Studies on Pectic Enzymes of Microorganisms

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Abstract
Endo-polygalacturonase (endo-PG) of Aspergillus saitoi was purified through ammonium sulfate fractionation, Amberlite IRC-50 column chromatography, and several combinations of Sephadex column chromatography. The purified endo-PG, which was almost homogeneous ultracentrifugally and electro -phoretically, had the sedimentation constant of 2.2 S and the absorption maximum at 277 m[mu]. Its optimum pH and temperature were 4.8-5.0 and 45[degree]C, respectively, and it was most stable between pH 4.0 and 6.0, but over 90% of the activity was lost at 50[degree]C for 10 min. The purified enzyme was a typical endo-PG, and hydrolyzed about 60% and 17% of glycosidic linkage of polygalacturonic acid and pectin, respectively. This enzyme preparation had no pectlnesterase, trans-ellminase, and apple juice-clarifying activities, but macerated potato tuber slices singly.

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