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Biosynthesis of Fungal Chitinolytic Enzymes and Their Potent Biotechnological Appliances

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Book cover Recent Advancement in White Biotechnology Through Fungi

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Abstract

Chitin is the world’s second most abundant polysaccharide (after cellulose) and most plenteous amino-polysaccharide in environment. Its recalcitrant structure contributes mechanical strength to the chitin-bearing organisms. Chitinolytic enzymes or chitinases are group of glycosyl hydrolases which collectively and ultimately breaks chitin to its building block N-acetylglucosamine. Chitinolytic enzymes are ubiquitous among most of the living taxa, starting from bacteria to human beings, where they play different imperative biological functions. In spite of its cosmopolitan distribution in nature, chitinase from microorganisms are extensively explored. Chitinase has engrossed worldwide colossal attention due to its widespread applicability in biocontrol, biomedical, waste management, and pharmaceutical sectors, and owing to these employments, there is a steady increment in the demand of chitinases in present scenario. Perusal of literature attested that among the reports on microbial chitinase, a fungus contributes a lion’s share. In fungi, chitinase plays multiple physiological roles including degradation of indigenous and exogenous chitin. Classical fermentation method in optimized condition is generally applied for the production of chitinase, whereas with the advent and advancement of genetic engineering, overproduction/overexpression of chitinase is now becoming a fascinated approach. In the present deliberation, biosynthesis of fungal chitinolytic enzymes, their classification, physiological role, potential applications, and future perspectives are outlined and highlighted.

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References

  • Adrangi S, Faramarzi MA (2013) From bacteria to human: a journey into the world of chitinases. Biotechnol Adv 31:1786–1795

    Google Scholar 

  • Aïzi DE, Cheba BA (2015) Influence of chitinous waste on soil bacterial community: biofertilizer effect and antifungal activity. Procedia Technol 19:965–971

    Google Scholar 

  • Araujo AC, Souto-Padrón T, de Souza W (1993) Cytochemical localization of carbohydrate residues in microfilariae of Wuchereria bancrofti and Brugia malayi. J Histochem Cytochem 41:571–578

    Google Scholar 

  • Bell DK, Wells HD, Markham CR (1982) In vitro antagonism of Trichoderma species against six fungal plant pathogens. Phytopathology 72:379–382

    Google Scholar 

  • Benhamou N, Asselin A (1989) Attempted localization of a substrate for chitinase in plant cells reveals abundant N-acetyl D-glucosamine residues in secondary walls. Biol Cell 67:341–350

    Google Scholar 

  • 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 App Microbiol 103:1845–1852

    Google Scholar 

  • Binod P, Palkhiwala P, Gaikaiwari R, Nampoothiri KM, Duggal A, Dey K, Pandey A (2013) Industrial enzymes - present status and future perspectives for India. J Sci Industrial Res 72:271–286

    Google Scholar 

  • 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

    Google Scholar 

  • Brzezinska MS, Jankiewicz U, Burkowska A, Walczak M (2014) Chitinolytic microorganisms and their possible application in environmental protection. Curr Microbiol 68:71–81

    Google Scholar 

  • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 37:D233–D238

    Google Scholar 

  • Chamberland H, Charest PM, Ouellette GB, Pauze FJ (1985) Chitinase-gold complex used to localize chitin ultrastructurally in tomato root cells infected by Fusarium oxysporum f. sp. radicislycopersici, compared with a chitin specific gold-conjugated lectin. Histochem J 17:313–321

    Google Scholar 

  • Chen C, McIver J, Yang Y, Bai Y, Schultz B, McIver A (2007) Foliar application of lipo-chitooligosaccharides (Nod factors) to tomato (Lycopersicon esculentum) enhances flowering and fruit production. Can J Plant Sci 87:365–372

    Google Scholar 

  • Cody R, Davis N, Lin J, Shaw D (1990) Screening microorganisms for chitin hydrolysis and production of ethanol from amino sugars. Biomass 21:285–295

    Google Scholar 

  • Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773–782

    Google Scholar 

  • de Assis CF, Araújo NK, Pagnoncelli MGB, da Silva Pedrini MR, de Macedo GR, dos Santos ES (2010) Chitooligosaccharides enzymatic production by Metarhizium anisopliae. Bioprocess Biosyst Eng 33:893–899

