海藻酸钙微球酶催化的模拟。

Q2 Biochemistry, Genetics and Molecular Biology Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-10-31 DOI:10.1155/2012/459190
Ameel M R Al-Mayah
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引用次数: 21

摘要

建立了固定床固定化酶反应器的通用数学模型,以模拟生物催化剂颗粒内部的扩散和反应过程。采用固定化α-淀粉酶对淀粉水解过程进行建模和模拟。玉米淀粉在恒定pH为5.5,温度为50℃的条件下水解。底物流速为0.2 ~ 5.0 mL/min,底物初始浓度为1 ~ 100 g/L。α-淀粉酶固定在平均直径2mm的海藻酸钙水凝胶珠上。在这项工作中考虑了Michaelis-Menten动力学。考虑了底物流速(即停留时间)和初始浓度对颗粒内扩散的影响。发现系统的性能受底物流速和初始浓度的影响。反应由反应速率控制。模型方程是基于稳态条件下的实验数据模拟的非线性二阶微分方程。利用MATLAB软件包中的有限元软件进行数值模拟。模拟结果对生物催化剂头内的底物和产物浓度曲线给出了满意的结果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Simulation of enzyme catalysis in calcium alginate beads.

A general mathematical model for a fixed bed immobilized enzyme reactor was developed to simulate the process of diffusion and reaction inside the biocatalyst particle. The modeling and simulation of starch hydrolysis using immobilized α-amylase were used as a model for this study. Corn starch hydrolysis was carried out at a constant pH of 5.5 and temperature of 50°C. The substrate flow rate was ranging from 0.2 to 5.0 mL/min, substrate initial concentrations 1 to 100 g/L. α-amylase was immobilized on to calcium alginate hydrogel beads of 2 mm average diameter. In this work Michaelis-Menten kinetics have been considered. The effect of substrate flow rate (i.e., residence time) and initial concentration on intraparticle diffusion have been taken into consideration. The performance of the system is found to be affected by the substrate flow rate and initial concentrations. The reaction is controlled by the reaction rate. The model equation was a nonlinear second order differential equation simulated based on the experimental data for steady state condition. The simulation was achieved numerically using FINITE ELEMENTS in MATLAB software package. The simulated results give satisfactory results for substrate and product concentration profiles within the biocatalyst bead.

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来源期刊
Enzyme Research
Enzyme Research Biochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
4.60
自引率
0.00%
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0
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