Characterization of a Ginsenoside-Transforming beta-glucosidase from Paenibacillus mucilaginosus and Its Application for Enhanced Production of Minor Ginsenoside F-2

Abstract

A novel beta-glucosidase (BglPm) was identified from Paenibacillus mucilaginosus KCTC 3870(T) which has ginsenoside converting activity. The gene, termed bglPm, consists of 1,260 bp and belongs to glycoside hydrolase family 1 (GH1). After being overexpressed and purified from Escherichia coli, the enzymatic properties of BglPm were investigated. The enzyme exhibited an optimal activity at 45 degrees C and pH 7.5 and showed high bioconversion ability for major ginsenoside Rb-1 and Rd into ginsenoside F-2. Thus, it was used for mass production of relatively high pure F-2 from relatively abundant protopanaxadiol type ginsenosides mixture (PPDGM) with combined usage of ginsenoside Rc-hydrolyzing enzyme. Scale-up of production using 250 g of the PPDGM resulted in 152 g of F-2 with 80.1% chromatography purity and 95.7% recovery. These results suggest that this enzyme would be useful in the preparation of pharmacologically active ginsenoside F-2 in the functional food and pharmaceutical industries.