Purification and Characterization of a Rhamnogalacturonase with Protopectinase Activity from Trametes sanguinea

Publisher Website
Google Scholar
Abstract
In a culture filtrate of Trametes sanguinea IFO 6490, we found a protopectin‐solubilizing enzyme, protopectinase‐T, that did not degrade polygalacturonic acid. The enzyme was purified to homogeneity with hydrophobia, cation‐exchange, anion‐exchange, and size‐exclusion chromatographies. It had an apparent molecular mass of 55 kDa by SDS/PAGE and 39 kDa by size‐exclusion chromatography on Superose 12. The isoelectric point was at pH 8.1. Protopectinase‐T was stable from pH 3.0 to 6.0 and at temperatures up to 50°C. The optimum pH for enzyme activity was 4.0 at 37°C, and the optimum temperature was 50°C at pH 5.0. Protopectinase‐T catalyzed the release of highly polymerized pectin from lemon peel protopectin.

This publication has 30 references indexed in Scilit: