참고문헌
- Davies, G. and Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolase. Structure 3, 853-859. https://doi.org/10.1016/S0969-2126(01)00220-9
- Morimoto, K., Karita, S., Kimura, T., Sakka, K. and Ohmiya, 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.
-
Svitil, A. L. and Kirchman, D. L. (1998) A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: implications for the ecology and evolution of
$1,4-{\beta}-glycanases$ . Microbiology 144, 1299-1308. https://doi.org/10.1099/00221287-144-5-1299 - Watanabe, T., Uchida, M., Kobori, K. and Tanaka, H. (1994) Site-directed mutagenesis of Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulars WL-12. Biosci. Biotech. Biochem. 58, 2283-2285. https://doi.org/10.1271/bbb.58.2283
- Watanabe, T., Oyanagi, W., Suzuki, K. and Tanaka, H. (1990) Chitinase A1 in chitin degradation. J. Bacteriol. 172, 4017-4022.
- Blaak, H. and Schrempf, H. (1995) Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form. Eur. J. Biochem. 229, 132-139. https://doi.org/10.1111/j.1432-1033.1995.tb20447.x
- Suginta, W., Vongsuwan, A., Songdiriritthigul, C., Prinz, H., Estibeiro, P., Duncan, R. R., Svati, J. and Fothergill- Gilmore, L. A. (2004) An endochitinase A from Vibio carchariae: cloning, expression, masss and sequence analyses, and chitin hydrolysis. Arch. Biochem. Biophys. 424, 171-180. https://doi.org/10.1016/j.abb.2004.01.017
- Lin, F. P., Juang, W. Y., Chang, K. H. and Chen, H. C. (2001) G561 site-directed deletion mutant chitinase from Aeromonas caviae is active without its 304 C-terminal amino acid residues. Arch. Microbiol. 175, 220-225. https://doi.org/10.1007/s002030100261
- Chuang, H. H. and Lin, F. P. (2007) New role of C-terminal 30 amino acids on the insoluble chitin hydrolysis in actively engineered chitinase from Vibio parahaemolyticus. Appl. Microbiol. Biotechnol. 76, 123-133. https://doi.org/10.1007/s00253-007-0990-0
- Watanabe, T., Ito, Y., Yamada, T., Hashimoto, M., Sekine, S. and Tanaka, H. (1994) The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176, 4465-4472. https://doi.org/10.1128/jb.176.15.4465-4472.1994
- Wang, F. P., Li, Q., Zhou, Y., Li, M. G. and Xiao, X. (2003) The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis. Proteins 53, 908-916. https://doi.org/10.1002/prot.10501
- Chan, M. C., Lai, P. L. and Wu, M. L. (2004) Biochemical characterization and site-directed mutational analysis of the double chitin-binding domain from chitinase 92 of Aeromonas hydrophila JP101. FEMS Microbiol. Lett. 232, 61-66. https://doi.org/10.1016/S0378-1097(04)00014-X
- Pichyangkura, R., Kudan, S., Kuttiyawong, K., Sukwattanasinitt, M. and Aiba, S. (2002) Quantitative production of 2-acetamido-2-deoxy-D-glucose from crystalline chitin by bacterial chitinase. Carbohydr. Res. 337, 557-559. https://doi.org/10.1016/S0008-6215(02)00007-1
- Suzuki, K., Taiyoji, M., Sugawar, N., Nikaidou, N., Henrissat, B. and Watanabe, T. (1999) The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem. J. 343, 587-596. https://doi.org/10.1042/0264-6021:3430587
- Prag, G., Vorias, C. E. and Oppenheim, A. B. (2001) Conservation of structural elements and catalytic mechanism in the chitinolytic enzymes from Serratia marcescens; in Chitin Enzymology (Muzzarelli, R. A. A., ed.) p. 351, European Chitin Society, Ancona, Italy.
