Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6

D Galani, Richard KO Apenten

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Thermodynamic parameters for thermal denaturation of -lactoglobulin (-lg) should account for the dissociation coupled unfolding (DCU) transitions, Dimer&unknown;Monomer&unknown;Unfolded state. Purified -Blg (0.4-4mgml-1 in 50mM glycine-glycine-HCl buffer, pH 2.6) was heated and monitored by UV-difference spectrophotometry. The Monomer&unknown;Unfolded state transition occurred at 65-95oC with Tm equal to 82oC and a Gibbs free energy change (GU0) of 51kJmol-1. Such results were combined with parameters for -Blg dissociation leading to the Gibbs free energy change for DCU (DCU0) of 128 (+/-8.3)kJmol-1. The enthalpy and entropy change for DCU was (HDCU0) equal to 373kJmol-1 and (HDCU0) 824Jmol-1K-1. Thus, the room temperature stability of -Blg is 76kJmol-1 higher than reported previously. The possible significance of such results for protein stability function relations (PSFR) is discussed
LanguageEnglish
Pages137-142
JournalThermochimica Acta
Volume1
Issue number363
DOIs
Publication statusPublished - 1 Nov 2000

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Lactoglobulins
Denaturation
biopolymer denaturation
thermodynamic equilibrium
Thermodynamics
dissociation
Gibbs free energy
glycine
Glycine
Amino acids
monomers
Monomers
Spectrophotometry
spectrophotometry
Dimers
Enthalpy
Buffers
Entropy
buffers
enthalpy

Cite this

Galani, D ; Apenten, Richard KO. / Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6. In: Thermochimica Acta. 2000 ; Vol. 1, No. 363. pp. 137-142.
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Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6. / Galani, D; Apenten, Richard KO.

In: Thermochimica Acta, Vol. 1, No. 363, 01.11.2000, p. 137-142.

Research output: Contribution to journalArticle

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AU - Galani, D

AU - Apenten, Richard KO

PY - 2000/11/1

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AB - Thermodynamic parameters for thermal denaturation of -lactoglobulin (-lg) should account for the dissociation coupled unfolding (DCU) transitions, Dimer&unknown;Monomer&unknown;Unfolded state. Purified -Blg (0.4-4mgml-1 in 50mM glycine-glycine-HCl buffer, pH 2.6) was heated and monitored by UV-difference spectrophotometry. The Monomer&unknown;Unfolded state transition occurred at 65-95oC with Tm equal to 82oC and a Gibbs free energy change (GU0) of 51kJmol-1. Such results were combined with parameters for -Blg dissociation leading to the Gibbs free energy change for DCU (DCU0) of 128 (+/-8.3)kJmol-1. The enthalpy and entropy change for DCU was (HDCU0) equal to 373kJmol-1 and (HDCU0) 824Jmol-1K-1. Thus, the room temperature stability of -Blg is 76kJmol-1 higher than reported previously. The possible significance of such results for protein stability function relations (PSFR) is discussed

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