催化学报

催化学报 ›› 2008, Vol. 29 ›› Issue (4): 403-408.

• 研究论文 • 上一篇    下一篇

华根霉菌丝体结合脂肪酶催化酯合成动力学拆分2-辛醇

单天宇1,王栋1,徐岩1,何军邀2   

  1. 1 江南大学生物工程学院工业生物技术教育部重点实验室, 江苏无锡 214122; 2 浙江工业大学药学院, 浙江杭州 310014
  • 收稿日期:2008-04-25 出版日期:2008-04-25 发布日期:2012-03-22

Kinetic Resolution of 2-Octanol by Esterification with Mycelium-Bound Lipase from Rhizopus chinensis

SHAN Tianyu1, WANG Dong1, XU Yan1*, HE Junyao2   

  1. 1 Key Laboratory of Industrial Biotechnology of the Ministry of Education, College of Bioengineering, Jiangnan University, Wuxi 214122, Jiangsu, China; 2 College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014, Zhejiang, China
  • Received:2008-04-25 Online:2008-04-25 Published:2012-03-22

PDF

956

被引次数

42

摘要： 研究了华根霉CCTCC M201021菌丝体结合脂肪酶(RCL)在非水相中催化酯合成动力学拆分外消旋2-辛醇的能力. 发现RCL对该反应具有较好的光学选择性(E>100),辛酸和异辛烷分别是最佳的酰基供体和反应溶剂,体系水活度的减少对反应的光学选择性没有明显影响,但能显著提高反应初速度. 在相同转化率下,通过添加3A分子筛降低体系水含量可使反应初始速度提高7.3倍. 当底物浓度提高到0.230 mol/L, 反应40 h时转化率达44.4%, 产物酯的ee值为94.7%. 与三种商品化脂肪酶进行了比较,发现在相同条件下RCL对2-辛醇的拆分不但具有较好的光学选择性(E=103.1), 而且也表现出较高的反应初速度和转化率.

关键词: 华根霉, 菌丝体结合脂肪酶, 选择性酯化, 动力学拆分, 2-辛醇

Abstract: The application of mycelium-bound lipase from Rhizopus chinensis CCTCC M201021 (RCL) to the kinetic resolution of 2-octanol by esterification in nonaqueous media was studied using octanoic acid and isooctane as the acyl donor and solvent, respectively. Water activity did not obviously affect the enantioselectivity of lipase but could notablely improve the initial velocity of the reaction. At the same conversion, the initial velocity of production of (R)-ester was increased by 7.3 times by the addition of3Amolecular sieves to reduce the water content of the system. When the substrate concentration was increased to 0.230 mol/L, (R)-ester was obtained with 44.4% conversion and 94.7% enantiomeric excess after reaction for40 h. Compared with three commercial lipases, RCL showed not only high enantioselectivity (E=103.1) but also more satisfied initial velocity and conversion.

Key words: Rhizopus chinensis, mycelium-bound lipase, enantioselective esterification, kinetic resolution, 2-octanol