微型反应器
固定化酶
化学
生物催化
催化作用
化学工程
转氨作用
动力学
间歇式反应器
苯乙酮
色谱法
反应机理
酶
有机化学
物理
量子力学
工程类
作者
Nataša Miložič,Martin Lubej,Mitja Lakner,Polona Žnidaršič–Plazl,Igor Plazl
标识
DOI:10.1016/j.cej.2016.12.030
摘要
A mathematical model comprising transport phenomena and enzyme-catalyzed reaction performed on the inner walls of the continuously operated microreactor with surface-immobilized-transaminase was developed. Oriented enzyme immobilization enabling unhindered accessibility of enzyme active sites was obtained by using fusion protein N-SBM-ATA-wt consisting of selected ω-transaminase ATA-wt and the positively charged Zbasic2 tag, which established ionic interactions with silicon/glass microchannel surface. Enzyme-catalyzed transamination of (S)-(−)-α-methylbenzylamine and pyruvate to acetophenone and l-alanine was described by surface kinetics based on a ping-pong bi-bi mechanism. Reaction kinetic parameters were preliminarily defined in a batch system using various initial substrates concentrations and further applied in the surface reaction description. Based on the prevailing kinetic and convection/diffusion phenomena, the developed model could be reduced to the one-dimensional model which enabled immobilized enzyme concentration estimation and showed good agreement with experimental data from the outlet of the microreactor at various flow rates and inlet substrates concentrations. Moreover, the model successfully predicted performance of two consecutively connected microreactors coated with N-SBM-ATA-wt and could be further used to design and optimize efficient and sustainable processes of chiral amine syntheses catalyzed with surface immobilized enzymes.
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