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• W2001962823 abstract "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−1 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." @default.
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• W2001962823 date "2012-10-01" @default.
• W2001962823 modified "2023-10-10" @default.
• W2001962823 title "Enzymatic transformation of the major ginsenoside Rb2 to minor compound Y and compound K by a ginsenoside-hydrolyzing β-glycosidase from <i>Microbacterium esteraromaticum</i>" @default.
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• W2001962823 doi "https://doi.org/10.1007/s10295-012-1158-1" @default.
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