Añón M C, Sorgentini D A, Wagner J R
Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA) and Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 47 y 116 (1900) La Plata, Argentina.
J Agric Food Chem. 2001 Oct;49(10):4852-8. doi: 10.1021/jf010384s.
Functional properties related to water protein interactions of soy protein isolates depend on the structural and aggregation characteristics of their major components (storage globulins 7S and 11S) that could be modified by the preparation procedure, thermal and/or chemical treatments, and drying methods. Commercial and laboratory isolates with different functionalities resulting from their structural modifications were compared. Isolates with high solubility or excessive thermally induced insolubilization or compact calcium-induced aggregates caused low water-imbibing capacity (WIC) values. The highest WIC results from the balance between intermediate solubility and the formation of aggregates with good hydration properties. The apparent viscosity of dispersions of commercial (spray dried) and laboratory (lyophilized) isolates depends on the WIC, the morphology and size of the particles, and the interaction of the hydrated particles. The hydration properties and viscosity of protein isolate suspensions were strongly determined by the amount and properties of the insoluble fraction.
大豆分离蛋白与水-蛋白质相互作用相关的功能特性取决于其主要成分（贮藏球蛋白7S和11S）的结构和聚集特性，这些特性可通过制备程序、热和/或化学处理以及干燥方法进行修饰。对因结构修饰而具有不同功能的商业分离蛋白和实验室分离蛋白进行了比较。具有高溶解度、过度热诱导不溶性或紧密钙诱导聚集体的分离蛋白导致低吸水能力（WIC）值。最高的WIC来自于中等溶解度与具有良好水合特性的聚集体形成之间的平衡。商业（喷雾干燥）和实验室（冻干）分离蛋白分散体的表观粘度取决于WIC、颗粒的形态和大小以及水合颗粒的相互作用。蛋白分离物悬浮液的水合特性和粘度强烈地取决于不溶部分的量和性质。
