Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium |
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| Affiliation: | 1. College of Biotechnology and Pharmaceutical Engineering, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing University of Technology, Nanjing 210009, PR China;2. Zhejiang Jiuzhou Pharmaceutical Co. Ltd., 99 Waisha Road, Jiaojiang, Taizhou, Zhejiang 318000, PR China;1. Hubei Key Laboratory of Environmental and Health Effects of Persistent Toxic Substances, Jianghan University, Wuhan 430056, China;2. Institute of Environment and Health, Jianghan University, Wuhan, 430056, China;3. State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, 100085, China;4. Institute of Resources and Environment, Henan Polytechnic University, Jiaozuo, 454003, China;5. College of Resources and Environment, University of Chinese Academy of Sciences, Beijing, 100190, China |
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| Abstract: | Racemic DL-tert-leucine (DL-Tle) was resolved to obtain enantiopure L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative with immobilized penicillin G acylase (PGA). The effects of pH, reaction temperature, substrate concentration and reaction time on the reaction were investigated. The reaction was conveniently carried out at 0.4 M substrate concentration in water at pH 8.0 and 30 °C. Under the optimized reaction conditions, L-Tle was obtained in an enantiopure form (>99% ee) with 45.8% substrate conversion after 4 h. The thermal stability and operational stability of immobilized PGA were examined. Furthermore, the preparation of L-Tle was successfully performed in a recirculating packed bed reactor (RPBR) system and immobilized PGA exhibited a long-term stability for 51 days with a slight decrease of activity. The isolated D-enantiomer was racemized at 160 °C for 15 min and reused as substrate. The results obtained clearly demonstrated a potential for industrial application of immobilized PGA in the preparation of L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative. |
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| Keywords: | Immobilized penicillin G acylase Biocatalysis Bioprocess design Optimization Packed bed bioreactors |
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