Biocatalytic resolution of glycidyl phenyl ether using a novel epoxide hydrolase from a marine bacterium,Rhodobacterales bacterium HTCC2654 |
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| Authors: | Jung-Hee Woo Ji-Hyun Kang Young-Ok Hwang Jang-Cheon Cho Sang-Jin Kim Sung Gyun Kang |
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| Affiliation: | 1. From the Marine Biotechnology Research Centre, Korea Ocean Research and Development Institute, Ansan, P. O. Box 29, 425-600, Korea;2. Division of Biology and Ocean Sciences, Inha University, Incheon 402-751, Korea;3. Gyeongbuk Institute for Marine Bio-Industry, Uljin 767-813, Gyeongbuk, Korea;1. Department of Chemistry and Earth Sciences, College of Arts and Sciences, Qatar University, P.O. Box 2713, Doha, Qatar;2. Department of Physics, Hashemite University, P.O. Box 150459, Zarqa 13115, Jordan;1. College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 211816, China;2. School of Chemistry & Environmental Engineering, Jiangsu University of Technology, Changzhou 213001, China;1. Technical Development, R&D Department, MAG-ISOVER K.K., 2046-1 Kami-inayoshi, kasumigaura-shi, Ibaraki 315-8518, Japan;2. Department of Electrical Engineering, Nagaoka University of Technology, 1603-1 Kamitomioka-cho, Nagaoka Niigata 940-2188, Japan;3. Yoshimura Co., Ltd., 4-39 kukikita 2 chome, kuki-shi, Saitama 346-0007, Japan;4. Japan Fine Ceramics Center, 2-4-1 Mutsuno, Atsuta-ku, Nagoya 456-8587, Japan;1. Department of Innovative and Engineered Materials, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8502, Japan;2. Bioplastic Research Team, Biomass Engineering Program Cooperation Division, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan |
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| Abstract: | As a continuous effort of developing highly enantioselective epoxide hydrolase from marine microorganisms, it was found that Rhodobacterales bacterium HTCC2654 was highly enantioselective toward racemic glycidyl phenyl ether (GPE). An open reading frame (ORF) encoding a putative epoxide hydrolase (EHase) was cloned from the genome of R. bacterium HTCC2654, followed by expression and purification in Escherichia coli. The purified EHase (REH) hydrolyzed (S)-GPE preferentially over (R)-GPE. Enantiopure (R)-GPE from kinetic resolution of 29.2 mM racemic GPE using the purified REH could be obtained with enantiopurity of more than 99.9% enantiomeric excess (ee) and 38.4% yield (theoretical, 50%) within 20 min (enantiomeric ratio (E-value): 38.4). The enantioselective activity of REH toward GPE was also confirmed by the analysis of the vicinal diol, 3-phenoxy-1,2-propanediol. To our knowledge, this study demonstrates the highest enantioselective resolution of racemic GPE using a purified biocatalyst among the known native EHases. |
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