Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates.
Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates.
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DOI：
10.1021/jf990823b
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发表时间：
2000-07
影响因子：
6.1
通讯作者：
J. Wagner;D. Sorgentini;M. Añón
中科院分区：
文献类型：
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作者：
J. Wagner;D. Sorgentini;M. Añón
由于水溶性是蛋白质的主要水合性质，因此对不同条件下制备的商品大豆分离蛋白和实验室大豆分离蛋白的溶解度值进行了比较分析。相反，蛋白质表现出的表面疏水性是一种物理化学性质，它在很大程度上决定了蛋白质分子聚集从而失去溶解度的倾向。基于这些理由，将分离物的溶解度作为其蛋白质表面疏水性的函数进行分析，结果确定了三组明确的实验室分离物：(a)原生，(B)部分或完全变性，具有高溶解度和表面疏水性，以及(C)完全变性，具有低溶解度和表面疏水性。商业分离株不能包括在这些类群中；它们被分为（A’）部分原生和（C’）完全变性。这两组的溶解度值与C组相似，但表面疏水性要低得多。讨论了导致上述基团的不同过程，以及大豆蛋白受特定制备条件（即蛋白质浓度、化学或热处理、盐的存在、干燥和磷脂添加等）影响的方式。
Because water solubility is the main hydration property of proteins, solubility values of commercial and laboratory soy protein isolates, prepared under different conditions, were comparatively analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical property that determines, to a great extent, the tendency of protein molecules to aggregate and so to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial isolates could not be included in any of these groups; they were grouped as (A') partially native and (C') totally denatured. Solubility values in these two groups were similar to those of group C, but the surface hydrophobicity levels were much lower. The different processes leading to the groups mentioned above are discussed, along with the way the soy proteins are influenced by the specific preparation conditions, namely, protein concentration, chemical or thermal treatments, presence of salts, drying, and phospholipid addition, among others.