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General Biochemical Characterization of Thermostable Extracellular beta-Amylase from Clostridium thermosulfurogenes.嗜热硫还原梭菌耐热胞外β-淀粉酶的一般生化特性。
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Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences.一株嗜碱芽孢杆菌分离株中新型液化α-淀粉酶的酶学性质、完整核苷酸序列及氨基酸序列
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从蜡状芽孢杆菌中提取、纯化和表征耐热耐碱α-淀粉酶。

Extraction, Purification and Characterization of Thermostable, Alkaline Tolerant α-Amylase from Bacillus cereus.

机构信息

CAS in Marine Biology, Annamalai University, Parangipettai, 608502 India.

出版信息

Indian J Microbiol. 2011 Oct;51(4):424-9. doi: 10.1007/s12088-011-0160-z. Epub 2011 Feb 13.

DOI:10.1007/s12088-011-0160-z
PMID:23024403
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3209940/
Abstract

Thermostable alkaline α-amylase producing bacterium Bacilluscereus strain isolated from Cuddalore harbour waters grew maximally in both shake flask and fermentor, and produced α-amylase at 35°C, pH 7.5 and 1.0% of substrate concentrations. α-Amylase activity was maximum at 65°C, pH 8.0, 89% of its activity was sustained even at pH 11.0. Added with MnCl(2,) α-amylase activity showed 4% increase but it was inhibited by EDTA. The molecular weight of the purified α-amylase is 42 kDa.

摘要

从库达洛尔港水中分离出的产热碱性α-淀粉酶的芽孢杆菌菌株在摇瓶和发酵罐中均能最大程度地生长，并在 35°C、pH7.5 和 1.0%的底物浓度下产生α-淀粉酶。α-淀粉酶活性在 65°C、pH8.0 时达到最大值，其活性在 pH11.0 时仍保持 89%。加入 MnCl2 后，α-淀粉酶活性增加了 4%，但被 EDTA 抑制。纯化的α-淀粉酶的分子量为 42 kDa。