从可降解片状几丁质的海洋细菌嗜水气单胞菌H-2330中分离并鉴定几丁质酶
Isolation and characterization of chitinase from a flake-chitin degrading marine bacterium, Aeromonas hydrophila H-2330.
作者信息
Hiraga K, Shou L, Kitazawa M, Takahashi S, Shimada M, Sato R, Oda K
机构信息
Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Japan.
出版信息
Biosci Biotechnol Biochem. 1997 Jan;61(1):174-6. doi: 10.1271/bbb.61.174.
A flake-chitin degrading marine bacterium was isolated and identified as Aeromonas hydrophila. This strain secreted five chitinases and an beta-N-acetylglucosaminidase. The main chitinase (Chi-A) was purified and characterized. The optimum pH of Chi-A was 5-8, and the activity was inhibited by Hg2+ and Fe3+. Chi-A was different from chitinases of other Aeromonas species with respect to molecular weight (62,000) and insensitivity to monoiodoacetate. The amino-terminal amino acid sequence showed extensive similarity with chitinases from Gram-negative bacteria.
分离出一株能降解片状几丁质的海洋细菌，鉴定为嗜水气单胞菌。该菌株分泌五种几丁质酶和一种β-N-乙酰氨基葡萄糖苷酶。对主要的几丁质酶（Chi-A）进行了纯化和特性分析。Chi-A的最适pH为5-8，Hg2+和Fe3+会抑制其活性。Chi-A在分子量（62,000）和对碘乙酸的不敏感性方面与其他嗜水气单胞菌属的几丁质酶不同。其氨基末端氨基酸序列与革兰氏阴性菌的几丁质酶具有广泛的相似性。
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