Relationships between different hydration properties of commercial and laboratory soybean isolates.
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.
Añón
M C
MC
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.
Sorgentini
D A
DA
Wagner
J R
JR
D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006358:Hot Temperature; D008855:Microscopy, Electron, Scanning; D012995:Solubility; D030262:Soybean Proteins / Q000737:chemistry*; D013025:Glycine max / Q000737:chemistry*; D014783:Viscosity; D014867:Water
D030262:Soybean Proteins; D014867:Water