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 °C was suppressed. The polymerization ability of glutenin was weakened rather than gliadin for frozen-stored gluten. Enhanced level of β-structures at the expense of α-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 frozen-stored 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.