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Dynamic shear moduli of isolated soy protein solutions upon heating were measured to monitor gelation. Onsetsof gelation coincide with onset temperatures of denaturation in glycinin and β-conglycinin solutions, whereas in isolated soyproteins, onset of gelation was above denaturation temperature of β-conglycinin with storage modulus increasing in two steps.The first increase in storage modulus of isolated soy proteins occurred at about 78.5oC, while the second increase started atabout 93oC. Gel properties of soy protein gels having different proportions of glycinin and β-conglycinin were measured bycompression-decompression test. β-Conglycinin was responsible for gel elasticity. Glycinin significantly increased hardness,toughness, and fracturability of gels at high heating temperature near 100oC. Results reveal texture of soy protein gels can becontrolled by regulating ratio of glycinin to β-conglycinin and heating temperature.