    Google Scholar 

  • de Vries MH, Wessels JGH (1973) Release of protoplasts from Schizophyllum commune by combined action of purified α-1,3-glucanase and chitinase derived from Trichoderma viride. J Gen Microbiol 76(3):19–330

    Google Scholar 

  • Duo-Chuan L (2006) Review of fungal chitinases. Mycopathologia 161:345–360

    Google Scholar 

  • Duo-Chuan L, Hang S-H, Liu K-Q, Lu J (2004) Purification and partial characterization of a chitinase from the mycoparasitic fungus Trichothecium roseum. J Gen Appl Microbiol 50:35–39

    Google Scholar 

  • Firag MA, Al-Nusarie ST (2014) Production, optimization, characterization and antifungal activity of chitinase produced by Aspergillus terrus. African J Biotechnol 13(14):1567–1578

    Google Scholar 

  • 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

    Google Scholar 

  • Giambattista RD, Federici F, Petruccioli M, Fence M (2001) The chitinolytic activity of Penicillium janthinellum P9: purification, partial characterization and potential application. J Appl Microbiol 91:498–505

    Google Scholar 

  • Goettel MS, Koike M, Kim JJ, Aiuchi D, Shinya R, Brodeur J (2008) Potential of Lecanicillium spp. for management of insects, nematodes and plant diseases. J Invert Pathol 98:256–261

    Google Scholar 

  • Gohel V, Singh A, Vimal M, Ashwini P, Chhatpar HS (2006) Bioprospecting and antifungal potential of chitinolytic microorganisms. Afri J Biotechnol 5:54–72

    Google Scholar 

  • Gortari MC, Hours RA (2008) Fungal chitinases and their biological role in the antagonism onto nematode eggs. A review. Mycol Progress 7:221–238

    Google Scholar 

  • Govindsamy V, Gunaratna KR, Balasubramanian R (1998) Properties of extracellular chitinase from Myrothecium verrucaria, an antagonist to the groundnut rust Puccinia arachidis. Canadian J Plant Pathol 20:62–68

    Google Scholar 

  • Halder SK (2018) Insight of chitinolytic cascade of marine bacteria: a vista for material cycling and valorization. Acta Sci Microbiol 1(9):1–3

    Google Scholar 

  • Halder SK, Mondal KC (2018) Microbial valorization of chitinous bioresources for chitin extraction and production of chito-oligomers and N-acetylglucosamine: trends, perspectives and prospects. In: Patra J, Das G, Shin HS (eds) Microbial biotechnology. Springer, Singapore

    Google Scholar 

  • Halder SK, Adak A, Maity C, Jana A, Das A, Paul T, Ghosh K, Das Mohapatra PK, Pati BR, Mondal KC (2013a) Exploitation of fermented shrimp-shell hydrolysate as functional food: assessment of antioxidant, hypocholesterolemic and prebiotic activities. Ind J Exp Biol 51(11):924–934

    Google Scholar 

  • Halder SK, Maity C, Jana A, Das A, Paul T, Das Mohapatra PK, Pati BR, Mondal KC (2013b) Proficient biodegradation of shrimp shell waste by Aeromonas hydrophila SBK1 for the concomitant production of antifungal chitinase and antioxidant chitosaccharides. Int Biodeterior Biodegradation 79:88–97

    Google Scholar 

  • Halder SK, Jana A, Das A, Paul T, Das Mohapatra PK, Pati BR, Mondal KC (2014) Appraisal of antioxidant, anti-hemolytic and DNA shielding potentialities of chitosaccharides produced innovatively from shrimp shell by sequential treatment with immobilized enzymes. Food Chem 158:325–334

    Google Scholar 

  • Halder SK, Jana A, Paul T, Das A, Ghosh K, Pati BR, Mondal KC (2016) Purification and biochemical characterization of chitinase of Aeromonas hydrophila SBK1 biosynthesized using crustacean shell. Biocat Agri Biotechnol 5:211–218

    Google Scholar 

  • Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S (2013) Chitinases: an update. J Pharm Bioallied Sci 5:21–29

