Heat-induced polymerization behavior variation of frozen-stored gluten

Food Chem. 2018 Jul 30:255:242-251. doi: 10.1016/j.foodchem.2018.02.047. Epub 2018 Feb 12.

Abstract

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.

Keywords: Frozen storage; Gluten; Heat; Polymerization behavior.

MeSH terms

  • Freezing
  • Gliadin / chemistry
  • Glutens / chemistry*
  • Hot Temperature
  • Polymerization
  • Viscosity

Substances

  • Glutens
  • Gliadin
  • glutenin