Purification and characterization of two novel β-glucosidases from Penicillium oxalicum and their application in bioactive ginsenoside production. (August 2014)

• Record Type: Journal Article
• Authors: Gao, Juan; Wang, Jiao; Cui, Jing; Wang, Nan; Bai, Yeming; Yuan, Ye; Zhou, Yifa
• Is Part Of: Biocatalysis and biotransformation. Volume 32:Number 4(2014)
• Page Start: 199
• Page End: 207
• Publication Date: 2014-08
• Subjects: Enzymes -- Biotechnology -- Periodicals; Enzymes -- Industrial applications -- Periodicals; Biotransformation (Metabolism) -- Periodicals; 660.63
• DOI: 10.3109/10242422.2014.934365
• Languages: English
• ISSNs: 1024-2422

Abstract

<abstract> <title>Abstract</title> <p>The fungus <italic>Penicillium oxalicum</italic> is able to selectively metabolize the 20(S)-protopanaxadiol ginsenosides Rb1, Rb2 and Rc to the bioactive ginsenoside compound K using extracellular glycosidases. In this study, two novel extracellular ginsenoside-hydrolyzing enzymes GH3-1 and GH3-2 were purified and characterized from <italic>P. oxalicum</italic> culture. Using ginsenosides as substrates, GH3-1 and GH3-2 synergistically catalyzed the hydrolysis of Rb1, Rb2 and Rc to yield the final product Compound K (C-K). The hydrolysis pathways were determined to be: Rb1→Rd→F2→C-K, Rb2→CO→CY→C-K and Rc→Mb→Mc→C-K for GH3-1 and GH3-2, respectively. The two enzymes differ, especially in composition, molecular weight, stability and substrate specificity, from GH1, a glycosidase previously purified from the same fungus. These enzymes could be of interest in glycoside degradation, especially in the production of minor ginsenosides.</p> </abstract>