𝔖 Bobbio Scriptorium
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Immobilized enzyme catalysis with reaction-generated pH change

✍ Scribed by J. E. Bailey; Mary T. C. Chow

Book ID
102765650
Publisher
John Wiley and Sons
Year
1974
Tongue
English
Weight
541 KB
Volume
16
Category
Article
ISSN
0006-3592

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✦ Synopsis

Abstract

Many enzyme‐catalyzed reactions involve the liberation or consumption of hydrogen ions. In this paper a mathematical model is employed to investigate how such reactions behave when the enzyme is immobilized. Shifted pH optima, disappearance of an optimum pH, insensitivity to bulk pH, and very large effectiveness factors are some of the phenomena which appear as a result of pH coupling between the reaction and the enzyme's activity. Several of the qualitative features revealed by the model are consistent with earlier experimental observations. In addition, preliminary guidelines for optimal choice of enzyme support are suggested.

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Modelling the effects of electrostatic i
Modelling the effects of electrostatic interaction with reaction-generated pH change on the kinetics of immobilized enzymes
✍ K.B. Ramachandran; A.S. Rathore; S.K. Gupta πŸ“‚ Article πŸ“… 1995 πŸ› Elsevier Science 🌐 English βš– 577 KB

A mathematical model to describe the effects of electrostatic interaction with reaction-generated \(\mathrm{pH}\) change on the kinetics of immobilized enzyme has been developed to evaluate quantitatively the effect of partitioning of the hydrogen ion in and outside the carrier on overall reaction r