- Suzuki, K., Sugawara, N., Suzuki, M., Uchiyama, T., Katouno, F. and Nikaidou, N. (2002) Chitinases A, B, and C1 from Serratia marcescens 2170: enzymatic properties and synergism on chitin degradation. Biosci. Biotechnol. Biochem. 66, 1075-1083. https://doi.org/10.1271/bbb.66.1075
- Tsujibo, H., Orikoshi, H., Tanno, H., Fujimoto, K., Miyamoto, K., Imada, C. and Inamori, Y. (1993) Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J. Bacteriol. 175, 111-115. https://doi.org/10.1128/jb.175.1.111-116.1993
-
Perrakis, A., Tew, I., Dauter, Z., Oppenheim, A. B., Chet, I., Wilson, K. S. and Vorgias, C. E. (1994) Crystal structure of a bacterial chitinase at 2.3
${\AA}$ resolution. Structure 2, 1160- 1180. - Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J. and Watanabe, T. (2001) Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem. 276, 41343-41349. https://doi.org/10.1074/jbc.M103610200
- Miyamoto, K., Nukui, E., Itoh, H., Sato, T., Kobayashi, T., Imada, C., Watanabe, E., Inamori, Y. and Tsujibo, H. (2002) Molecular analysis of the gene encoding a novel chitin-binding protease from Alteromonas sp. strain O-7 and its role in the chitinolytic system. J. Bacteriol. 184, 1865-1872. https://doi.org/10.1128/JB.184.7.1865-1872.2002
- Orikoshi, H., Baba, H., Nakayama, S., Kashu, H., Miyamoto, K., Yasuda, M. and Tsujibo, H. (2003) Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from Alteromonas sp. strain O-7. J. Bacteriol. 185, 1153-1159. https://doi.org/10.1128/JB.185.4.1153-1160.2003
- Brurberg, M. B., Nes, I. F. and Eijsink, V. G. (1996) Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142, 1581. https://doi.org/10.1099/13500872-142-7-1581
- van Aalten, D. M. F., Synstad, B., Brurberg, M. B., Hough, E., Riise, B. W., Eijsink, V. G. H. and Wierenga, R. K. (2000) Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proc. Nat. Acad. Sci. U. S. A. 97, 5842-5847. https://doi.org/10.1073/pnas.97.11.5842
- Orikoshi, H., Nakayama, S., Miyamoto, K., Hanato, C., Yasuda, M., Inamori, Y. and Tsujibo, H. (2005) Roles of four chitinases (ChiA, ChiB, ChiC, and ChiD) in the chitin degradation system of marine bacterium Alteromonas sp. Strain O-7. Appl. Environ. Microbiol. 71, 1811-1815. https://doi.org/10.1128/AEM.71.4.1811-1815.2005
- Kudan, S. and Pichyangkura, R. (2009) Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1. Appl. Biochem. Biotechnol. 157(1), 23-35. https://doi.org/10.1007/s12010-008-8328-7
- Takayanagi, T., Ajisaka, K., Takiguchi, Y. and Shimahar, K. (1991) Isolation and characterization of thermostable chitinase from Bacillus licheniformis X-7u. Biochim. Biophys. Acta. 1078, 404-410. https://doi.org/10.1016/0167-4838(91)90163-T
- Trackuk, L. A., Revina, L. P., Shemayakina, T. M., Chestukhina, G. G. and Stepanov, V. M. (1996) Chitinases of Bacillus licheniformis B-6839: isolation and properties. Can. J. Microbiol. 42, 307-315. https://doi.org/10.1139/m96-046
- Tantimavanich, S., Pantuwatana, S., Bhumiratana, A. and Panbangred, W. (1998) Multiple chitinase enzyme from a single gene of Bacillus licheniformis TP-1. J. Ferment. Bioeng. 85, 259-265. https://doi.org/10.1016/S0922-338X(97)85672-3
- Chuang, H. H., Lin, H. Y. and Lin, F. P. (2008) Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis: implication of necessity for enzyme properties. FEBS J. 275, 2240-2254. https://doi.org/10.1111/j.1742-4658.2008.06376.x
- Kuttiyawong, K., Nakapong, S. and Pichyangkura, R. (2008) The dual exo/endo-type mode and the effect of ionic strength on the mode of catalysis of chitinase 60 (CHI60) from Serratia sp. TU09 and its mutants. Carbohydr. Res. 343, 2754-2762. https://doi.org/10.1016/j.carres.2008.05.020
- Sakai, K., Uchiyama, T., Matahira, Y. and Nanjo, F. (1991) Immobilization of chitinolytic enzymes and continuous production of N-acetylglucosamine with the immobilized enzymes. J. Ferment. Bioeng. 72, 168-172. https://doi.org/10.1016/0922-338X(91)90211-X
- Trudel, J. and Asselin, A. (1989) Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178, 362-366. https://doi.org/10.1016/0003-2697(89)90653-2
- Oakley, R. R. and Kirsch, D. R. (1980) Simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105, 361-363. https://doi.org/10.1016/0003-2697(80)90470-4
- Imoto, T. and Yagishita, K. (1971) A simple activity measurement of lysozyme. Agri. Biol. Chem. 35, 1154-1156. https://doi.org/10.1271/bbb1961.35.1154
- Tanaka, T., Fujuwara, S., Nishikori, S., Fukui, T., Takagi, M. and Imanaka, T. (1999) A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic Archaeon Pyrococcus kodakaraensis KOD1. Appl. Environ. Microbiol. 65, 5338-5344.