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Interaction of selected cosolvents with bovine alpha-lactalbumin.

Gunasekhar, P. M. and Prakash, V. (2008) Interaction of selected cosolvents with bovine alpha-lactalbumin. International Journal of Biological Macromolecules, 42 (4). pp. 348-55. ISSN 0141-8130

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Abstract

Alpha-lactalbumin constitutes about 3% of bovine milk proteins. The preferential solvent interactions between selected cosolvents (sorbitol, sucrose and glycerol) and alpha-lactalbumin at pH 7.5 was determined using precision densitimetry. The preferential interaction parameter (xi(3)) and other thermodynamic parameters were calculated at different solvent concentrations. The xi(3) parameter was maximum at 30%, 45% and 40% (w/v) concentrations with the values of -0.282g/g, -0.171g/g and -0.299g/g for sorbitol, sucrose and glycerol, respectively. Thus the principal driving energy in the system being preferential hydration and mutual exclusion of bulk solvent. There was only a marginal change in the CD spectra of the protein with these cosolvents indicating the integrity of secondary structures. The results of thermal denaturation measurements indicated an increase in thermal stability of alpha-lactalbumin with these cosolvents. In the presence of 30% sorbitol there was an increase in the apparent thermal transition temperature (apparent T(m)) from 65 to 71 degrees C. These results indicate that the selected cosolvents in this study stabilizes alpha-lactalbumin without altering the structure of the protein.

Item Type: Article
Uncontrolled Keywords: �-Lactalbumin; Densimetry; Protein stabilization; Sorbitol; Glycerol; Sucrose; Thermal transition temperature (apparent Tm)
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 24 May 2012 10:56
Last Modified: 24 May 2012 10:56
URI: http://ir.cftri.com/id/eprint/1805

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