Title of article :
Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1
Author/Authors :
Snehasish Basu، نويسنده , , Abhrajyoti Ghosh، نويسنده , , Amit Bera، نويسنده , , Manabendra N. Saha، نويسنده , , Dhrubajyoti Chattopadhyay، نويسنده , , Krishanu Chakrabarti، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Pages :
7
From page :
8088
To page :
8094
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.
Keywords :
Bacillus pumilus DKS1Pectate lyaseThermodynamic activation and inactivationparameters
Journal title :
Bioresource Technology
Serial Year :
2008
Journal title :
Bioresource Technology
Record number :
413928
Link To Document :
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