The effects of thermal treatment on the subtilisin Carlsberg-induced coagulations of soy protein isolate (SPI) and soy proteins in 7S and 11S fractions, most of which are beta-conglycinin and glycinin, respectively, were examined by measuring the turbidity (OD(660)) of the reaction solutions. With the treatment at 37-60 degrees C, the turbidity did not increase at all by the proteolysis, while with the treatment at 70-96 degrees C, it drastically increased. The degree of the coagulation is the highest for the treatment at 80 degrees C and the most remarkable for 11S soy protein. Changes in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern of the digests during the proteolysis were in good agreement with those in the turbidities for SPI and 7S and 11S soy proteins. Circular dichroism analysis revealed that the amounts of nonstructured protein in SPI and 7S and 11S soy proteins were initially 40-50%, increased to 55-60% by the treatment at 80 degrees C, and further increased to 65-75% by the proteolysis. The maximum fluorescence intensity of SPI and 7S and 11S soy proteins increased with an increase in the incubation temperature up to 80 degrees C. These findings suggest that the thermal treatment at 80 degrees C most effectively changes the secondary structure of soy proteins and renders them coagulate when hydrolyzed by subtilisin Carlsberg.

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