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

Basu, Snehasish ; Ghosh, Abhrajyoti ; Bera, Amit ; Saha, Manabendra N. ; Chattopadhyay, Dhrubajyoti ; Chakrabarti, Krishanu (2008) Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1 Bioresource Technology, 99 (17). pp. 8088-8094. ISSN 0960-8524

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S09608...

Related URL: http://dx.doi.org/10.1016/j.biortech.2008.03.032

Abstract

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°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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Bacillus pumilus DKS1; Pectate Lyase; Thermodynamic Activation and Inactivation Parameters
ID Code:10258
Deposited On:04 Nov 2010 06:46
Last Modified:29 Jan 2011 08:40

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