On gelation of soy protein isolate during cold storage, strength, deformation, elasticity E 0 and Newtonian viscosity N of the gels greatly increased with addition of one unit/g protein of microbial transglutaminase when kept for 3 days at 5˚C, while retardation time decreased. With addition of 3 units/g protein, the gels were too hard, but became brittle after being kept for 3 days at 5˚C. The viscoelasticity of gel treated during cold storage was superior to that of gel heated after having been kept in cold storage. It was assumed that the texture of the gel treated for one day at 5˚C was nearly equivalent to that of the gel treated at 40˚C for 60 min, on enzyme reactivity of transglutaminase. e e e e-(␥-glutamyl)lysine bonds in the gels were not formed in the case of the gel without transglutaminase, but increased linearly in the gel with transglutaminase. Contents of the sulfhydryl group of the gel were found to decrease during cold storage, and the degree of decrease was smaller in the gel with transglutaminase than in the gel without transglutaminase. This indicated less contribution of disulfide bonds in the gel treated with transglutaminase during cold storage.Keywords: soy protein, gel formation, cold storage, microbial transglutaminase, e-(␥-glutamyl)lysine bonds, sulfhydryl groups Transglutaminase (glutaminyl-peptide: amine ␥-glutamyltransferase, E.C. 2.3.2.13; TGase) catalyzes an acyl transfer reaction between a ␥-carboxyamide of peptide or protein-bound glutamine and a primary amine.When TGase acts on protein molecules, e-(␥-glutamyl)lysine (abbreviated e-(␥-Glu)Lys) bonds are formed. Many studies have been carried out to use this unique enzyme reaction, crosslinking between protein molecules, to change rheological properties of food proteins (Whitaker, 1977;Ikura et al., 1980;Motoki & Nio, 1983). TGase, derived from a microorganism, has been found and mass produced (Ando et al., 1989). Enzymological properties and various basic effects on physical properties of food proteins have been reported Nonaka et al., 1992;Nonaka et al., 1994;Nonaka et al., 1996).The principal mechanism of gelation of soy protein isolate (abbreviated SPI) is due to the formation of disulfide bonds, reported by Wolf and Smith (1961), Circle et al. (1964), Aoki and Sakurai (1969), Saio et al. (1971) on heat-induced gel, and by Watanabe et al. (1963), andHashizume et al. (1974) on freezeinduced gel. On the other hand, as described in previous reports (Soeda, 1994a;1994b;1995a;Soeda & Baba, 1999), the gel (abbreviated Cold-gel) was obtained by keeping it in cold storage. The Cold-gel showed physical properties characterized by flexibility and springiness, which were excellent compared with the viscoelasticity of heat-induced or freeze-induced gel. We also reported that characteristics of gels required for application of SPI gel in food processing were flexibility and springiness related to masticability and swallowing in the mouth, and that Cold-gel provided an improved texture in processed foods (Soeda, 1995b). These superior t...