Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
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DOI：
10.1021/jf00040a002
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发表时间：
1994-04
影响因子：
6.1
通讯作者：
Haiming Zhu;S. Damodaran
中科院分区：
文献类型：
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作者：
Haiming Zhu;S. Damodaran
研究了热诱导对乳清分离蛋白(WPI)理化性质的影响。在70℃加热的WPI(5%)在1分钟内发生快速构象变化。非周期结构含量的增加主要是以牺牲β片状结构为代价的。通过pH-溶解度曲线和在pH为4.6的NaC l溶液中溶解度曲线的变化来衡量蛋白质表面的疏水性增加。然而，用顺式对羟基苯甲酸结合法测定的表面疏水性降低了。相反，WPI(9%)在90℃加热时，二级结构含量没有明显变化
Heat-induced changes in the physicochemical properties of whey protein isolate (WPI) have been studied. WPI (5%) heated at 70 o C underwent rapid conformational changes within 1 min. The aperiodic structure content increased primarily at the cost of β-sheet structure. The hydrophobic character, as measured by changes in the pH-solubility profile and the solubility profile at pH 4.6 in NaCl solutions, of the protein surface increased. However, the surface hydrophobicity, as measured by the cis-parinaric acid binding method, decreased. In contrast, WPI (9%) heated at 90 o C did not exhibit significant changes in the secondary structure content