A novel ginsenoside-hydrolyzing enzyme from Penicillium oxalicum and its application in ginsenoside Rd production. (December 2013)

• Record Type: Journal Article
• Authors: Gao, Juan; Hu, Yanbo; Ji, Li; Wang, Nan; Wang, Jiao; Tai, Guihua; Zhou, Yifa
• Is Part Of: Biocatalysis and biotransformation. Volume 31:Number 6(2013)
• Page Start: 305
• Page End: 312
• Publication Date: 2013-12
• Subjects: Enzymes -- Biotechnology -- Periodicals; Enzymes -- Industrial applications -- Periodicals; Biotransformation (Metabolism) -- Periodicals; 660.63
• DOI: 10.3109/10242422.2013.857316
• Languages: English
• ISSNs: 1024-2422

Abstract

<abstract> <title>Abstract</title> <p>The fungus <italic>Penicillum oxalicum</italic> can selectively metabolize the major 20(S)-protopanaxadiol ginsenosides Rb1, Rb2, and Rc using extracellular glycosidases yielding a series of bioactive metabolites. A β-glucosidase GH1 was purified from the culture of <italic>P. oxalicum</italic> with a yield of 9.5% and a specific activity of 3.9 × 10³ U/mg. GH1 was a tetramer with a native molecular weight of 484 kDa and its <italic>p</italic>I value was pH 4.2. GH1 specifically cleaved the β-(1-6)-glucosidic linkage at C-20 site of ginsenoside Rb1 to give the sole product Rd. The optimum conditions were established to be pH 4.5, 55°C, and 0.25 U/ml purified enzyme at 2 mg/ml ginsenoside Rb1. GH1 could be used in the pharmaceutical industry.</p> </abstract>