Recombinant Rice Quiescin Sulfhydryl Oxidase Strengthens the Gluten Structure through Thiol/Disulfide Exchange and Hydrogen Peroxide Oxidation

J Agric Food Chem. 2022 Jul 27;70(29):9106-9116. doi: 10.1021/acs.jafc.2c01652. Epub 2022 Jun 23.

Abstract

Recombinant rice quiescin sulfhydryl oxidase (rQSOX) has the potential to improve the flour processing quality, but the mechanisms remain unclear. The effects of rQSOX on bread quality, dough rheology, and gluten structure and composition, with glucose oxidase as a positive control, were investigated. rQSOX addition could improve the dough processing quality, as proved by enhanced viscoelastic properties of dough as well as a softer crumb, higher specific volume, and lower moisture loss of bread. These beneficial effects were attributed to gluten protein polymerization and gluten network strengthening, evidenced by the improved concentration of SDS-insoluble gluten and formation of large gluten aggregates and the increased α-helix and β-turn conformation. Furthermore, decreased free sulfhydryl and increased dityrosine in gluten as well as improved H2O2 content in dough suggested that the rQSOX dough strengthening mechanism was mainly based on the formation of disulfide bonds and dityrosine cross-links in gluten by both thiol/disulfide direct exchange and hydrogen peroxide indirect oxidation pathways.

Keywords: disulfide bonds; dityrosine linkages; dough processing quality; gluten network; recombinant rice quiescin sulfhydryl oxidase.

MeSH terms

  • Bread
  • Disulfides
  • Flour
  • Glutens* / chemistry
  • Hydrogen Peroxide
  • Oryza*
  • Oxidoreductases
  • Peroxides
  • Rheology
  • Sulfhydryl Compounds / chemistry
  • Triticum / chemistry

Substances

  • Disulfides
  • Peroxides
  • Sulfhydryl Compounds
  • Glutens
  • Hydrogen Peroxide
  • Oxidoreductases
  • sulfhydryl oxidase