FANG Yue-qin, ZHU Long-bao, HUANG Nan, ZHOU Li, DING Zhong-yang, LIU Ying, ZHOU Zhe-min. Chiral resolution of D, L- phenylalanineusing immobilized phenylalanine ammonia- lyase for production of D- phenylalanine[J]. Science and Technology of Food Industry, 2015, (11): 243-246. DOI: 10.13386/j.issn1002-0306.2015.11.041
Citation: FANG Yue-qin, ZHU Long-bao, HUANG Nan, ZHOU Li, DING Zhong-yang, LIU Ying, ZHOU Zhe-min. Chiral resolution of D, L- phenylalanineusing immobilized phenylalanine ammonia- lyase for production of D- phenylalanine[J]. Science and Technology of Food Industry, 2015, (11): 243-246. DOI: 10.13386/j.issn1002-0306.2015.11.041

Chiral resolution of D, L- phenylalanineusing immobilized phenylalanine ammonia- lyase for production of D- phenylalanine

  • In order to establish a new method for the production of D- phenylalanine, the chiral resolution of D, L- phenylalanine using immobilized phenylalanine ammonia lyase ( PAL) was investigated. The mesoporous silica materials MCM-41 was used as support. Under the optical immobilization conditions, a maximum activity of PAL was 92% of the free enzyme.The reusability of immobilized enzyme retained 85% activity after 20 cycles.Using the immobilized PAL to catalyze resolution of D, L- phenylalanine, a 98% conversion ratio of L- phenylalanine was attained within 24 h, and the enantiomeric excess value of D- phenylalanine attained 96%. The immobilization enzyme ran continuously for 10 batches, the conversion ratio retained above 95%. Therefore, the immobilized PAL showed commercial application for the production of D- phenylalanine from chiral resolution of D, L- phenylalanine.
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