Efficient continuous kinetic resolution of racemic 2-aminobutanol over immobilized penicillin G acylase |
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Authors: | Jianxin Wang Na Liu Xiaobo Cheng |
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Affiliation: | 1. School of Chemical Engineering and Technology, Tianjin University, Tianjin, People’s Republic of China;2. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin, People’s Republic of China |
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Abstract: | In this paper, an efficient method was established for continuous kinetic resolution of racemic 2-aminobutanol by selective hydrolysis of N-phenylacetyl (±)-2-aminobutanol over immobilized penicillin G acylase (PGA) in a fixed-bed reactor. Several N-acylated derivatives of 2-aminobutanol were screened in batch experiments, and it was found that the hydrolysis of N-phenylacetyl (±)-2-aminobutanol proceeded smoothly in the presence of immobilized penicillin G acylase with satisfied enantioselectivity. Thus, the reaction parameters were optimized in a fixed-bed reactor. Under the optimized conditions, 39.3% conversion of N-phenylacetyl (±)-2-aminobutanol and 98.2% ee value of S-2-aminobutanol were obtained. This fixed-bed system was operated continuously for 40 h without significant decrease of enzyme activity. It has been demonstrated to be more efficient compared to the batch experiments. |
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Keywords: | Acylase 2-aminobutanol continuous hydrolysis kinetic resolution penicillin G |
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