Purification and Characterization of a Bioscouring Pectate Lyase from Paenibacillus sp. WZ008 with High Activity on Pectin

摘要

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 Ca~(2+) addition while the enzyme exhibited the maximal activity on polygalacturonic acid in the presence of 4 mM Ca~(2+). The purified enzyme demonstrated the optimum activity at a temperature range of 55-60°C and pH 9.6. The Ca~(2+) ion enhanced the enzyme activity but Mn~(2+), Ba~(2+) and EDTA strongly inhibited it.