Simulation of Enzyme Catalysis in Calcium Alginate Beads
Author(s) -
Ameel Mohammed Rahman Al-Mayah
Publication year - 2012
Publication title -
enzyme research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.439
H-Index - 39
eISSN - 2090-0406
pISSN - 2090-0414
DOI - 10.1155/2012/459190
Subject(s) - calcium alginate , substrate (aquarium) , diffusion , chemistry , immobilized enzyme , residence time (fluid dynamics) , plug flow , starch , volumetric flow rate , hydrolysis , chemical engineering , reaction rate , chromatography , rate equation , particle size , catalysis , kinetics , thermodynamics , calcium , organic chemistry , enzyme , oceanography , physics , geotechnical engineering , quantum mechanics , engineering , geology
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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