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无溶剂固定化脂肪酶催化酯交换合成苯甲酸丙酯:优化与动力学建模。

Synthesis of propyl benzoate by solvent-free immobilized lipase-catalyzed transesterification: Optimization and kinetic modeling.

机构信息

Department of Chemistry, Institute of Chemical Technology, Mumbai, 400019, India.

出版信息

Bioprocess Biosyst Eng. 2021 Feb;44(2):369-378. doi: 10.1007/s00449-020-02448-9. Epub 2020 Sep 30.

DOI:10.1007/s00449-020-02448-9
PMID:32997184
Abstract

The present study aimed to analyze reaction kinetics and mechanism for the synthesis of propyl benzoate in solvent-free conditions. Lipase was immobilized on Hydroxypropyl methylcellulose (HPMC) and polyvinyl alcohol (PVA) polymer blend by entrapment method. Among different lipases immobilized on a support, Candida cylindracea (CCL) showed excellent activity. Systematic studies were done to optimize the reaction conditions. The activation energy was found to be 16.2 kcal/mol for immobilized CCL. Kinetic parameters were calculated, which depicted that propyl benzoate synthesized using immobilized CCL followed the ternary complex model in which propanol inhibits lipase activity at higher concentrations. Recyclability of the catalyst was checked up to four catalytic cycles and 40% retention of activity was observed up to the fourth cycle. Finally, the applicability of developed protocol to synthesize various alkyl benzoates was explored.

摘要

本研究旨在分析无溶剂条件下合成苯甲酸丙酯的反应动力学和机理。通过包埋法将脂肪酶固定在羟丙基甲基纤维素(HPMC)和聚乙烯醇(PVA)聚合物共混物上。在固定在载体上的不同脂肪酶中,圆酵母(CCL)表现出优异的活性。进行了系统的研究以优化反应条件。发现固定化 CCL 的活化能为 16.2 kcal/mol。计算了动力学参数,表明使用固定化 CCL 合成的丙酸丙酯遵循三元复合物模型,其中在较高浓度下丙醇抑制脂肪酶活性。催化剂的可回收性检查了多达四个催化循环,在第四个循环中观察到 40%的活性保持。最后,探索了所开发的方案在合成各种烷基苯甲酸酯中的适用性。

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