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

Galani, D and Apenten, Richard KO (2000) Revised equilibrium thermodynamic parameters for thermal denaturation of -lactoglobulin at pH 2.6. Thermochimica Acta, 1 (363). pp. 137-142. [Journal article]

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

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


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

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Nutrition Innovation Centre for Food and Health (NICHE)
ID Code:15772
Deposited By: Dr Richard Owusu-Apenten
Deposited On:27 Sep 2010 13:01
Last Modified:27 Sep 2010 13:01

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