Biotransformation of ginsenosides Re and Rg1 into ginsenosides Rg2 and Rh1 by recombinant β-glucosidase

Abstract

Ginsenosides Re and Rg1 were transformed by recombinant β-glucosidase (Bgp1) to ginsenosides Rg2 and Rh1, respectively. The bgp1 gene consists of 2,496bp encoding 831 amino acids which have homology to the glycosyl hydrolase families 3 protein domain. Using 0.1mg enzyme ml(-1) in 20mM sodium phosphate buffer at 37°C and pH 7.0, the glucose moiety attached to the C-20 position of ginsenosides Re and Rg1, was removed: 1mg ginsenoside Re ml(-1) was transformed into 0.83mg Rg2ml(-1) (100% molar conversion) after 2.5h and 1mg ginsenoside Rg1ml(-1) was transformed into 0.6mg ginsenoside Rh1ml(-1) (78% molar conversion) in 15min. Using Bgp1 enzyme, almost all initial ginsenosides Re and Rg1 were converted completely to ginsenosides Rg2 and Rh1. This is the first report of the conversion of ginsenoside Re to ginsenoside Rg2 and ginsenoside Rg1 to ginsenoside Rh1 using the recombinant β-glucosidase.