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›› 2001, Vol. 1 ›› Issue (3): 0-0.

• 3 •    

固定化米曲霉氨基酰化酶反应动力学及其连续拆分DL–蛋氨酸实验

王淑豪, 李晓峰, 吴艳玲, 等   

  1. 天津大学化工学院制药工程系，天津 300072
  • 出版日期:2001-06-20 发布日期:2001-06-20

Enzymatic Kinetics of Immobilized L-aminoacylase and Its Continuous Resolution of DL-methionine

WANG Shu-hao, LI Xiao-feng, WU Yan-ling, SONG Zheng-xiao, MA Zhong-hai, YUAN Ying-jin   

  1. Dept. Pharm. Eng., School of Chem. Eng. & Technol., Tianjin Univ., Tianjin 300072, China
  • Online:2001-06-20 Published:2001-06-20

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摘要： 探讨了用明胶-戊二醛固定化米曲霉菌球氨基酰化酶反应动力学，对固定化菌体连续光学拆分DL-蛋氨酸进行了研究. 当底物浓度小于200 mmol/L时，没有底物抑制现象，此时拆分反应速率符合Michaelis-Menten方程. 在37℃时, 米氏常数和最大反应速率分别为11.9 mmol/L和1.3 mmol/L. 在连续拆分反应中反应物体积流量为7.5 ml/h，底物浓度为200和400 mmol/L时，L-蛋氨酸的转化率分别为93%和78%. 随体积流量的增加，L-蛋氨酸转化率降低. 固定化菌体的操作半衰期为82 d.

关键词: 固定化米曲霉, 氨基酰化酶, 动力学, 拆分, 蛋氨酸

Abstract: L-aminoacylase of Aspergillus oryzae pellets was immobilized by gelatin and glutaraldhyde. Kinetic constants of L-aminoacylase in immobilized pellets were determined and the optical resolution of DL-methionine by using immobilized Aspergillus oryzae pellets was investigated. When substrate concentration was less than 200 mmol/L, there was no substrate inhibition, and the reaction adhered to Michaelis-Menten equation. At 37°C, kinetic constants Km and Vm were 11.9 and 1.3 mmol/L respectively. L-methionine conversion at volumetric flow rate of 7.5 ml/h with substrate concentration of 200 and 400 mmmol/L was 93% and 78% respectively. L-methionine conversion decreased with increasing volumetric flow rate. Half-life of operation of immobilized L-aminoacylase was 82 d.

Key words: immobilized, Aspergillus oryzae, L-aminoacylase, kinetics, resolution, L-methionine

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