Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1

被引：34

作者：

Basu, Snehasish ^{[1
]}

Ghosh, Abhrajyoti ^{[1
]}

Bera, Amit ^{[1
]}

Saha, Manabendra N.

Chattopadhyay, Dhrubajyoti ^{[1
]}

Chakrabarti, Krishanu ^{[1
]}

机构：

[1] Univ Calcutta, Univ Coll Sci, Dept Biochem, Kolkata 700019, W Bengal, India

来源：

BIORESOURCE TECHNOLOGY | 2008年 / 99卷 / 17期

关键词：

Bacillus pumilus DKS1; pectate lyase; thermodynamic activation and inactivation parameters;

D O I：

10.1016/j.biortech.2008.03.032

中图分类号：

S2 [农业工程];

学科分类号：

0828 ;

摘要：

An extracellular pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 degrees C and pH 8.5. The presence of 1 mM calcium and manganese enhanced pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy-enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this pectate lyase may have potential implications in fibre degumming. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：8088 / 8094

页数：7

共 42 条

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