svasti J, Fothergill-Gilmore LA (2004) An endochitinase A from Vibrio carchariae: cloning, expression, mass and sequence analyses, and chitin hydrolysis. Arch Biochem Biophys 424:171–180. https://doi.org/10.1016/j.abb.2004.01.017 PubMed DOI

Svedese VM, Tiago PV, Bezerra JDP, Paiva LM, de Luna Alves Lima EA, Porto ALF (2013) Pathogenicity of Beauveria bassiana and production of cuticle-degrading enzymes in the presence of Diatraea saccharalis cuticle. Afr J Biotechnol 12:6491–6497. https://doi.org/10.5897/AJB2013.11972 DOI

Synowiecki J, Al-Khateeb NA (2003) Production, properties, and some new applications of chitin and its derivatives. Crit Rev Food Sci Nutr 43:145–171. https://doi.org/10.1080/10408690390826473 PubMed DOI

Synstad B, Vaaje-Kolstad G, Cederkvist FH, Saua SF, Horn SJ, Eijsink VGH, Sorlie M (2008) Expression and characterization of endochitinase C from Serratia marcescens BJL200 and its purification by a one-step general chitinase purification method. Biosci Biotechnol Biochem 72:715–723. https://doi.org/10.1271/bbb.70594 PubMed DOI

Taechowisan T, Peberdy JF, Lumyong S (2003) Chitinase production by endophytic Streptomyces aureofaciens CMUAc130 and its antagonism against phytopathogenic fungi. Ann Microbiol 53:447–461

Tanabe T, Kawase T, Watanabe T, Uchida Y, Mitsutomi M (2000) Purification and characterization of a 49-kDa chitinase from Streptomyces griseus HUT 6037. J Biosci Bioeng 89:27–32 PubMed DOI

Thirumurugan D, Sankari D, Vijayakumar R (2015) Screening of chitinase production and antifungal activity of Streptomyces sp. ACT7 from east coast region. South India Int J Pharm Sci 7:38–41

Tikhonov VE, Lopez-Llorca LV, Salinas J, Jansson HB (2002) Purification and characterization of chitinases from the nematophagous fungi Verticillium chlamydosporium and V. suchlasporium. Fungal Genet Biol 35:67–78. https://doi.org/10.1006/fgbi.2001.1312 PubMed DOI

Toharisman A, Suhartono MT, Spindler-Barth M, Hwang JK, Pyun YR (2005) Purification and characterization of a thermostable chitinase from Bacillus licheniformis Mb-2. World J Microbial Biotechnol 21:733–738. https://doi.org/10.1007/s11274-004-4797-1 DOI

Tran TN, Doan CT, Nguyen VB, Nguyen AD, Wang SL (2018) The isolation of chitinase from Streptomyces thermocarboxydus and its application in the preparation of chitin oligomers. Res Chem Intermed. https://doi.org/10.1007/s11164-018-3639-y DOI

Tsujibo H, Hatano N, Endo H, Miyamoto K, Inamori Y (2000) Purification and characterization of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520 and cloning of the encoding gene. Biosci Biotechnol Biochem 64:96–102. https://doi.org/10.1271/bbb.64.96 PubMed DOI

Tsujibo H, Kubota T, Yamamoto M, Miyamoto K, Inamori Y (2003) Characterization of chitinase genes from an alkaliphilic actinomycete, Nocardiopsis prasina OPC-131. Appl Environ Microbiol 69:894–900. https://doi.org/10.1128/AEM.69.2.894-900.2003 PubMed DOI PMC

Tweddell RJ, Jabaji-Hare SH, Charest PM (1994) Production of chitinases and β-1,3-glucanases by Stachybotrys elegans, a mycoparasite of Rhizoctonia solani. Appl Environ Microbiol 60:489–495 PubMed DOI PMC

Vaaje-Kolstad G, Horn SJ, van Aalten DMF, Synstad B, Eijsink VGH (2005) The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 280:28492–28497. https://doi.org/10.1074/jbc.M504468200 PubMed DOI

Velmurugan N, Kalpana D, Han JH, Cha HJ, Lee YS (2011) A novel low temperature chitinase from the marine fungus Plectosphaerella sp. strain MF-1. Bot Mar 54:75–81. https://doi.org/10.1515/BOT.2010.068 DOI

