Identification and characterization of a novel intracellular alkaline α-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8

被引：50

作者：

Ballschmiter, M ^{[1
]}

Fütterer, O ^{[1
]}

Liebl, W ^{[1
]}

机构：

[1] Univ Gottingen, Inst Mikrobiol & Genet, D-37077 Gottingen, Germany

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2006年 / 72卷 / 03期

关键词：

D O I：

10.1128/AEM.72.3.2206-2211.2006

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The gene for a novel alpha-amylase, designated AmyC, from the hyperthermophilic bacterium Thermotoga maritima was cloned and heterologously overexpressed in Escherichia coli. The putative intracellular enzyme had no amino acid sequence similarity to glycoside hydrolase family (GHF) 13 alpha-amylases, yet the range of substrate hydrolysis and the product profile clearly define the protein as an alpha-amylase. Based on sequence similarity AmyC belongs to a subgroup within GHF 57. On the basis of amino acid sequence similarity, Glu185 and Asp349 could be identified as the catalytic residues of AmyC. Using a 60-min assay, the maximum hydrolytic activity of the purified enzyme, which was dithiothreitol dependent, was found to be at 90 degrees C. AmyC displayed a remarkably high pH optimum of pH 8.5 and an unusual sensitivity towards both ATP and EDTA.

引用

页码：2206 / 2211

页数：6

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