Indexed on: 01 Oct '13Published on: 01 Oct '13Published in: Biotechnology Letters
The specific activity of a recombinant β-glucosidase from Pyrococcus furiosus for protopanaxatriol (PPT)-type ginsenosides followed the order Rf > R1 > Re > R2 > Rg2, which were converted to Rh1, Rg1, Rg1, Rh1, and Rh1, respectively. No activity was observed with Rg1 and Rh1. Thus, P. furiosus β-glucosidase hydrolyzed the outer glycoside at the C-6 position in PPT-type ginsenosides whereas the enzyme did not hydrolyze the inner glucoside at the C-6 position and the glucoside at the C-20 position. The activity for Rf was optimal at 95 °C, pH 5.5, 5 mM ginsenoside, and 32 U enzyme l−1. Under these conditions, P. furiosus β-glucosidase completely converted from R1 to Rg1 after 10 h, with a productivity of 0.4 g l−1 h−1 and completely converted Rf to Rh1 after 1.2 h, with a productivity of 2.74 g l−1 h−1.