4.7 Article

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

Journal

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.2c01652

Keywords

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

Funding

  1. Research and Development Plan in Key Areas of Guangdong Province [2020B020225004, 2019B020213002]
  2. National Natural Science Fund of China [31801474]
  3. Guangdong Special Support Program [2019BT02N112]
  4. Agricultural competitive industry discipline team building project of Guangdong Academy of Agricultural Sciences [202108TD]
  5. Special Fund for Scientific Innovation Strategy-Construction of High Level Academy of Agriculture Science [R2017YJ-YB1005, R2018PY-QF002, R2020PYJX009]
  6. Innovative Research Team Construction Project for Modern Agricultural Industry Common Key Technologies of Guangdong Province [2022KJ117]
  7. Innovative Research and Promotion Project for Modern Agricultural Industry Technology System of Guangdong Province [2022KJ1050]
  8. Guangdong Provincial Scientific and Technological Research Program [2020B020225004]

Ask authors/readers for more resources

Recombinant rice quiescin sulfhydryl oxidase (rQSOX) has been found to improve the flour processing quality by promoting gluten protein polymerization and network strengthening.
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 alpha-helix and beta-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.

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