RESUMO
Transglutaminase (TGase) induced-crosslinking of soy protein isolate (SPI) was markedly influenced by the substrate aggregation state. Results showed that appropriate heating significantly accelerated the TGase crosslinking, and the 7S and 11S acidic subunits were more susceptible to the enzyme than the 11S basic proteins. The content of ε-(γ-glutamyl)-lysine isopeptide bonds increased from 4.74 to 8.61 µmol/g protein when the heating intensity was increased from 75 °C for 15 min to 95 °C for 30 min, due to sufficient unfolding of the protein structure. Rheological data indicated that the gel formed from the SPI heated at 95 °C for 30 min exhibited the best properties, with a 60 % increase in the storage modulus compared with the unheated sample. However, excessive heating (95 °C, 60-120 min) caused severe aggregation of SPI and formation of insoluble aggregates, resulting in poor crosslinking efficiency and weaker gel properties.