Heat-induced polymerization behavior variation of frozen-stored gluten

The current study comparatively investigated the heat-induced polymerization behavior of fresh and frozen-stored gluten to replenish the gluten deterioration mechanism in frozen dough from the perspective of subsequent polymerization behavior during heating. The results showed that disulfide-mediated polymerization of frozen-stored gluten upon heating at 95 degrees C was suppressed. The polymerization ability of glutenin was weakened rather than gliadin for frozen-stored gluten. Enhanced level of beta-structures at the expense of alpha-helices was detected during the incipient heating of fresh gluten, while converse trend was noticed for the frozen-stored gluten. Frozen-stored gluten exhibited less exposure of surface hydrophobic groups during the initial heating, suggesting that it was less responsive to the unfolding process. The weakened viscoelastic properties of frozenstored gluten throughout heating protocols were mainly originated from glutenin macropolymer depolymerization as well as the hindered formation of glutenin-gliadin crosslinking and non-covalent bonds.