Gelation and gel properties of soybean glycinin in a transglutaminase-catalyzed system

Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase

“…In the subunits of -conglycinin, the susceptibility of -subunit to MTGase was lower than that of Ј-and -subunits. Similar results have been reported in TGase or MTGase-induced cross-linking reactions of soy globulins and pea legumin (Kang et al, 1994;Larré, Kedzior, Chenu, Viroben, & Gueguen, 1992;Nonaka et al, 1989;Zhang, Matsumura, Matsumoto, Hayshi, & Mori, 2003). The reactivity diVerence of protein constituents of SPI to MTGase could be considered to relate with the native structure of glycinin and -conglycinin.…”

“…This indicated a rapidly increasing degree of covalent cross-linking of the components forming the three-dimensional network, and that a more elastic gel matrix was formed. Similar change patterns of the mechanical moduli were observed in the MTGase-catalyzed gelation of soybean glycinin (Kang et al, 1994) and casein micelles (Schorsch, Carrie, Clark, & Norton, 2000). The on-set of gelation of SPI Fig.…”

Adsorption of oat proteins to air–water interface in relation to their colloidal state

“…a-polypeptide was more prone to intermolecular crosslinking compared to the bpolypeptide. The higher reactivity of the acidic polypeptide to microbial TG compared to the basic polypeptide was previously reported for oat globulins as well as soy glycinin (Hsieh, Yu, Chang, Chen, & Tsai, 2014;Kang et al, 1994;Zhang, Matsumura, Matsumoto, Hayashi, & Mori, 2002). It was related to the structural characteristics of the subunit as the basic polypeptide possess a highly compact secondary structure and located tightly folded in the interior of the globulin molecule, surrounded by the more hydrophilic acidic polypeptides (Shotwell, Afonso, Davies, Chesnut, & Larkins, 1988).…”

Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

“…Enzyme accessibility to substrate and protein solubility have been identified as playing roles in transglutaminase cross-linking (Coussons et al, 1992;Kang et al, 1994). Thus, Renzetti et al (2008a) concluded that the improved baking performance of buckwheat flours treated with transglutaminase was due to the high level of glutamine and lysine in the soluble protein fraction of the flour and also potentially the presence of more accessible enzyme binding sites than oat flours.…”