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- Title
Enzymatic transformation of the major ginsenoside Rb2 to minor compound Y and compound K by a ginsenoside-hydrolyzing β-glycosidase from Microbacterium esteraromaticum.
- Authors
Quan, Lin-Hu; Jin, Yan; Wang, Chao; Min, Jin-Woo; Kim, Yeon-Ju; Yang, Deok-Chun
- Abstract
The ginsenoside-hydrolyzing β -glycosidase (Bgp3) derived from Microbacterium esteraromaticum transformed the major ginsenoside Rb2 to more pharmacologically active minor ginsenosides including compounds Y and K. The bgp3 gene consists of 2,271 bp encoding 756 amino acids which have homology to the glycosyl hydrolase family 3 protein domain. Bgp3 is capable of hydrolyzing beta-glucose links and arabinose links. HPLC analysis of the time course of ginsenoside Rb2 hydrolysis by Bgp3 (0.1 mg enzyme ml in 20 mM sodium phosphate buffer at 40 °C and pH 7.0) showed that the glycosidase first hydrolyzed the inner glucose moiety attached to the C-3 position and then the arabinopyranose moiety attached to the C-20 position. Thus, Bgp3 hydrolyzed the ginsenoside Rb2 via the following pathway: Rb2 → compound Y → compound K.
- Subjects
GINSENOSIDES; ENZYMATIC analysis; BACTERIAL transformation; GLYCOSIDASES; MICROBACTERIUM; PHARMACOLOGY
- Publication
Journal of Industrial Microbiology & Biotechnology, 2012, Vol 39, Issue 10, p1557
- ISSN
1367-5435
- Publication type
Article
- DOI
10.1007/s10295-012-1158-1