Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd

Myung Keun Park; Chang-Hao Cui; Sung Chul Park; Seul-Ki Park; Jin-Kwang Kim; Mi-Sun Jung; Suk-Chae Jung; Mi-Sun Jung; Suk-Chae Jung; Sun-Chang Kim; Wan-Taek Im

doi:10.1007/s12275-014-3601-7

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Research Support, Non-U.S. Gov't
Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd: 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, Wan-Taek Im ⁵; Journal of Microbiology 2014;52(5):399-406.
DOI: https://doi.org/10.1007/s12275-014-3601-7
Published online: May 9, 2014

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 Korea¹Department 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

Corresponding author: Wan-Taek Im , Tel: +82-42-3504451,

Received: 18 November 2013 • Revised: 24 December 2013 • Accepted: 24 December 2013

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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.

Keywords: biotransformation;β-glucosidase;recombinant enzyme;minor ginsenoside;Arthrobacter chlorophenolicus

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Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd

J. Microbiol. 2014;52(5):399-406. Published online May 9, 2014

DOI: https://doi.org/10.1007/s12275-014-3601-7

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