红链霉菌产生的几丁质酶的纯化与特性分析

Purification and characterization of chitinase produced by Streptomyces erythraeus.

作者信息

Hara S, Yamamura Y, Fujii Y, Mega T, Ikenaka T

机构信息

Department of Chemistry, Osaka University College of Science.

出版信息

J Biochem. 1989 Mar;105(3):484-9. doi: 10.1093/oxfordjournals.jbchem.a122691.

DOI:10.1093/oxfordjournals.jbchem.a122691

PMID:2732220

Abstract

A chitinase was purified from the culture filtrate of Streptomyces erythraeus (SE). The enzyme (SE chitinase) has a molecular weight of 30,000 and pI 3.7, and shows optimal activity at pH 5.0 with an optimal ionic strength of less than 0.2 M NaCl. SE chitinase could hydrolyze chitin and its derivatives, but could not hydrolyze cell walls of Micrococcus lysodeikticus. The substrate specificity of SE chitinase was compared with those of hen egg white (HEW) and SE lysozymes. The binding mode of the chitinase to substrates was investigated using chitooligosaccharides and their derivatives. The results showed that the binding mode of SE chitinase to the substrate is similar to that of HEW and SE lysozymes.

摘要

从红色链霉菌（SE）的培养滤液中纯化出一种几丁质酶。该酶（SE几丁质酶）的分子量为30,000，等电点为3.7，在pH 5.0时表现出最佳活性，最佳离子强度小于0.2 M NaCl。SE几丁质酶可以水解几丁质及其衍生物，但不能水解溶壁微球菌的细胞壁。将SE几丁质酶的底物特异性与鸡蛋清（HEW）和SE溶菌酶的底物特异性进行了比较。使用壳寡糖及其衍生物研究了几丁质酶与底物的结合模式。结果表明，SE几丁质酶与底物的结合模式与HEW和SE溶菌酶的相似。