Vincy V, Shoba MV, Viveka S, Vijaya TM, Rani GJB (2014) Isolation and characterization of chitinase from bacteria of shrimp pond. Euro J Exp Bio 4:78–82

Vyas P, Deshpande M (1991) Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP. J Gen Appl Microbiol 37:267–275. https://doi.org/10.2323/jgam.37.267 DOI

Waghmare SR, Ghosh JS (2010) Chitobiose production by using a novel thermostable chitinase from Bacillus licheniformis strain JS isolated from a mushroom bed. Carbohydr Res 345:2630–2635. https://doi.org/10.1016/j.carres.2010.09.023 PubMed DOI

Wang Q, Duan B, Yang R, Zhao Y, Zhang L (2015) Screening and identification of chitinolytic actinomycetes and study on the inhibitory activity against turfgrass root rot disease fungi. JBM 3:56–65. https://doi.org/10.4236/jbm.2015.33009 DOI

Wang SL, Chang WT (1997) 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 63:380–386 PubMed DOI PMC

Wang SL, Hsiao WJ, Chang WT (2002) Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium. J Agric Food Chem 50:2249–2255. https://doi.org/10.1021/jf011076x PubMed DOI

Wang SY, Moyne AL, Thottappilly G, Wu SJ, Locy RD, Singh NK (2001) Purification and characterization of a Bacillus cereus exochitinase. Enzyme Microb Technol 28:492–498. https://doi.org/10.1016/s0141-0229(00)00362-8 PubMed DOI

Wang YJ, Yang Q (2009) Cloning and expression of a novel chitinase chi58 from Chaetomium cupreum in Pichia pastoris. Biochem Genet 47:547–558. https://doi.org/10.1007/s10528-009-9251-5 PubMed DOI

Wattanalai R, Wiwat C, Boucias DG, Tartar A (2004) Chitinase gene of the dimorphic mycopathogen, Nomuraea rileyi. J Invertebr Pathol 85:54–57. https://doi.org/10.1016/j.jip.2003.12.007 PubMed DOI

Wu JH, Ali S, Ren SX (2010) Evaluation of chitinase from Metarhizium anisopliae as biopesticide against Plutella xylostella. Pakistan J Zool 42:521–528

Wu Q, Mushi NE, Berglund LA (2020) High-strength nanostructured films based on well-preserved α-chitin nanofibrils disintegrated from insect cuticles. Biomacromol 21:604–612. https://doi.org/10.1021/acs.biomac.9b01342 DOI

Xiao L, Xie CC, Cai J, Lin ZJ, Chen YH (2009) Identification and characterization of a chitinase-produced Bacillus showing significant antifungal activity. Curr Microbiol 58:528–533. https://doi.org/10.1007/s00284-009-9363-5 PubMed DOI

Xie XH, Fu X, Yan XY, Peng WF, Kang LX (2021) A broad-specificity chitinase from Penicillium oxalicum k10 exhibits antifungal activity and biodegradation properties of chitin. Mar Drugs. https://doi.org/10.3390/md19070356 PubMed DOI PMC

Yadav M, Goswami P, Paritosh K, Kumar M, Pareek N, Vivekanand, (2019) Seafood waste: a source for preparation of commercially employable chitin/chitosan materials. Bioresour Bioprocess 6:8. https://doi.org/10.1186/s40643-019-0243-y DOI

Yahiaoui M, Laribi-Habchi H, Bouacem K, Asmani KL, Mechri S, Harir M, Bendif H, Aissani-El Fertas R, Jaouadi B (2019) Purification and biochemical characterization of a new organic solvent-tolerant chitinase from Paenibacillus timonensis strain LK-DZ15 isolated from the Djurdjura Mountains in Kabylia. Carbohydr Res, Algeria. https://doi.org/10.1016/j.carres.2019.107747 DOI

Yan Q, Fong SS (2018) Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase. Biotechnol Rep. https://doi.org/10.1016/j.btre.2018.e00274 DOI

Yandigeri MS, Malviya N, Solanki MK, Shrivastava P, Sivakumar G (2015) Chitinolytic Streptomyces vinaceusdrappus S5MW2 isolated from Chilika lake, India enhances plant growth and biocontrol efficacy through chitin supplementation against Rhizoctonia solani. World J Microbiol Biotechnol 31:1217–1225. https://doi.org/10.1007/s11274-015-1870-x PubMed DOI

