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首页> 外文期刊>Food and Bioproducts Processing. Transactions of the Institution of Chemical Engineers, Part C >Determination of immobilized enzyme apparent kinetic parameters in packed-bed reactors: Presentation of a new methodolog
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Determination of immobilized enzyme apparent kinetic parameters in packed-bed reactors: Presentation of a new methodolog

机译:固定床反应器中固定化酶表观动力学参数的确定:一种新方法的介绍

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摘要

A new explicit equation is proposed for the determination of immobilized enzyme apparent Michaelis-Menten kinetic parameters in packed-bed reactors. The mathematical analysis is based on recycling systems. The present methodology is easily applicable for a wide range of operating conditions. It is free from the probable limitations of the single-pass apparent immobilized enzyme kinetic parameter estimation technique that requires simultaneous measurement of column substrate inlet and effluent concentrations at a specified time. The experimental system is composed of a substrate reservoir and a circulating flow packed-bed immobilized enzyme reactor. The experimental data is gathered for glucose decomposition reaction in a recirculation system with immobilized glucose oxidase on a weak base ion exchanger resin. The apparent kinetic parameter, K theta sub(m) values were calculated with a new explicit equation, proposed in this work, and they are found to be 0.48 x 10 super(-3) and 0.60 x 10 super(-3) mmol cm super(-3) for the recirculation rates of 75 and 25 cm super(3) min super(-1), respectively.
机译:提出了一个新的显式方程式,用于确定填充床反应器中固定化酶的表观Michaelis-Menten动力学参数。数学分析基于回收系统。本方法论可容易地适用于广泛的操作条件。它没有单次通过表观固定化酶动力学参数估计技术的可能限制,该技术要求在指定时间同时测量色谱柱底物入口和流出物浓度。实验系统由底物池和循环流化床固定化酶反应器组成。收集了在弱碱离子交换树脂上固定葡萄糖氧化酶的再循环系统中葡萄糖分解反应的实验数据。用这项工作中提出的新的显式方程计算了表观动力学参数K theta sub(m)值,发现它们是0.48 x 10 super(-3)和0.60 x 10 super(-3)mmol cm super(-3)分别为75和25 cm super(3)min super(-1)的再循环率。

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