| THE IMMOBILIZATION OF AMINOACYLASE AND THE RESOLUTION OF D,L-PHENYLALANINE |
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| 作者姓名： | 韩际宏 姜坪 何炳林 |
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| 作者单位： | Dept.of Biochem.，Graduare School of medical Sciences，Cornell University，New York，NY 10021，USA，Institute of Polymer Chemistry，Nankai University，Tianjin 300071，PRC，Institute of Polymer Chemistry，Nankai University，Tianjin 300071，PRC |
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| 摘 要： | A polymer with suitable physical characters and matched functional groups was synthesized,and used as a supporter to immobilize aminoacylase. The results showed that this supporterhad high immobilizing capacity and high selectivity for aminoacylase. Immobilized amino-acylase had high specific activity. In this paper, we determine the physical and chemicalcharacters of aminoacylase for resolution of D,L--phenylalanine, including its optimum tem-perature, pH, ion concentration, activated ion, substrate concentration, thermal stability anddenaturation. The immobilized aminoacylase was used to resolve the D,L-phenylalaninecontinuously. Thc resolved products was separated and purified with ion-exchange resins. L-phenylalanine solution was concentrated by vacuum evaporation and its hydrochloride wasformed. Checking of final product with polarimeter showed high yield and purity.
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THE IMMOBILIZATION OF AMINOACYLASE AND THE RESOLUTION OF D,L-PHENYLALANINE |
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| HAN JI-HONG,JIANG PING,HE BING-LIN Institute of Polymer Chemistry,Nankai University,Tianjin ,PRC.THE IMMOBILIZATION OF AMINOACYLASE AND THE RESOLUTION OF D,L-PHENYLALANINE[J].Science in China(Chemistry),1991(6). |
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| Authors: | HAN JI-HONG JIANG PING HE BING-LIN Institute of Polymer Chemistry Nankai University Tianjin PRC |
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| Institution: | HAN JI-HONG,JIANG PING,HE BING-LIN Institute of Polymer Chemistry,Nankai University,Tianjin 300071,PRC |
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| Abstract: | A polymer with suitable physical characters and matched functional groups was synthesized,and used as a supporter to immobilize aminoacylase. The results showed that this supporterhad high immobilizing capacity and high selectivity for aminoacylase. Immobilized amino-acylase had high specific activity. In this paper, we determine the physical and chemicalcharacters of aminoacylase for resolution of D,L--phenylalanine, including its optimum tem-perature, pH, ion concentration, activated ion, substrate concentration, thermal stability anddenaturation. The immobilized aminoacylase was used to resolve the D,L-phenylalaninecontinuously. Thc resolved products was separated and purified with ion-exchange resins. L-phenylalanine solution was concentrated by vacuum evaporation and its hydrochloride wasformed. Checking of final product with polarimeter showed high yield and purity. |
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| Keywords: | aminoacylase immobilization phenylalanine racemate resolution |
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