A型产气荚膜梭菌胞外α-淀粉酶的纯化与特性分析
Purification and characterization of an extracellular alpha-amylase from Clostridium perfringens type A.
作者信息
Shih N J, Labbé R G
机构信息
Department of Food Science, University of Massachusetts, Amherst 01003, USA.
出版信息
Appl Environ Microbiol. 1995 May;61(5):1776-9. doi: 10.1128/aem.61.5.1776-1779.1995.
Abstract
An alpha-amylase (EC 3.2.1.1) secreted by Clostridium perfringens NCTC 8679 type A was purified to homogeneity and characterized. It was isolated from concentrated cell-free culture medium by ion-exchange and gel permeation chromatography. The enzyme exhibited maximal activity at pH 6.5 and 30 degrees C without the presence of calcium. The pI of the enzyme was 4.75. The estimated molecular weight of the purified enzyme was 76 kDa. The purified enzyme was inactivated between 35 and 40 degrees C, which increased to between 45 and 50 degrees C in the presence of calcium (5 mM). The purified enzyme produced a mixture of oligosaccharides as major end products of starch hydrolysis, indicating alpha-amylase activity.
摘要
对A型产气荚膜梭菌NCTC 8679分泌的一种α淀粉酶（EC 3.2.1.1）进行了纯化并鉴定其特性。通过离子交换和凝胶渗透色谱从浓缩的无细胞培养基中分离得到该酶。该酶在pH 6.5和30℃且不存在钙的情况下表现出最大活性。该酶的等电点为4.75。纯化酶的估计分子量为76 kDa。纯化酶在35至40℃之间失活，在存在5 mM钙的情况下，失活温度范围升高至45至50℃。纯化酶产生寡糖混合物作为淀粉水解的主要终产物，表明具有α淀粉酶活性。
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