The contribution of soybean protein to the physical properties of tofu, a product manufactured by curdling soy milk with coagulants such as calcium or magnesium chloride, was studied by comparing the properties of soy milk prepared from soybeans with different subunits (I, IIa, and IIb) of glycinin with amino acid residues deleted. The breaking stress value of the tofu curds prepared from soybeans having group I was higher than those without group I. The soy milks having group I contained more protein particles and showed more sensitivity to calcium and magnesium ions than those without group I. The amounts of glycinin and protein particles were higher in the soy milks having group I than those in the soy milks without group I. To elucidate the influence of each group on the breaking stress, the glycinin content was adjusted to an identical level in soy milks having each group. Among the tofu curds from three groups, their order of hardness according to their breaking stress was IIa, IIb, and I. The order of particle content among these soy milks was also IIa, IIb, and I. Therefore, the results suggested that the breaking stress value of the tofu curd is dependent upon the number of protein particles in the soy milk and that the number of the particles is determined by the proportion and structure of glycinin in the soybean.

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Soybean glycinin groups I, IIa, and IIb were purified from soybeans composed of only glycinin groups I, IIa, and IIb, respectively. When these protein solutions were heated, the amount of the particulate protein formed in these solutions was greatest in the order of groups IIa, IIb, and I. The protein solubilities decreased upon the addition of magnesium chloride in the order of groups IIa, IIb, and I. It was determined by differential scanning calorimetry analysis that the denaturation temperatures of groups I, IIa, and IIb were 92.8, 96.0, and 97.9 degrees C, and that the enthalpies of their transitions were 24.2, 27.4, and 28.1 J g(-)(1), respectively. The alpha-helix rates of groups I, IIa, and IIb in aqueous solution were analyzed by circular dichroism and were 19, 16, and 15%, respectively. The beta-sheet rates of groups I, IIa, and IIb were 44, 38, and 39%, respectively. In all group proteins, the alpha-helix rates were decreased by heating and the beta-sheet rates were increased. The surface hydrophobicity of these group proteins increased as a result of heating, and those of groups IIa and IIb were larger than that of group I. The surface hydrophobicity of these protein groups increased by heating, and those of groups IIa and IIb were larger than that of group I and beta-conglycinin. Breaking stress of curds prepared from these group proteins containing more than 1 of beta-conglycinin ration showed similar values, but the order of those containing less than 1 in strength was groups I, IIb and IIa. These results suggest that the increase of particulate contents and the curd formation are related to the increase of surface hydrophobicity by heating.

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