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

Richard KO Apenten; N Berthanon

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

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

Richard KO Apenten
, N Berthanon

Research output: Contribution to journal › Article › peer-review

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

Original language	English
Pages (from-to)	15
Journal	Food Chemistry
Volume	51
Issue number	1
DOIs	https://doi.org/10.1016/0308-8146(94)90041-8
Publication status	Published (in print/issue) - 1994

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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",

year = "1994",

doi = "10.1016/0308-8146(94)90041-8",

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journal = "Food Chemistry",

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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

JF - Food Chemistry

IS - 1

ER -

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

Abstract

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