RESUMO
En este trabajo se presenta un estudio sistemático sobre el efecto del incremento en el número de grupos OH de alcoholes y polioles de cuatro carbonos sobre las propiedades conformacionales de la β-lactoglobulina. Los cambios en el comportamiento de las soluciones acuosas de la proteína por la adición de 1-butanol, 1,2-butanodiol, 1,2,4-butano-triol y 1,2,3,4-butanotetrol fueron determinados por espectroscopia UV, de fluorescencia y DC en el UV lejano, y en el UV cercano a 298,15 K. Los resultados muestran que el butanol ejerce una mayor modificación en la estructura de la proteína y el efecto va disminuyendo a medida que se incrementa el número de grupos OH.
In this work we present a systematic study of the effect of the increase of OH groups in alcohols and polyols of four carbon atoms on the conformational properties of β-lactoglobulin. The changes in the behavior of the aqueous solution of the protein by the addition of 1-butanol, 1,2-butanediol, 1,2,4-butanetriol y 1,2,3,4-butano-tetrol were determined by UV, far and near UV CD spectra and fluorescence spectroscopy at 298.15K. The results show that the largest modification ofprotein structure is due to butanol and the effect decreases as the number of OH groups increase.
Neste trabalho apresenta-se um estudo sistemático sob o efeito do acréscimo do número de grupos OH de alcoóis e polióis de quatro carbonos nas propriedades conformacionais da β-lactoglobulina. As mudanças no comportamento das soluções aquosas da proteína, pela adição de 1-butanol, 1,2 butanodiol, 1,2,4 e 1,2,3,4 butanotetrol butanotriol, foram determinados por espectroscopia UV, fluorescência e DC no UV distante, e no UV próximo a 298,15 K. Os resultados mostraram que o butanol tem uma maior influencia na estrutura da proteína, e o seu efeito diminui com o aumento do número de grupos OH.
RESUMO
A systematic study concerning the effect of aqueous solution of alcohols and polyols with four carbon atoms on beta-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.