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SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β‐GALACTOSIDASE ADSORBED TO A PHENOL‐FORMALDEHYDE RESIN
Author(s) -
GRULKE ERIC A.,
OKOS MARTIN R.,
SYVERSON ALDRICH
Publication year - 1977
Publication title -
journal of food process engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 45
eISSN - 1745-4530
pISSN - 0145-8876
DOI - 10.1111/j.1745-4530.1977.tb00191.x
Subject(s) - thermal diffusivity , chemistry , mass transfer , particle (ecology) , adsorption , kinetic energy , immobilized enzyme , formaldehyde , chromatography , substrate (aquarium) , hydrolysis , catalysis , phenol , mass transfer coefficient , lactose , particle size , chemical engineering , thermodynamics , enzyme , organic chemistry , oceanography , physics , quantum mechanics , engineering , geology
The mass transfer and kinetic properties of both soluble and immobilized β‐galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading.