Purification and Characterization of Three Extracellular Protopectinases with Polygalacturonase Activities from Trichosporon penicillatum.

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  • Purification and Characterization of Three Extracellular Protopectinases with Polygalacturonase Activities from<i>Trichosporon penicillatum</i>

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In a culture filtrate of Trichosporon penicillatum B2, which is a γ-ray irradiation mutant induced from T. penicillatum SNO3, we found three kinds of pectin-releasing enzymes, protopectinases SE1, SE2, and SE3, that have endo-polygalacturonase activity. These enzymes were purified to homogeneity with cation-exchange and size exclusion chromatographies. The major PPase in the culture filtrate was PPase SE1, which accounted for 75% of total activities in the culture filtrate, and the two others were 0.15% (PPase SE2) and 0.007% (PPase SE3). Their molecular masses were approximdtely 41, 41 and 42 kDa on SDS-PAGE, respectively. They had similar enzymatic propertied but different PPase activity and pH- and thermo-stability. Antibody against PPase S, which is produced by strain SNO3, inhibited the activities of PPase SE1, SE2, and SE3. However PPase SE1 was completely inhibited by treatment with the anti-PPase S antibody, but the activities of PPases SE2 and SE3 remained at 20 and 50% of the original activity, respectively.

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