Yang CY, Ho YC, Pang JC, Huang SS, Tschen JSM (2009) Cloning and expression of an antifungal chitinase gene of a novel Bacillus subtilis isolate from Taiwan potato field. Bioresour Technol 100:1454–1458. https://doi.org/10.1016/j.biortech.2008.07.039 PubMed DOI

Yang S, Fu X, Yan Q, Guo Y, Liu Z, Jiang Z (2016) Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenicibacillus barengoltzii. Food Chem 192:1041–1048. https://doi.org/10.1016/j.foodchem.2015.07.092 PubMed DOI

Youn DK, No HK, Prinyawiwatkul W (2013) Preparation and characteristics of squid pen β-chitin prepared under optimal deproteinisation and demineralisation condition. Int J Food Sci Technol 48:571–577. https://doi.org/10.1111/ijfs.12001 DOI

Yu G, Xie LQ, Li JT, Sun XH, Zhang H, Du Q, Li QY, Zhang SH, Pan HY (2015) Isolation, partial characterization, and cloning of an extracellular chitinase from the entomopathogenic fungus Verticillium lecanii. Genet Mol Res 14:2275–2289. https://doi.org/10.4238/2015.March.27.13 PubMed DOI

Yuli PE, Suhartono MT, Rukayadi Y, Hwang JK, Pyun YR (2004) Characteristics of thermostable chitinase enzymes from the Indonesian Bacillus sp. 13.26. Enzyme Microb Technol 35:147–153. https://doi.org/10.1016/j.enzmictec.2004.03.017 DOI

Zarei M, Aminzadeh S, Zolgharnein H, Safahieh A, Daliri M, Noghabi KA, Ghoroghi A, Motallebi A (2011) Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A. Braz J Microbiol 42:1017–1029. https://doi.org/10.1590/S1517-838220110003000022 PubMed DOI PMC

Zeltins A, Schrempf H (1995) Visualization of α-chitin with a specific chitin-binding protein (CHB1) from Streptomyces olivaceoviridis. Anal Biochem 231:287–294. https://doi.org/10.1006/abio.1995.0053 PubMed DOI

Zhang A, He Y, Wei G, Zhou J, Dong W, Chen K, Ouyang P (2018) Molecular characterization of a novel chitinase CmChi1 from Chitinolyticbacter meiyuanensis SYBC-H1 and its use in N-acetyl-D-glucosamine production. Biotechnol Biofuels. https://doi.org/10.1186/s13068-018-1169-x PubMed DOI PMC

Zhang S, Jiang S, Xiong Y, Fu H, Sun S, Qiao H, Zhang W, Jiang F, Jin S, Gong Y (2014) Six chitinases from oriental river prawn Macrobrachium nipponense: cDNA characterization, classification and mRNA expression during post-embryonic development and moulting cycle. Comp Biochem Physiol B Biochem Mol Biol 167:30–40. https://doi.org/10.1016/j.cbpb.2013.09.009 PubMed DOI

Zhang Z, Yuen GY (2000) The role of chitinase production by Stenotrophomonas maltophilia strain C3 in biological control of Bipolaris sorokiniana. Phytopathology 90:384–389. https://doi.org/10.1094/PHYTO.2000.90.4.384 PubMed DOI

Zhao Y, Li Z, Gu X, Su Y, Liu L (2020) Imaginal disc growth factor 6 (Idgf6) is involved in larval and adult wing development in Bactrocera correcta (Bezzi) (Diptera: Tephritidae). Front Genet. https://doi.org/10.3389/fgene.2020.00451 PubMed DOI PMC

Zhong W, Ding S, Guo H (2015) The chitinase C gene PsChiC from Pseudomonas sp. and its synergistic effects on larvicidal activity. Genet Mol Biol 38:366–372. https://doi.org/10.1590/S1415-475738320140320 PubMed DOI PMC

Zhu XF, Zhou Y, Feng JL (2007) Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5. J Zhejiang Univ Sci B 8:831–838. https://doi.org/10.1631/jzus.2007.B0831 PubMed DOI PMC

Zong H, Li K, Liu S, Song L, Xing R, Chen X, Li P (2017) Improvement in cadmium tolerance of edible rape (Brassica rapa L.) with exogenous application of chitooligosaccharide. Chemosphere 181:92–100. https://doi.org/10.1016/j.chemosphere.2017.04.024 PubMed DOI

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...