Changes in Protein Non-Covalent Bonds and Aggregate Size during Dough Formation
| Autor: | Bin Xiao Fu, Katsuyuki Hayakawa, Shiro Aono, Sonoo Iwaki, Chikako Otobe |
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| Rok vydání: | 2020 |
| Předmět: |
non-covalent bond
Health (social science) Low protein 030309 nutrition & dietetics Plant Science Protein aggregation lcsh:Chemical technology Health Professions (miscellaneous) Microbiology Article 03 medical and health sciences chemistry.chemical_compound 0404 agricultural biotechnology wheat mixing Non-covalent interactions lcsh:TP1-1185 chemistry.chemical_classification dough 0303 health sciences Aggregate (composite) flour High protein fungi aggregation nutritional and metabolic diseases food and beverages 04 agricultural and veterinary sciences Gluten Proteins 040401 food science Gluten Monomer chemistry Biophysics Food Science |
| Zdroj: | Foods, Vol 9, Iss 1643, p 1643 (2020) Foods Volume 9 Issue 11 |
| ISSN: | 2304-8158 |
| Popis: | This research investigated changes in the amounts and sizes of monomeric proteins and protein aggregates during dough mixing, with a focus on the contribution of non-covalent bonds in the aggregation of gluten proteins. High protein flour (HF) and low protein flour (LF) were used in this study. As dough mixing progressed from flour to overmixed dough, the total amount of protein aggregates increased while the amount of monomeric protein decreased. Omega-gliadin was the major monomeric protein that decreased in quantity. Interestingly, the amount of larger-sized protein aggregates decreased and that of smaller-sized protein aggregates increased. The amount of gluten protein macro-polymer aggregated through strong non-covalent bonds decreased whereas aggregates formed with weaker non-covalent bonds increased. LF dough behaved similar to HF dough. Large-sized gluten protein aggregates disaggregated due to the weakening of non-covalent bonds and became smaller. Omega-gliadin was incorporated into gluten protein aggregates during dough mixing. |
| Databáze: | OpenAIRE |
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