The effect of slow intraparticle diffusion on observed immmobilized enzyme stability

✍ Scribed by Gene K. Leet; Peter J. Reilly

• Publisher: Elsevier Science
• Year: 1981
• Tongue: English
• Weight: 633 KB
• Volume: 36
• Category: Article
• ISSN: 0009-2509
• DOI: 10.1016/0009-2509(81)80036-x

✦ Synopsis

The isothermal deactivation of immobilized enzymes was studied for cases where the main reaction followed Michaelis-Menten kinetics and rates of deactivation reactions were first order in enzyme activity.

Observed enzyme activities and deactivation rates were predicted by orthogonal collocation when intraparticle diffusion was limiting and presence of reactant could either increase or decrease the deactivation rate. Use of the Bischoff-Aris general modulus allowed the analytical proof that apparent coefficients for immobilized enzymes following Michaelis-Menten kinetics, under strong intraparticle diffusion control, whose deactivation was unaffected by reactant concentration, were exactly half those of enzymes not under diffusion limitation.