Chitinase

Main Article Content

Song Jinzhu
Yang Qian

Abstract

Chitin is one of the most abundant polymers in nature and an important component for many organisms. For catalyzing and hydrolyzing chitin into N-acetylglucosamine (GlcNAC) and (GlcNAC)n, chitinases have being received much attention in many fields. This article mainly introduced the recent research on chitinase, including structure, function and application of the enzyme.


Keywords:  chitinase, structure, function


Corresponding author: E-mail: [email protected]

Article Details

Section
Review Ariticle

References

[1] N. Majeti and R.A. Kumar, Review of chitin and chitosan applications. Recat. Funct. Polym., 2000, 46, 1-27.
[2] W. Suntornsuk, P. Pochanakanich and L. Suntonsuk, Fungal chitosan production on food processing by-products. Proc. Bio-chem., 2002, 37, 727-729.
[3] A.S. Sahai, Manocha: Chitinase of fungi and plants: their involvement in morphogenesis and host-parasite interaction. FEMS Microbiol. Rev., 1993, 11, 317-338.
[4] G.E. Harman, C.K. Hayes, M. Lorito, R.M. Broadway, A. Di Pietro, C. Peterbauer and A. Tronsmo, Chitinolytic enzymes of Trichoderma harzianum: purification of chitobiosidase and endochitinase. Phytopathology, 1993, 83, 313-331.
[5] B. Henrissat and A. Bairoch, New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 1993, 293, 781-788.
[6] F. Hamel, R. Boivin, C. Temblay and G. Bellemare, Structural and evolutionary relationships among chitinase of flowing plants. J. Mol. Evol., 1997, 44, 614-624.
[7] A. Perrakis, K.S. Wilson, I. Chet, A.B. Oppenheim and C.E. Vorgias, Phylogenetic relationships of chitinases. In chitin enzymology. Edited by Muzzarelli R.A.A. Ancona: European Chitin Society, 1993, 103, 221-226.
[8] D.B. Collinge, K.M. Kragh, J.D. Mikkelsen, K.K. Nielsen, U. Rasmussen and K. Vad, Plant chitinases. Plant Mol. Biol., 1990, 14, 357-368.
[9] P.A. Jekel, J.B.H. Hartmann and J.J. Beintema, The primary structure of Hevamine, an enzyme with lysozyme/ chitinase activity from Havea brasiliensis latex. Eur. J. Biochem., 1991, 200, 123-130.
[10] T. Boller, A. Gebri, F. Mauch and U. Vogeli, Chitinase in bean leaves, induction by ethylene, purification, properties, and possible function. Planta, 1983, 157, 22-31.
[11] G.W. Gooday, A.M. Humphreys and W.H. Mcintosh, Roles of chitinase in fungal growth. In: Chitin in nature and technology (R. Muzzarelli, C. Jeuniaux and G.W. Gooday, eds), 1986, 83-91, Plenum Press, New York.
[12] Gao Bida, Strategy of chitinase gene transfer for plant disease control progress, problems and prospect, 1999, 19(2), 21-28.
[13] W.T. Terra, C. Ferreira, B.P. Jordao and R.J. Dillion. Digestive enzymes. In: Biology of the Insect Midgut. Eds M.J. Lchana and P.F. Bollingsley, 1996, pp. 153-194, Chapman and Hall. London.
[14] M.J. Lehane, Petritrophic matrix structure and function. J. Annu. Rev. Entomol., 1997, 42, 525-550.
[15] K.J. Kramer, I.L.M Corpuz and H. Choi et al. Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinase of Manduca Sexta. J. Insect Biochem. Mol. Biol., 1993, 23, 691-701.
[16] S.E. Reynoid and R.I. Samules, Physiology and biochemistry of insect moulting fluid. Adv. Insect Physiol., 1996, 26, 157-232.
[17] K.J. Kramer and A.S. Muthukrishnan, Insect chitinase: molecular Biology and potential use biopesticides. J. Insect Biochem. Mol. Biol., 1997, 27(11), 887-900.
[18] M.M. Alam, N. Nikaidou, H. Tanaka et al., Cloning and sequencing of chic gene of Bacillus circulans ML-12 and relationship of its product to some other chitinases and chitinase-like proteins, J. Ferment Bioeng., 1995, 80, 454-461.
[19] Zhu Xuefeng, Chen Chongshun and Yu Zhifang. Biofunction of chitinase from plant. Chemistry of Life, 2000, 20(1), 36-37.
[20] H. Schckler, Chet 1: Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi. J. Ind. Microbiol. Biotechnol., 1997, 19, 196-201.
[21] S. P. Robinson, A.K. Jacobs and I.B. Dry, A class IV chitinase is highly expressed in grape beeries during ripening. Plant Physiol., 1997, 114, 771-778.
[22] K.M. Kragh, T. Hendriks and A.T. Jong et al. Characterization of chitinase able to rescue somatic embryos of the temperature-sensitive carrot variant ts II. Plant Molecular Biology, 1996, 31(3), 631-645.
[23] Kai-jun Zhao and Mee-len Chye. Methyl jasmonate induces expression of a novel Brassica juncea chitinase with two chitin-binding domains. Plant Molecular Biology, 1999, 40, 1009-1018.
[24] J.J. Beintema, Structural features of plant chitinase and chitin-bending proteins. FEBS, 1994, 350, 159-163.
[25] B. Iseli, T. Boller and T.M. Neuhaus, Mutation of either of two essential glutamates converts the catalytic domain of tobacco class I chitinase into a chitin-binding lectin. Plant Physiol., 1998, 134(1), 45-54.
[26] Gao Bida, Advances in the molecular biology of plant chitinase, J. of Human Agriculture University, 1996, 22(3), 815-822.
[27] M.D. Anderson, A. Jensen, R. Leah and J.K. Skiver, Heterologous expression and characterization of wild type and mutant forms of a 26 kD endochitinase from barley (Hordeum vulgare L), Biochemical Journal, 1997, 322(3), 815-822.
[28] G. Garcia-Casodo, C. Collada, I. Allona, Casador and L. F. Pacios, Site-directed mutagenesis of active site residues in a class I endochitinase from chestnut seeds. Glycobiology, 1998, 8(10), 1021-1028.
[29] I. Kunze, C. Nilson and K. Adler et al. Biochem. Biophys. Acta – N. 1998, 1395, 329-344.
[30] A.L. Svitil, S.M.N. Chadhain, J.A. Moore and D.L. Kirchman, Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin. J. Environ. Microbiol., 1997, 63, 408-413.
[31] U. Benecke, Bacillus chitinovorus, eien chitin zersetzenden spaltpilz. Bot. Ztg., 1995, 63, 227-231.
[32] T. Watanabe, Y. Tyaamada and M. Hashimoto et al. The roles of the C-terminal domain and type III domain and type III of chitinase A1 from Bacillus circulans W1-12 in chitin degradation. J. Bacteriol., 1994, 176, 4465-4472.
[33] H. Tsujibo, H. Orikoshi and K.Shiotani et al. Characterization of chitin c from a marine bacterium, Alteromonas sp. Strain O-7 and its corresponding gene and domain structure. Appl. Environ. Microbiol., 1998, 64, 427-478.
[34] T. Ohno, S. Armand, T. Hata, N. Nikaidou, B. Henrissat, M. Mitsutomi and T. Watanable, A modular family 19 chitinase found in the prokaryotic organism Sreptomyces griseus HUT6037. J. Bacteriol., 1996, 178, 5065-5070.
[35] S. Haran, H. Schickier and L. Chet, Molecular mechanisms of lytic-enzymes involved in the biocontrol activity of Trichoderma harzianum. Microbiol., 1996, 142, 2321-2331.
[36] H. Schickler, S. Haran, A. Opperheim and L. Chet, Induction of the Trochoderma harziaunm chitinolytic system is triggered by the chitin monomer, N-acetylglucosamine. Mycol. Res., 1998, 102(10), 1224-122.
[37] Ada Viterbo, Shoshan Haran, Dana Friesem, Ofir Ramot and Ilan Chet, Antifungal activity of a novel dedochitinase gene (chit36) from Trichoderma harzianum Rifai TM. FEMS Microbiology Letters, 2001, 200, 169-174.
[38] M.J. Kuranda and P.W. Robbins, Chitinase is required for cell separation during the growth of Saccharomyces cerevisiae. J. Biol. Chem., 1991, 266, 19758-19767.
[39] C.K. Hayes, S. Klemsdal, M. Lorito, A. Di Pietro, C. Peterbauer, J.P. Nakas, A. Tronsmo and G.E. Harman, Isolation and sequence of an endochitinase-encoding gene from a cDNAlibraby of Trichoderma harzianum. Gene, 1994, 138, 143-148.
[40] M. Carmen Limon, Emilio Margolles Clark, Tahia Benitez and Merja Penttila, Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum, FEMS Microbiology Letter, 2001, 198, 57-63.
[41] K. Hiraga, L. Shou, M. Kitazawa, S. Takahashi, M. Shimada, R. Sato and K. Oda, Isolation and characterization of chitinase from a flak-chitin degrading marine bacterium, Aeromonas hydrophila H-2330. Biosc. Biptech. Biochem., 1997, 61, 174-176.