Ulster University Logo

Ulster Institutional Repository

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

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

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]

Full text not available from this repository.

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

Repository Staff Only: item control page