石油炼制与化工 ›› 2020, Vol. 51 ›› Issue (5): 31-36.

• 催化剂 • 上一篇    下一篇

聚合物涂覆的酶催化酯交换反应研究

段宝轩1,2,李诗浩3,王洪海1,2,李春利1,2,卢一凡1,2   

  1. 1.河北工业大学化工学院
    2.河北工业大学化工过程集成与资源利用节能国家地方联合工程实验室
    3.天津大学化工学院生化工程系和系统生物工程重点实验室(教育部)
  • 收稿日期:2019-11-11 修回日期:2019-12-07 出版日期:2020-05-12 发布日期:2020-05-28
  • 通讯作者: 王洪海 E-mail:ctstwhh@hebut.edu.cn
  • 基金资助:
    河北省自然科学基金;国家自然科学基金资助项目;天津市企业科技特派员项目

STUDY ON TRANSESTERIFICATION CATALYZED BY POLYMER COATED ENZYME

    

  1.  
  • Received:2019-11-11 Revised:2019-12-07 Online:2020-05-12 Published:2020-05-28
  • Supported by:
     

摘要: 针对酶促反应精馏技术中酶制催化剂的稳定性与成本问题,将南极假丝酵母脂肪酶B(CALB)通过疏水相互作用固定于大孔吸附树脂NKA中,通过聚乙二醇化修饰制备固定化脂肪酶NKA-CALB-PEG,与商业固定化脂肪酶Novozyme435相比,在稳定性和成本上显著改善。通过NKA-CALB-PEG催化乙酸乙酯-正丁醇酯交换反应动力学试验确定最优的反应条件为:搅拌速率300 r/min、催化剂用量10%、乙酸乙酯/正丁醇摩尔比1∶1、温度65 ℃。在333.15~348.15 K下,将试验数据拟合得到反应动力学方程,比较试验值与计算值,结果表明此宏观动力学方程具备合理性。

关键词: 固定化脂肪酶, 聚乙二醇化, 酯交换, 动力学方程

Abstract: Aiming at the stability and cost of enzyme catalyst in enzymatic reactive distillation technology, Candida antarctica Lipase B (CALB) was immobilized on the macroporous adsorption resin NKA by hydrophobic interaction, and the immobilized lipase NKA-CALB-PEG was prepared by PEGylation. Compared with the commercial immobilized lipase Novozyme435, the stability and cost of NKA-CALB-PEG were significantly improved. The optimal reaction conditions for NKA-CALB-PEG catalytic transesterification of EtAC and BuOH were as follows: the stirring speed was 300 r/min, the amount of catalyst was 10%, the molar ratio of BuOH/EtAC was 1∶1, the temperature was 65 ℃. At 333.15-348.15 K, the experimental data were fitted to obtain the kinetic equation of the reaction. Comparing the experimental values with the calculated results showed that the macro kinetic equation was reasonable.

Key words: immobilized lipase, PEGylation, transesterification, kinetic equation

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