Expression of a Pleurotus ostreatus Versatile Peroxidase Gene in Pichia pastoris and Its Degradation of Corn Stover Lignin
The Pleurotus ostreatus versatile peroxidase gene was transferred into Pichia pastoris strain X33 and expression was achieved.The enzymatic properties of recombinant yeast were deter-mined and its ability to degrade corn stover lignin was determined.The results showed that the opti-mal pH values for the decomposition of 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonic acid,2,6-dimethoxyphenol,2-methoxyphenol and veratryl alcohol by recombinant versatile peroxidase were 2.5,3,3.5 and 4.5,respectively.Except for the optimum reaction temperature for decomposition vera-tryl alcohol,which was 40 ℃,the optimum temperature of other substrates was 50 ℃,and it had good thermal stability and acid and alkali resistance.The degradation rates of lignin in corn stover by re-combinant multifunctional peroxidase and by native Pleurotus ostreatus were 23.59％and 10.93％,re-spectively.The results provide a theoretical basis for studying the mechanism of lignin degradation by versatile peroxidase.
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