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Updated: May 11, 2026

Screening and Isolation of C-Glycoside-Cleaving Intestinal Bacteria
Published on: February 28, 2025
Isolation and characterization of novel ginsenoside-hydrolyzing glycosidase from Microbacterium esteraromaticum that
Lin-Hu Quan1, Chao Wang, Yan Jin
1Department of Oriental Medicinal Material and Processing, College of Life Science, Kyung-Hee University, Seocheon-dong, Giheung-gu, Yongin-si, Gyeonggi-do, 446-701, Republic of Korea. linhuk10@gmail.com
Abstract:
Ginsenoside Rb2 was transformed by recombinant glycosidase (Bgp2) into ginsenosides Rd and 20(S)-Rg3. The bgp2 gene consists of 2,430 bp that encode 809 amino acids, and this gene has homology to the glycosyl hydrolase family 2 protein domain. SDS-PAGE was used to determine that the molecular mass of purified Bgp2 was 87 kDa. Using 0.1 mg ml(-1) of enzyme in 20 mM sodium phosphate buffer at 40 °C and pH 7.0, 1.0 mg ml(-1) ginsenoside Rb2 was transformed into 0.47 mg ml(-1) ginsenoside 20(S)-Rg3 within 120 min, with a corresponding molar conversion yield of 65 %. Bgp2 hydrolyzed the ginsenoside Rb2 along the following pathway: Rb2 → Rd → 20(S)-Rg3. This is the first report of the biotransformation of ginsenoside Rb2 to ginsenoside 20(S)-Rg3 using the recombinant glycosidase.
