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Purification and Characterization of a Bioscouring Pectate Lyase from Paenibacillus sp. WZ008 with High Activity on Pectin
Abstract:
An extracellular pectate lyase was purified from the culture supernatant of Paenibacillus sp. WZ008 grown in the pectin-containing medium. The enzyme was purified to homogeneity in three steps and found to have a molecular weight of around 45 kDa. Highly methylated pectin was the optimum substrate in the case of no Ca2+ addition while the enzyme exhibited the maximal activity on polygalacturonic acid in the presence of 4 mM Ca2+. The purified enzyme demonstrated the optimum activity at a temperature range of 55-60°C and pH 9.6. The Ca2+ ion enhanced the enzyme activity but Mn2+, Ba2+ and EDTA strongly inhibited it.
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457-461
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January 2012
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© 2012 Trans Tech Publications Ltd. All Rights Reserved
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