| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 684534 | Bioresource Technology | 2008 | 7 Pages |
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
Related Topics
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Process Chemistry and Technology
Authors
Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Manabendra N. Saha, Dhrubajyoti Chattopadhyay, Krishanu Chakrabarti,