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A novel ginsenoside-hydrolyzing beta-glucosidase was purified from Paecilomyces Bainier sp. 229 by a combination of QSepharose FF, phenyl-Sepharose CL-4B, and CHT ceramic hydroxyapatite column chromatographies. The purified enzyme was a monomeric protein with a molecular mass estimated to be 115 kDa. The optimal enzyme activity was observed at pH 3.5 and(More)
The title compound, C(41)H(70)O(12)·CH(4)O, was prepared by microbial transformation. Within the steroid skeleton of the mol-ecule, three six-membered rings exhibit a chair conformation, while the five -membered ring adopts an envelope conformation. The two pyranosyl rings also adopt chair conformations. The mol-ecules are held together by an extensive(More)
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