Abstract

SUMMARYThe cellulase system of Poronia punctata has properties similar to that of other fungi. Poronia punctata cellulase assays on carboxymethyl cellulose (CMC) demonstrated major and minor peaks of activity at pH 4.8 and 5.6 respectively. A side peak of activity occurred at pH 4.4 but its exact nature or relationship to CMC hydrolysis is unclear. Poronia punctata cellulase assays on microcrystalline cellulose (MCC) and filter paper demonstrated reversed pH values for major and minor peaks of hydrolysis compared to the CMC experiments; the major peak of activity occurred at pH 5.5 with the minor peak at pH 4.6. These results suggest the presence of a dual enzyme system in P. punctata. Optimal temperature activities for P. punctata cellulase were demonstrated to be 55 C with CMC as substrate and 45 C with filter paper and MCC as substrates. Assays using filter paper as a substrate do not rise above 1% total conversion to reducing sugar; with MCC as substrate, approximately 2.7% is converted, and with CMC as substrate a yield of 4.7% is obtained.

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