来自嗜热紫链霉菌OPC-520的一种耐热几丁质酶的纯化及性质
Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520.
作者信息
Tsujibo H, Minoura K, Miyamoto K, Endo H, Moriwaki M, Inamori Y
机构信息
Osaka University of Pharmaceutical Sciences, Japan.
出版信息
Appl Environ Microbiol. 1993 Feb;59(2):620-2. doi: 10.1128/aem.59.2.620-622.1993.
Abstract
A chitinase was purified from the culture filtrate of Streptomyces thermoviolaceus OPC-520. The enzyme showed a high optimum temperature (70 to 80 degrees C), a high optimum pH level (8.0 to 10.0), and heat stability. This enzyme showed high sequence homology with chitinases from Serratia marcescens QMB1466 and Bacillus circulans WL-12.
摘要
从嗜热紫链霉菌OPC - 520的培养滤液中纯化出一种几丁质酶。该酶表现出较高的最适温度（70至80摄氏度）、较高的最适pH值水平（8.0至10.0）以及热稳定性。这种酶与粘质沙雷氏菌QMB1466和环状芽孢杆菌WL - 12的几丁质酶具有高度的序列同源性。
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