Isolation and characterization of novel ginsenoside-hydrolyzing glycosidase from Microbacterium esteraromaticum that transforms ginsenoside Rb2 to rare ginsenoside 20( S)-Rg3.

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 of enzyme in 20 mM sodium phosphate buffer at 40 °C and pH 7.0, 1.0 mg ml ginsenoside Rb2 was transformed into 0.47 mg ml 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. [ABSTRACT FROM AUTHOR]