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Thermal stability of beta-lactoglobulin in the presence of aqueous solution of alcohols and polyols |
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| Authors: | Romero Carmen M Lozano José M Sancho Javier Giraldo Gloria I |
| Institution: | aDepartamento de Química, Universidad Nacional de Colombia, Bogotá, Colombia bDepartamento de Farmacia, Universidad Nacional de Colombia, Bogotá, Colombia cDepartamento de Biología y Biología Celular y Molecular, Facultad de Ciencias Universidad de Zaragoza, Spain dDepartamento de Química, Universidad Nacional de Colombia, Manizales, Colombia |
| Abstract: | A systematic study concerning the effect of aqueous solution of alcohols and polyols with four carbon atoms on β-lactoglobulin stability is presented. The protein was chosen due to its functional properties and applications in food and pharmaceutical industries and because its structure and properties in aqueous solution have been widely described. The alcohols having a four carbon chain were selected to examine the effect of the gradual increase in the number of OH groups on protein stability. Protein thermal stability in water, buffers and dilute aqueous solutions of 1-butanol, 1,2-butanediol, 1,2,4-butanetriol and 1,2,3,4-butanetetrol was evaluated by fluorescence spectroscopy. The results were used to determine the temperature range in which the unfolding process is reversible and the protein denaturation temperature in acetate buffer pH 5.5 and in the aqueous mixed solvents. Thermodynamic results show that alcohol denaturating effect diminishes gradually as the number of OH groups increase. |
| Keywords: | β-Lactoglobulin Thermal denaturation Protein stability Alcohol Polyol |
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