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

D Galani; Richard KO Apenten

doi:10.1016/S0040-6031(00)00606-7

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

D Galani, Richard KO Apenten

Faculty Of Life & Health Sciences

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

20 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

Original language	English
Pages (from-to)	137-142
Journal	Thermochimica Acta
Volume	1
Issue number	363
DOIs	https://doi.org/10.1016/S0040-6031(00)00606-7
Publication status	Published (in print/issue) - 1 Nov 2000

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http://www.ingentaconnect.com/content/els/00406031/2000/00000363/00000001/art00606

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title = "Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6",

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",

author = "D Galani and Apenten, {Richard KO}",

year = "2000",

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doi = "10.1016/S0040-6031(00)00606-7",

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journal = "Thermochimica Acta",

publisher = "Elsevier",

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TY - JOUR

T1 - Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6

AU - Galani, D

AU - Apenten, Richard KO

PY - 2000/11/1

Y1 - 2000/11/1

N2 - 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

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

U2 - 10.1016/S0040-6031(00)00606-7

DO - 10.1016/S0040-6031(00)00606-7

M3 - Article

VL - 1

SP - 137

EP - 142

JO - Thermochimica Acta

JF - Thermochimica Acta

IS - 363

ER -

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

Abstract

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