Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1 |
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Authors: | Basu Snehasish Ghosh Abhrajyoti Bera Amit Saha Manabendra N Chattopadhyay Dhrubajyoti Chakrabarti Krishanu |
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Institution: | Department of Biochemistry, University College of Science, Calcutta University, 35 Ballygunge Circular Road, West Bengal, Kolkata 700 019, India. |
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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 35kDa. The purified enzyme exhibited maximal activity at a temperature of 75 degrees C and pH 8.5. The presence of 1mM 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. |
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