    Google Scholar 

  • Harighi MJ, Motallebi M, Zamani MR (2006) Purification of chitinase 42 from Trichoderma atroviride PTCC5220. Iran J Biol 19:203–214

    Google Scholar 

  • Hartl L, Zach S, Seidl-Seiboth V (2012) Fungal chitinases: diversity, mechanistic properties and biotechnological potential. Appl Microbiol Biotechnol 93:533–543

    Google Scholar 

  • Hassas-Roudsari M, Goff HD (2012) Ice structuring proteins from plants: mechanism of action and food application. Food Res Int 46:425–436

    Google Scholar 

  • He H, Chen X, Sun C, Zhang Y, Gao P (2006) Preparation and functional evaluation of oligopeptide-enriched hydrolysate from shrimp (Acetes chinensis) treated with crude protease from Bacillus sp. SM98011. Bioresour Technol 97:385–390

    Google Scholar 

  • Inokuma K, Takano M, Hoshino K (2013) Direct ethanol production from N-acetylglucosamine and chitin substrates by Mucor species. Biochem Eng J 72:24–32

    Google Scholar 

  • 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

    Google Scholar 

  • Kidibule PE, Santos-Moriano P, Jiménez-Ortega E, Ramírez-Escudero M, Limón MC, Remacha M, Plou FJ, Sanz-Aparicio J, Fernández-Lobato M (2018) Use of chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: enzymatic activity and structural basis of protein specificity. Microb Cell Factories 17(1):47. https://doi.org/10.1186/s12934-018-0895-x

    Google Scholar 

  • Kour D, Rana KL, Verma P, Yadav AN, Kumar V, Singh DH (2017) Biofertilizers: eco-friendly technologies and bioresources for sustainable agriculture. In: Proceeding of international conference on innovative research in engineering science and technology, p 43

    Google Scholar 

  • Kumar S, Stecher G, Tamura K (2016) MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets. Mol Biol Evol 33:1870–1874

    Google Scholar 

  • Kunert J, Zemek J, Augustín J, Kuniak E, Chalupová V (1985) Chitinolytic activity of ovicidal soil fungi. Biologia (Bratislava) 40(11):1157–1165

    Google Scholar 

  • Langner T, Göhre V (2016) Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions. Curr Genet 62(2):243–254

    Google Scholar 

  • Manocha MS, Zhonghua Z (1997) Immunochemical and cytochemical localization of chitinase and chitin in infected hosts of a biotrophic mycoparasite, Piptocephalis virginiana. Mycologia 89:185–194

    Google Scholar 

  • Matsumoto KS (2006) Fungal chitinase. In: Guevara-González RG, Torres-Pacheco I (eds) Advances in agricultural and food biotechnology. Research Signpost, Trivandrum, pp 289–304

    Google Scholar 

  • Mendonsa ES, Vartak PH, Rao JU, Deshpande MV (1996) An enzyme from Myrothecium verrucaria that degrades insect cuticle for biocontrol of Aedes aegypti mosquito. Biotechnol Lett 18:373–376

    Google Scholar 

  • Mercer CF, Greenwood DR, Grant JL (1992) Effect of plant and microbial chitinases on the eggs and juveniles of Meloidogyne hapla Chitwood. Nematologica 8:227–236

    Google Scholar 

  • 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 52:539–548

    Google Scholar 

  • Monteiro VN, Silva RN, Steindorff AS, Costa FT, Noronha EF, Ricart SAO, Sousa MV, Vainstein MH, Ulhoa CJ (2010) New insights in Trichoderma harzianum antagonism of fungal plant pathogens by secreted protein analysis. Curr Microbiol 61:298–305

    Google Scholar 

  • Nampoothiri KM, Baiju TV, Sandhya C, Sabu A, Szakacs G, Pandey A (2004) Process optimization for antifungal chitinase production by Trichoderma harzianum. Process Biochem 39:1583–1590

    Google Scholar 

  • Nguyen HQ, Quyen DT, Nguyen SLT, Vu VH (2015) An extracellular antifungal chitinase from Lecanicillium lecanii: purification, properties, and application in biocontrol against plant pathogenic fungi. Turkish J Biol 39:6–14

