| Title | Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd |
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| Author | Myung Keun Park 1, Chang-Hao Cui 1, Sung Chul Park 2, Seul-Ki Park 3, Jin-Kwang Kim 3, Mi-Sun Jung 4, Suk-Chae Jung 1,2, Mi-Sun Jung 4, Suk-Chae Jung 1,2, Sun-Chang Kim 1,2,3, and Wan-Taek Im 5* |
| Address | 1Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea, 2Intelligent Synthetic Biology Center, Daejeon 305-701, Republic of Korea, 3KAIST Institute for Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea, 4Youngdong University, 310, Chungbuk 370-701, Republic of Korea, 5Department of Biotechnology, Hankyoung National Univeristy, Kyonggi-do 456-749, Republic of Korea |
| Bibliography | Journal of Microbiology, 52(5),399-406, 2014, |
| DOI | DOI 10.1007/s12275-014-3601-7 |
| Key Words | biotransformation, β-glucosidase, recombinant enzyme, minor ginsenoside, Arthrobacter chlorophenolicus |
| Abstract | The focus of this study was the cloning, expression, and characterization of recombinant ginsenoside hydrolyzing β-glucosidase from Arthrobacter chlorophenolicus with an ultimate objective to more efficiently bio-transform ginse-nosides. The gene bglAch, consisting of 1,260 bp (419 amino acid residues) was cloned and the recombinant enzyme, over-expressed 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°C) BglAch hydrolyzed the outer glucose and arabino-pyranose moieties of ginsenosides Rb1 and Rb2 at the C20 position of the aglycone into ginsenoside Rd. This was fol-lowed by hydrolysis into F2 of the outer glucose moiety of ginsenoside Rd at the C3 position of the aglycone. Additio-nally, BglAch more slowly transformed Rc to F2 via C-Mc1 (compared to hydrolysis of Rb1 or Rb2). These results in-dicate that the recombinant BglAch could be useful for the production of ginsenoside F2 for use in the pharmaceutical and cosmetic industries. |