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Enzyme ResearchVolume 2012 2012, Article ID 459190, 13 pages

Research ArticleBiochemical Engineering Department, Al-Kawarizimi College of Engineering, University of Baghdad, Baghdad, Iraq

Received 1 June 2012; Revised 23 July 2012; Accepted 31 July 2012

Academic Editor: Albert Jeltsch

Copyright © 2012 Ameel M. R. Al-Mayah. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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 . 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.

Autor: Ameel M. R. Al-Mayah



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