Characterising the secondary structure changes occurring in high density systems of BLG dissolved in aqueous pH 3 buffer
Characterising the secondary structure changes occurring in high density systems of BLG dissolved in aqueous pH 3 buffer
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DOI：
10.1016/j.foodhyd.2014.12.027
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发表时间：
2015-04-01
影响因子：
10.7
通讯作者：
Tromp, R. H.
中科院分区：
文献类型：
--
作者：
Ioannou, J. C.;Donald, A. M.;Tromp, R. H.
这项研究着眼于降低水合水平的影响，作为水合蛋白二级结构转变的驱动力。采用简单的蛋白质-水体系，研究了在固定pH值、盐含量和温度条件下典型的富含蛋白质的乳制品体系的条件。从牛乳中提取的冻干β -乳球蛋白（A型）直接溶解在两种不同的缓冲体系中，浓度范围在1mg /ml（类似于54 μ M）和200mg /ml（类似于0.01 M）之间，但在固定的pH水平（pH 3）下。利用圆二色性（CD）、衰减全反射傅立叶变换红外光谱（ATR FTIR）和硫黄素T （ThT）荧光光谱法测量了在20℃下蛋白质溶液浓度对二级结构的影响。所有这些技术的结果表明，大多数二级结构的变化发生在低蛋白质浓度范围内。
This study looks at the influence of reduced levels of hydration as a driving force for transitions in the secondary structure of hydrated proteins. A simple protein-water system was used to study the conditions of typical protein-rich dairy food systems at a fixed pH level, salt content, and temperature. Freeze-dried beta-lactoglobulin (Type A) from bovine milk was dissolved directly into two different buffer systems over a wide range of concentrations between 1 mg/ml (similar to 54 mu M) and 200 mg/ml (similar to 0.01 M) but at a fixed pH level, pH 3. Circular dichroism (CD), attenuated total reflectance Fourier transform infrared spectroscopy (ATR FTIR), and thioflavin T (ThT) Assay fluorescence spectroscopy were used to measure changes in the secondary structure with respect to protein solution concentration at 20 degrees C. The findings of all of the techniques indicate that the majority of the secondary structure changes occur within the low protein concentration regime (i.e.