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Influence of Alcohols and Polyols on the Behavior of Aqueous Solutions of β-Lactoglobulin at pH 5.5

机译:醇和多元醇对β-乳球蛋白在pH 5.5下水溶液行为的影响

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The above is a very brief survey of what we have found studying the thermody-namic behavior of β-lactoglobulin in the attempt to comprehend protein stability. The denaturing effect induced by alcohols and polyols depends clearly on the number of OH groups, as well on concentration. The behavior of thermal denatur-ation of aqueous solutions of β-lactoglobulin in alcohols and polyols of four carbon atoms shows that 1-butanol produces the largest decrease in T_m as alcohol concentration increases. The effect diminishes as the number of hydroxyl groups increase and for 1,2,3,4-butanetetrol, which is a typical hydrophilic solute, an increase in temperature is observed as concentration increases. In the case of butanediols, the decrease in T_m is greater for 1,2-butanediol, which has a larger hydrophobic domain due to the vicinal position of the OH groups, and with 1,2,4-butanetriol a negligible effect is observed. The number and position of OH groups is also clearly reflected on the surface and viscometric behavior of β-lactoglobulin in aqueous solution. The decrease of surface tension with alcohol mole fraction becomes less pronounced as the number of OH groups increases, while for 1,2,3,4-butanetetrol the behavior changes and the solution surface tension becomes larger than the corresponding value for water. The largest increase in activation energy is due to butanol, and diminishes as the number of OH groups increase. Experimental results reveal that thermal stability, surface tension and viscometric properties of aqueous solutions of β-lactoglobulin are clearly influenced by the presence of alcohols and polyols. The observed behavior follows a similar trend to that observed for the properties of these alcohols in water, suggesting that their effect on β-lactoglobulin stability is a consequence of the alcohol-water interaction and the induced modification in solvent structure, rather than alcohol-protein interactions.
机译:上面是对我们发现的研究β-乳球蛋白热动力学行为以试图理解蛋白质稳定性的非常简短的综述。由醇和多元醇引起的变性作用显然取决于OH基的数目以及浓度。 β-乳球蛋白水溶液在醇和具有四个碳原子的多元醇中的热变性行为表明,随着醇浓度的增加,1-丁醇的T_m降低最大。随着羟基数的增加,该作用减弱,而对于典型的亲水性溶质即1,2,3,4-丁丁醇,随着浓度的增加,温度也会升高。在丁二醇的情况下,对于1,2-丁二醇,T_m的降低更大,由于OH基团的邻位,其具有较大的疏水域,并且对于1,2,4-丁三醇观察到的影响可忽略不计。羟基的数量和位置也清楚地反映在水溶液中β-乳球蛋白的表面和粘度行为上。随着OH基团数的增加,表面张力随醇摩尔分数的降低变得不那么明显,而对于1,2,3,4-丁丁醇的行为发生变化,溶液表面张力变得大于水的相应值。活化能的最大增加是由于丁醇,并且随着OH基数的增加而减少。实验结果表明,β-乳球蛋白水溶液的热稳定性,表面张力和粘度性质明显受到醇和多元醇的存在的影响。观察到的行为遵循与观察到的这些醇在水中的性质相似的趋势,表明它们对β-乳球蛋白稳定性的影响是醇-水相互作用和诱导的溶剂结构修饰的结果,而不是醇-蛋白质互动。

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