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A novel β-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°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.

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Characterization of a Ginsenoside-Transforming β-glucosidase from Paenibacillus mucilaginosus and Its Application for Enhanced Production of Minor Ginsenoside F2