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Study on Reaction Kinetics of Lipase-catalyzed Synthesis of Vanillyi Nonanoate in Acetone Media

机译:丙酮培养基中脂肪酶催化合成的反应动力学研究

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The reaction kinetics for synthesis of vaniilyi nonanoate (VN) by lipase-catalyzed transesterification of vaniilyi alcohol and methyl nonanoate in acetone was investigated in this study. The reaction catalyzed by lipase was carried out as follows: A reaction mixture containing given concentration of substrates (1ml) and lipase Novozyme 435 (20mg) in acetone (1ml) was shaken at 30 °C for 10min. The initial velocity of the reaction was calculated according to the concentration of VN detected by high performance liquid chromatography (HPLC), and the kinetic equation was obtained by analysis of the double reciprocal plot of initial velocity versus substrate concentration. The data calculated by the kinetic equation were basically in agreement with the experimental data with a correlation coefficient at 0.997. The inhibitory action of methanol (by-product) in the reaction was also investigated and the results indicated that the concentration of methanol influences both slope and intercept of y-axis of the double reciprocal curve, and the lines intersect on the X-axis. These results revealed that this transesterification follows the Ping-Pong reaction mechanism.
机译:用于通过vaniilyi醇和丙酮壬酸甲酯的脂肪酶催化的酯交换合成vaniilyi壬酸酯(VN)的反应动力学在本研究中进行了研究。通过脂肪酶催化的反应是如下进行:含有底物(1ml)中,脂肪酶的Novozyme 435(20毫克)在丙酮(1ml)中,在30℃振摇10分钟的给定浓度的反应混合物。反应的初始速度是根据VN的浓度计算由高效液相色谱(HPLC)检测,并且是由初始速度与底物浓度的双倒数作图的分析而获得的动力学方程。在与在0.997的相关系数的实验数据协议由动力学方程计算的数据基本上是。甲醇(副产物)的反应中的抑制作用也进行了研究,结果表明,甲醇影响斜率和双倒数曲线的y轴截距,并相交于X轴的线的浓度。这些结果表明,该酯交换反应遵循乒乓反应机制。

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