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