    Google Scholar 

  • Orunsi NA, Trinci APJ (1985) 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. Microbes 43:17–30

    Google Scholar 

  • Park JO, Hargreaves JR, McConville EJ, Stirling GR, Ghisalberti EL, Sivasithamparam K (2004) Production of leucinostatins and nematicidal activity of Australian isolates of Paecilomyces lilacinus (Thom) Samson. Lett Appl Microbiol 38:271–276

    Google Scholar 

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

    Google Scholar 

  • Patil NS, Jadhav JP (2015) Penicillium ochrochloron MTCC 517 chitinase: an effective tool in commercial enzyme cocktail for production and regeneration of protoplasts from various fungi. Saudi J Biol Sci 22:232–236

    Google Scholar 

  • 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

    Google Scholar 

  • Pope AM, Davis DA (1979) The influence of carbohydrates on the growth of fungal pathogens in vitro and in vivo. Postgraduate Med J 55:674–676

    Google Scholar 

  • Ragavendran C, Dubey NK, Natarajan D (2017) Beauveria bassiana (Clavicipitaceae): a potent fungal agent for controlling mosquito vectors of Anopheles stephensi, Culex quinquefasciatus and Aedes aegypti (Diptera: Culicidae). RSC Adv 7:3838–3851

    Google Scholar 

  • Rana KL, Kour D, Yadav AN, Kumar V, Dhaliwal HS (2016a) Biotechnological applications of endophytic microbes associated with barley (Hordeum vulgare L.) growing in Indian Himalayan regions. In: Proceeding of 86th annual session of NASI & symposium on “Science, Technology and Entrepreneurship for Human Welfare in The Himalayan Region”, p 80

    Google Scholar 

  • Rana KL, Kour D, Yadav AN, Kumar V, Dhaliwal HS (2016b) Endophytic microbes from wheat: diversity and biotechnological applications for sustainable agriculture. In: Proceeding of 57th Association of Microbiologist of India & International symposium on “Microbes and Biosphere: What’s New What’s Next”, p 453

    Google Scholar 

  • Rana KL, Kour D, Verma P, Yadav AN, Kumar V, Dhaliwal HS (2017) Diversity and biotechnological applications of endophytic microbes associated with maize (Zea mays L.) growing in Indian Himalayan regions. In: Proceeding of national conference on advances in food science and technology

    Google Scholar 

  • Rathore AS, Gupta RD (2015) Chitinases from bacteria to human: properties, applications, and future perspectives, Enzyme Res 2015(Article ID 791907):1–8. https://doi.org/10.1155/2015/791907

  • Rattanakit N, Plikomol A, Yano S, Wakayama M, Tachiki T (2002) Utilization of shrimp shellfish waste as a substrate for solid-state cultivation of Aspergillus sp. S1-13: evaluation of a culture based on chitinase formation which is necessary for chitin-assimilation. J Biosci Bioeng 93(6):550–556

    Google Scholar 

  • Rattanakit N, Yano S, Plikomol A, Wakayama M, Tachiki T (2008) Purification of Aspergillus sp. S1-13 chitinases and their role in saccharification of chitin in mash of solid-state culture with shellfish waste. J Biosci Bioeng 103(6):535–554

    Google Scholar 

  • Revah-Moiseev S, Carrod PA (1981) Conversion of the enzymatic hydrolysate of shellfish waste chitin to single cell protein. Biotechnol Bioeng 23:1067–1078

    Google Scholar 

  • Roopavathi AS, Vigneshwari R, Jayapradha R (2015) Chitinase: production and applications. J Chem Pharm Res 7(5):924–931

    Google Scholar 

  • Sahay H, Yadav AN, Singh AK, Singh S, Kaushik R, Saxena AK (2017) Hot springs of Indian Himalayas: potential sources of microbial diversity and thermostable hydrolytic enzymes. 3 Biotech 7:1–11

    Google Scholar 

  • Sahu BB, Sahu U, Barik NK, Agnibesh A, Paikaray A, Mohapatra S, Senapati S, Sahu JK (2017) Application of shellfish shell waste derived chitosan and chitooligosaccharides in agriculture horticulture and post-harvest value addition of agricultural products. Int J Fish Aqu Res 2(5):1–8

