Probing the binding between norbixin and dairy proteins by spectroscopy methods.
Probing the binding between norbixin and dairy proteins by spectroscopy methods.
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DOI：
10.1016/j.foodchem.2013.01.073
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发表时间：
2013-08
期刊：
影响因子：
8.8
通讯作者：
Yue Zhang;Q. Zhong
中科院分区：
文献类型：
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作者：
Yue Zhang;Q. Zhong
几个世纪以来，红色素(去甲氧胆碱)一直被用来给奶酪着色，但人们对这种色素和乳制品蛋白质之间的相互作用知之甚少。用荧光光谱、傅里叶变换红外光谱(FTIR)、圆二色谱(CD)和差示扫描量热法(DSC)研究了去甲比星与乳清分离蛋白(WPI)、酪氨酸钠(NaCN)和6种乳蛋白的结合作用。观察到去甲肾上腺素通过形成络合物有效地猝灭WPI和NaCN的荧光。NaCN与去甲氧胆碱的结合亲和力高于WPI-去甲胆碱。对于单独的蛋白质，牛血清白蛋白与去甲氧胆碱的结合亲和力高于β-乳球蛋白和α-乳蛋白，而κ-酪蛋白与去甲胆碱的结合效果好于α-和β-酪蛋白。结合改变了WPI和NaCN的构象，但不同蛋白质的结合程度和趋势有所不同。
Annatto (norbixin) has been used to color cheeses for centuries, but there is very little knowledge about interactions between the pigment and dairy proteins. In this study, binding of norbixin with whey protein isolate (WPI), sodium caseinate (NaCN), and 6 individual dairy proteins was investigated by using fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) and differential scanning calorimetry (DSC). Norbixin was observed to effectively quench the fluorescence of WPI and NaCN by forming complexes. The binding affinity between NaCN and norbixin was higher than that of WPI-norbixin. For individual proteins, bovine serum albumin had higher binding affinity with norbixin than β-lactoglobulin and α-lactalbumin, while κ-casein bound with norbixin better than α- and β-caseins. Binding changed the conformation of WPI and NaCN, but the extent and trend varied for individual proteins.