The thermodynamic stability of lipases and proteases from psychrotrophic bacteria

RK Owusu, A MAKHZOUM, J KNAPP

Research output: Contribution to journalArticle

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Abstract

The thermodynamic or conformational stability of psychrotroph lipases and proteases, measured as the Gibbs free energy difference (ΔG) between the native and denatured enzymes, were estimated from enzyme temperature-activity profile data. ΔG estimates of 8–10 kJ/mol and 16–17 kJ/mol were obtained for psychrotroph-derived lipases and proteases, respectively. Pseudomonas fluorescens strain AR-11 protease was unusually thermolabile (ΔG = 3·0–7·6 kJ/mol). These values were compared with values for some mesophilic and thermophilic enzymes and the possible relationship of ΔG to psychrotrophic enzyme heat-resistance is discussed.
LanguageEnglish
Pages187
JournalFood Chemistry
Volume39
Issue number2
DOIs
Publication statusPublished - 1991

Fingerprint

psychrotrophic bacteria
Lipase
Thermodynamics
thermodynamics
Bacteria
Thermodynamic stability
Peptide Hydrolases
proteinases
Enzymes
enzymes
Gibbs free energy
Pseudomonas fluorescens
heat tolerance
Heat resistance
Hot Temperature
Temperature
temperature

Cite this

Owusu, RK ; MAKHZOUM, A ; KNAPP, J. / The thermodynamic stability of lipases and proteases from psychrotrophic bacteria. In: Food Chemistry. 1991 ; Vol. 39, No. 2. pp. 187.
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The thermodynamic stability of lipases and proteases from psychrotrophic bacteria. / Owusu, RK; MAKHZOUM, A; KNAPP, J.

In: Food Chemistry, Vol. 39, No. 2, 1991, p. 187.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The thermodynamic stability of lipases and proteases from psychrotrophic bacteria

AU - Owusu, RK

AU - MAKHZOUM, A

AU - KNAPP, J

PY - 1991

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N2 - The thermodynamic or conformational stability of psychrotroph lipases and proteases, measured as the Gibbs free energy difference (ΔG) between the native and denatured enzymes, were estimated from enzyme temperature-activity profile data. ΔG estimates of 8–10 kJ/mol and 16–17 kJ/mol were obtained for psychrotroph-derived lipases and proteases, respectively. Pseudomonas fluorescens strain AR-11 protease was unusually thermolabile (ΔG = 3·0–7·6 kJ/mol). These values were compared with values for some mesophilic and thermophilic enzymes and the possible relationship of ΔG to psychrotrophic enzyme heat-resistance is discussed.

AB - The thermodynamic or conformational stability of psychrotroph lipases and proteases, measured as the Gibbs free energy difference (ΔG) between the native and denatured enzymes, were estimated from enzyme temperature-activity profile data. ΔG estimates of 8–10 kJ/mol and 16–17 kJ/mol were obtained for psychrotroph-derived lipases and proteases, respectively. Pseudomonas fluorescens strain AR-11 protease was unusually thermolabile (ΔG = 3·0–7·6 kJ/mol). These values were compared with values for some mesophilic and thermophilic enzymes and the possible relationship of ΔG to psychrotrophic enzyme heat-resistance is discussed.

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SP - 187

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JF - Food Chemistry

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