    Google Scholar 

  • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406–425

    Google Scholar 

  • Saxena AK, Yadav AN, Rajawat M, Kaushik R, Kumar R, Kumar M, Prasanna R, Shukla L (2016) Microbial diversity of extreme regions: an unseen heritage and wealth. Indian J Plant Genet Resour 29:246–248

    Google Scholar 

  • Seidl V (2008) Chitinases of filamentous fungi: a large group of diverse proteins with multiple physiological functions. Fungal Biol Rev 22:36–42

    Google Scholar 

  • Sharif R, Mujtaba M, Rahman MU, Shalmani A, Ahmad H, Anwar T, Tianchan D, Wang X (2018) The multifunctional role of chitosan in horticultural crops; a review. Molecules 23:872. https://doi.org/10.3390/molecules23040872

    Google Scholar 

  • Suman A, Verma P, Yadav AN, Saxena AK (2015) Bioprospecting for extracellular hydrolytic enzymes from culturable thermotolerant bacteria isolated from Manikaran thermal springs. Res J Biotechnol 10:33–42

    Google Scholar 

  • Thadathil N, Velappan SP (2014) Recent developments in chitosanase research and its biotechnological applications: a review. Food Chem 150:392–399

    Google Scholar 

  • Tikhonov VE, Lopez-Llorca LV, Salinas J, Jansson HB (2002) Purification and characterization of chitinases from the nematophagous fungi Verticillium chamydosporium and V. suchlasporium. Fungal Genet Biol 35:67–78

    Google Scholar 

  • Viterbo A, Haran S, Friesem D, Ramot O, Chet I (2001) Antifungal activity of a novel endochitinase gene (chit36) from Trichoderma harzianum Rifai TM. FEMS Microbiol Lett 200:169–174

    Google Scholar 

  • Vyas PR, Deshpande MV (1991) Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP. J Gen Appl Microbiol 37:267–275

    Google Scholar 

  • Yadav AN (2015) Bacterial diversity of cold deserts and mining of genes for low temperature tolerance. Ph.D. Thesis, IARI, New Delhi/BIT, Ranchi, pp. 234, doi: https://doi.org/10.13140/RG.2.1.2948.1283/2

  • Yadav AN (2017) Agriculturally important microbiomes: biodiversity and multifarious PGP attributes for amelioration of diverse abiotic stresses in crops for sustainable agriculture. Biomed J Sci Tech Res 1:1–4

    Google Scholar 

  • Yadav AN, Verma P, Sachan S, Kaushik R, Saxena A (2012) Diversity of culturable psychrotrophic bacteria from Leh Ladakh and bioprospecting for cold-active extracellular enzymes. In: Proceeding of national seminar on “biotechnological interventions for the benefit of mankind”, p 32

    Google Scholar 

  • Yadav AN, Sachan SG, Verma P, Kaushik R, Saxena AK (2016a) Cold active hydrolytic enzymes production by psychrotrophic Bacilli isolated from three sub-glacial lakes of NW Indian Himalayas. J Basic Microbiol 56:294–307

    Google Scholar 

  • Yadav AN, Sachan SG, Verma P, Saxena AK (2016b) Bioprospecting of plant growth promoting psychrotrophic Bacilli from cold desert of north western Indian Himalayas. Indian J Exp Biol 54:142–150

    Google Scholar 

  • Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, Kumagai H (2010) Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 beta-glucosidase from Kluyveromyces marxianus. Bioche J 431:39–49

    Google Scholar 

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Acknowledgments

The authors are grateful to the authority of Vidyasagar University and BIF Centre of the University for carrying out research in the relevant field. Corresponding author deeply acknowledged Department of Science and Technology, Govt. of India, for financial support as DST-INSPIRE fellowship. There are no conflicts of interest.

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Halder, S.K., Pal, S., Mondal, K.C. (2019). Biosynthesis of Fungal Chitinolytic Enzymes and Their Potent Biotechnological Appliances. In: Yadav, A., Mishra, S., Singh, S., Gupta, A. (eds) Recent Advancement in White Biotechnology Through Fungi. Fungal Biology. Springer, Cham. https://doi.org/10.1007/978-3-030-10480-1_8

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