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Optimum temperature and pH for the isolation of soy protein isolate (SPI) from soy protein concentrate (SPC) were established. Enzymatic hydrolysis of SPI with enzymes of different specificities such as trypsin, chymotrypsin, papain and urease was carried out and the products of hydrolysis were characterized by molecular mass determination [sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)] and thermal techniques [differential scanning calorimetry (DSC) and thermogravimetric analysis (TG)]. Enzymatic hydrolysis resulted in a significant reduction in molecular masses. However the thermal stability of hydrolysed SPI was similar to native SPI indicating that it is independent of molecular mass. DSC studies indicated an increase in temperatures of endothermic transition associated with SPI denaturation and loss of absorbed moisture in samples of lower molecular masses. [ABSTRACT FROM AUTHOR]

Thermal behaviour of blends based on N,N'-bis(4-itaconimidophenyl) ether (IE) and 4,4'-bis(4-allyl-2-methoxyphenoxy) benzophenone (R1) or 4,4'-bis(2-allylphenoxy) benzophenone (R2) are described in this paper. The reactive diluent content was varied from 5-50% (mass/mass) in these blends. A decrease in the melting point and exothermic peak temperature was observed with increasing mass percent of reactive diluent. Thermal stability of blends was affected at high mass percentage of reactive diluents. [ABSTRACT FROM AUTHOR]