The conformational stability of a lipase from a psychrotrophic Pseudomonas fluorescens

A Makhzoum, Richard Owusu, JS Knapp

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Abstract

The reversible unfolding by heat or guanidine hydrochloride of lipase from a psychrotrophic Pseudomonas fluorescens was studied by fluorescence spectrophotometry. Lipase conformational stability was assessed based on thermodynamic parameters, e.g. free energy (ΔG), enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes for unfolding. The degree of reversibility was 70% and 100% for heat or guanidine hydrochloride unfolding. ΔG(25°C), ΔG(H2O), ΔHm, ΔSm and ΔCp values for lipase unfolding were 9.5, 6.5 and 151 kJ/mol, 475 J/mol/K and 4.06 kJ/mol/K respectively. The ΔG values determined by direct monitoring of unfolding were comparable to the value of 15 kJ/mol estimated from the enzyme temperature-activity profile. The conformational stability of lipase from the psychrotrophic Pseudomonas fluorescens is shown to be significantly lower than the stability usually observed for mesophilic enzymes.
LanguageEnglish
Pages355-359
JournalFood Chemistry
Volume46
Issue number4
Publication statusPublished - 1993

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Pseudomonas fluorescens
Lipase
Hot Temperature
heat
guanidines
Guanidine
Specific heat
fluorescence emission spectroscopy
Fluorescence Spectrometry
Spectrophotometry
Entropy
Enzymes
enthalpy
entropy
enzymes
Thermodynamics
thermodynamics
Free energy
Enthalpy
Fluorescence

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Makhzoum, A ; Owusu, Richard ; Knapp, JS. / The conformational stability of a lipase from a psychrotrophic Pseudomonas fluorescens. In: Food Chemistry. 1993 ; Vol. 46, No. 4. pp. 355-359.
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abstract = "The reversible unfolding by heat or guanidine hydrochloride of lipase from a psychrotrophic Pseudomonas fluorescens was studied by fluorescence spectrophotometry. Lipase conformational stability was assessed based on thermodynamic parameters, e.g. free energy (ΔG), enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes for unfolding. The degree of reversibility was 70{\%} and 100{\%} for heat or guanidine hydrochloride unfolding. ΔG(25°C), ΔG(H2O), ΔHm, ΔSm and ΔCp values for lipase unfolding were 9.5, 6.5 and 151 kJ/mol, 475 J/mol/K and 4.06 kJ/mol/K respectively. The ΔG values determined by direct monitoring of unfolding were comparable to the value of 15 kJ/mol estimated from the enzyme temperature-activity profile. The conformational stability of lipase from the psychrotrophic Pseudomonas fluorescens is shown to be significantly lower than the stability usually observed for mesophilic enzymes.",
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Makhzoum, A, Owusu, R & Knapp, JS 1993, 'The conformational stability of a lipase from a psychrotrophic Pseudomonas fluorescens', Food Chemistry, vol. 46, no. 4, pp. 355-359.

The conformational stability of a lipase from a psychrotrophic Pseudomonas fluorescens. / Makhzoum, A; Owusu, Richard; Knapp, JS.

In: Food Chemistry, Vol. 46, No. 4, 1993, p. 355-359.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The conformational stability of a lipase from a psychrotrophic Pseudomonas fluorescens

AU - Makhzoum, A

AU - Owusu, Richard

AU - Knapp, JS

PY - 1993

Y1 - 1993

N2 - The reversible unfolding by heat or guanidine hydrochloride of lipase from a psychrotrophic Pseudomonas fluorescens was studied by fluorescence spectrophotometry. Lipase conformational stability was assessed based on thermodynamic parameters, e.g. free energy (ΔG), enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes for unfolding. The degree of reversibility was 70% and 100% for heat or guanidine hydrochloride unfolding. ΔG(25°C), ΔG(H2O), ΔHm, ΔSm and ΔCp values for lipase unfolding were 9.5, 6.5 and 151 kJ/mol, 475 J/mol/K and 4.06 kJ/mol/K respectively. The ΔG values determined by direct monitoring of unfolding were comparable to the value of 15 kJ/mol estimated from the enzyme temperature-activity profile. The conformational stability of lipase from the psychrotrophic Pseudomonas fluorescens is shown to be significantly lower than the stability usually observed for mesophilic enzymes.

AB - The reversible unfolding by heat or guanidine hydrochloride of lipase from a psychrotrophic Pseudomonas fluorescens was studied by fluorescence spectrophotometry. Lipase conformational stability was assessed based on thermodynamic parameters, e.g. free energy (ΔG), enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes for unfolding. The degree of reversibility was 70% and 100% for heat or guanidine hydrochloride unfolding. ΔG(25°C), ΔG(H2O), ΔHm, ΔSm and ΔCp values for lipase unfolding were 9.5, 6.5 and 151 kJ/mol, 475 J/mol/K and 4.06 kJ/mol/K respectively. The ΔG values determined by direct monitoring of unfolding were comparable to the value of 15 kJ/mol estimated from the enzyme temperature-activity profile. The conformational stability of lipase from the psychrotrophic Pseudomonas fluorescens is shown to be significantly lower than the stability usually observed for mesophilic enzymes.

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VL - 46

SP - 355

EP - 359

JO - Food Chemistry

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