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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Effects of pH on the Molecular Binding between /Mactoglobulin and Bixin
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Effects of pH on the Molecular Binding between /Mactoglobulin and Bixin

机译:pH值对/巨球蛋白与Bixin分子结合的影响

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摘要

Binding between β-lactoglobulin (β-Lg), the major whey protein, and bixin, the major carotenoid in annatto, was studied at pH 3.0—10.0. The Fourier transform infrared spectroscopy and UV—vis absorption spectroscopy results showed that the binding involved a complex formation. The tryptophan quenching fluorescence and analytical ultracentrifugation data showed that there were two specific binding sites and that the binding affinity increased significantly with an increase in pH. A higher efficiency of energy transfer from tryptophan fluorescence to bixin was observed at higher pH. Thermodynamic parameters and the number of specific binding sites obtained from isothermal titration calorimetry and analytical ultracentrifugation suggested that binding involved mostly hydrophobic interactions for the two specific binding sites. The impacts of pH on binding were correlated to the conformation of β-Lg, the hydrophobic pocket of which becomes more available at higher pH and ionic strength.
机译:在pH 3.0-10.0的条件下,研究了主要乳清蛋白β-乳球蛋白(β-Lg)与安乃肽中主要类胡萝卜素联蛋白之间的结合。傅里叶变换红外光谱和紫外可见吸收光谱结果表明,结合涉及复合物的形成。色氨酸猝灭荧光和分析超速离心数据表明,存在两个特定的结合位点,并且结合亲和力随pH的增加而显着增加。在较高的pH值下,从色氨酸荧光到联苯胺的能量转移效率更高。从等温滴定热法和分析超速离心获得的热力学参数和特异性结合位点的数量表明,结合主要涉及两个特异性结合位点的疏水相互作用。 pH对结合的影响与β-Lg的构象相关,β-Lg的疏水口袋在更高的pH和离子强度下变得更容易利用。

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