Molecular basis of sodium chloride dominated glutenin interaction and bread properties

Dough elasticity and bread quality depend on the gluten network formation which by nature is the oxidative crosslinking of glutenin. It is known for long, either in the kitchen or in the laboratory, sodium chloride (NaCl) enhances dough rheological properties while itself is not an oxidant. However,...

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Veröffentlicht in:Food science & technology 2021-05, Vol.142, p.111011, Article 111011
Hauptverfasser: Guo, Yizhan, Zhao, Chunfei, Yu, Peixuan, Gao, Jihui, Liang, Zhongxin, Ji, Ruiyang, Du, Haolan, Fu, Jiahui, Liang, Jianfen, Yang, Dong
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Sprache:eng
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Zusammenfassung:Dough elasticity and bread quality depend on the gluten network formation which by nature is the oxidative crosslinking of glutenin. It is known for long, either in the kitchen or in the laboratory, sodium chloride (NaCl) enhances dough rheological properties while itself is not an oxidant. However, besides NaCl induced gluten aggregation, the molecular mechanism behind this phenomenon is largely unknown. Azodicarbonamide (ADA) and Vitamin C (Vc) improve dough qualities with different mechanisms. Here, response surface methodology (RSM) was used to study the synergistic effect of ADA, Vc and NaCl on the dough and subsequent bread qualities. Results show that NaCl dominates the dough alveographic characters in the presence of oxidative flour improvers, and fine tune of NaCl concentration profoundly impacts subsequent bread properties. Consistent with free sulfhydryl assay and glutenin gel electrophoresis analysis, simulation study reveals that NaCl concentration affects glutenin conformation and intermolecular interaction which in turn impacts their orientation adjustment that lead to sulfhydryl contact and crosslinking. [Display omitted] •NaCl exhibits dominating effect on dough alveography than chemical improvers.•NaCl exhibits synergistic effect with oxidative flour improver.•Bread properties yield high sensitivity to NaCl at optimal improver conditions.•NaCl affects glutenin conformation and their intermolecular interactions.
ISSN:0023-6438
1096-1127
DOI:10.1016/j.lwt.2021.111011