Do D D, Hossain M M
Department of Chemical Engineering, University of Queensland, St Lucia, Queensland 4067, Australia.
Biotechnol Bioeng. 1986 Apr;28(4):486-93. doi: 10.1002/bit.260280404.
This article presents a method for determining the rate constant for deactivation and the internal distribution of immobilized enzyme. This method makes use of the parallel deactivation process in a diffusion-controlled regime, in which the internal activity profile behaves like a penetration front. This front basically traces through the initial active enzymatic profile, and one can determine the internal profile and the rate constant for deactivation from the experimentally observable bulk concentration versus time. This method is applied to the experimental data of the system of hydrogen-peroxide-immobilized catalase on controlled pore glass and Si-Al particles.
本文提出了一种用于确定固定化酶失活速率常数及其内部分布的方法。该方法利用了扩散控制体系中的平行失活过程，在此过程中内部活性分布表现为穿透前沿。该前沿基本上追踪初始活性酶分布，并且可以从实验可观测的本体浓度随时间的变化来确定内部分布和失活速率常数。该方法应用于过氧化氢固定化过氧化氢酶在可控孔径玻璃和硅铝颗粒体系的实验数据。
