The heating of 7S globulin caused changes in the intensities, but hardly affected the positions of the peaks and troughs of the second derivative absorption spectra at wavelengths below 270 nm. On the other hand, above 271 nm, changes were reflected both in the intensities and in the positions of peaks and troughs. The difference-second derivative absorption spectra indicated that 60 and 70 percent, respectively, of phenylalanine and tyrosine residues buried in the native 7S globulin remained as the buried form even after heating.A spectrofluorimetry and fluorescence-quenching study suggested that one residue of tryptophan in the 7S globulin tended to be transferred to the more hydrophobic interior on heating.Heating contributes to the orientation of texture in a food system.1~4) Sulfhydryldisulfide interchange plays a great role in the formation of texture.5~7) Eleven S globulin, one of the major proteins in the soybean, contains more sulfhydryl and disulfide residues than 7S globulin. Thus, the former was used as a model protein and its thermal aggregation was examined previously.8~n) Umeyaet al.12) indicated the difference of hardening phenomena between 7S and US globulins: the apparent viscosity of 7S globulin increased considerably in the cooling process after heating, but that of US globulin scarcely changed.Japanese traditional foods such as tofu, soybean curd and aburage, fried soybean curd, are produced by heat processing. Saio et al.13

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Sulfhydryl and disulfide residues play a great role in texture formation.1>2) Heating causes modification of

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