LAUSR

The recombinant thermostable β-glucosidase from Thermotoga thermarum DSM 5069T exhibited high selectivity to catalyze the conversion of ginsenoside Re and Rg1 to the more pharmacologically active minor ginsenoside Rg2 and Rh1, respectively. At a concentration of 1.36 U/mL of the enzyme, a temperature of 85°C, and pH 5.5, 10 g/L ginsenoside Re was transformed into 8.02 g/L Rg2 within 60 min, and 2 g/L ginsenoside Rg1 was transformed into 1.56 g/L Rh1 within 60 min. This paper provides the first report on the production of ginsenoside Rg2 and Rh1 by a highly thermostable β-glucosidase.