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Determination of enzyme global thermostability from equilibrium and kinetic analysis of heat inactivation

Apenten, Richard KO and Berthanon, N (1994) Determination of enzyme global thermostability from equilibrium and kinetic analysis of heat inactivation. Food Chemistry, 51 (1). p. 15. [Journal article]

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URL: http://dx.doi.org/10.1016/0308-8146(94)90041-8

DOI: doi:10.1016/0308-8146(94)90041-8

Abstract

An equilibrium-kinetic description for the two-stage irreversible thermoinactivation of enzymes (N D I) is examined by using chymotrypsin as a model. The parameter ΔG for enzyme unfolding (N D) and activation free energy for the D I reaction (ΔG#i) were summed to provide an index of enzyme global thermostability (ΔG#; ΔG# = ΔG + ΔG#i). There was good agreement between calculated and experimental global thermostability (i.e. enzyme stability with respect to reversible and irreversible thermoinactivation reaction steps) at 0–60°C. The results indicate that enzyme global thermostability may be markedly dependent on the rate of enzyme folding

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
ID Code:16898
Deposited By: Dr Richard Owusu-Apenten
Deposited On:01 Feb 2011 13:28
Last Modified:01 Feb 2011 13:28

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