Characterization of recombinant beta -glucosidase from Arthrobacter chlorophenolicus and biotransformation of ginsenosides Rb sub(1), Rb sub(2), Rc, and Rd

• Published in: The journal of microbiology 2014-05, Vol.52 (5), p.399-406
• Main Authors: Park, Myung Keun, Cui, Chang-Hao, Park, Sung Chul, Park, Seul-Ki, Kim, Jin-Kwang, Jung, Mi-Sun, Jung, Suk-Chae, Kim, Sun-Chang, Im, Wan-Taek
• Format: Article
• Language: English
• Subjects: Arthrobacter; Escherichia coli
• ISSN: 1225-8873; 1976-3794
• DOI: 10.1007/s12275-014-3601-7

The focus of this study was the cloning, expression, and characterization of recombinant ginsenoside hydrolyzing beta -glucosidase from Arthrobacter chlorophenolicus with an ultimate objective to more efficiently bio-transform ginsenosides. The gene bglAch, consisting of 1,260 bp (419 amino acid residues) was cloned and the recombinant enzyme, overexpressed in Escherichia coli BL21 (DE3), was characterized. The GST-fused BglAch was purified using GST.Bind agarose resin and characterized. Under optimal conditions (pH 6.0 and 37 degree C) BglAch hydrolyzed the outer glucose and arabinopyranose moieties of ginsenosides Rb1 and Rb2 at the C20 position of the aglycone into ginsenoside Rd. This was followed by hydrolysis into F sub(2) of the outer glucose moiety of ginsenoside Rd at the C3 position of the aglycone. Additionally, BglAch more slowly transformed Rc to F sub(2) via C-Mc sub(1) (compared to hydrolysis of Rb sub(1) or Rb sub(2)). These results indicate that the recombinant BglAch could be useful for the production of ginsenoside F sub(2) for use in the pharmaceutical and cosmetic industries.