Abstract
A cold-active ionically bound cell wall peroxidase was purified from a polyvinylpolypyrrolidone extract of mature vanilla beans by ultra filtration of 10 kDa and gel filtration chromatography on Sephacryl S-200. The M r was 46.5 kDa determined by electrophoresis on SDS–PAGE, while native gel filtration confirmed tetramer enzyme form of approximately 186 kDa. The optimum pH and temperature were 3.8 and 16 °C, respectively, as determined with guaiacol as the substrate ( K m 3.8 mmol/L). The p I was approximately 7.7. The POD was inhibited by 1,4-dithiothreitol, β-mercaptoethanol and sodium azide. The POD showed decreasing activity in the presence of ascorbic acid, NaEDTA and sodium dodecyl sulfate at 1 mmol/L. The enzyme lost 80% of its activity in the presence of 20% ethanol. These results will permit better understanding of POD role in vanilla curing process.
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