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

Richard KO Apenten, N Berthanon

Research output: Contribution to journalArticle

12 Citations (Scopus)

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
LanguageEnglish
Pages15
JournalFood Chemistry
Volume51
Issue number1
DOIs
Publication statusPublished - 1994

Fingerprint

heat inactivation
thermal stability
Hot Temperature
kinetics
Kinetics
Enzymes
enzymes
4 alpha-glucanotransferase
enzyme stability
protein folding
chymotrypsin
Enzyme Stability
Chymotrypsin
energy
Free energy
Chemical activation

Cite this

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title = "Determination of enzyme global thermostability from equilibrium and kinetic analysis of heat inactivation",
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",
author = "Apenten, {Richard KO} and N Berthanon",
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Determination of enzyme global thermostability from equilibrium and kinetic analysis of heat inactivation. / Apenten, Richard KO; Berthanon, N.

In: Food Chemistry, Vol. 51, No. 1, 1994, p. 15.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Determination of enzyme global thermostability from equilibrium and kinetic analysis of heat inactivation

AU - Apenten, Richard KO

AU - Berthanon, N

PY - 1994

Y1 - 1994

N2 - 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

AB - 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

U2 - 10.1016/0308-8146(94)90041-8

DO - 10.1016/0308-8146(94)90041-8

M3 - Article

VL - 51

SP - 15

JO - Food Chemistry

T2 - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

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