Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions
| Autor: | Yi Luan, Mangang Wu, Qingling Wang, Zhikun Li, Juan Hu, Ge Qingfeng, Rui Liu, Hai Yu, Ranran Wei |
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| Rok vydání: | 2021 |
| Předmět: |
Health (social science)
Chemistry Chemical technology myofibrillar protein sulfhydryl-blocking agent disulfide bond protein-stabilized emulsions interface protein membrane N-Ethylmaleimide Disulfide bond Plant Science TP1-1185 Health Professions (miscellaneous) Microbiology Article food_chemistry chemistry.chemical_compound Polymer chemistry heterocyclic compounds Food Science |
| Zdroj: | Foods; Volume 10; Issue 12; Pages: 3079 Foods, Vol 10, Iss 3079, p 3079 (2021) Foods |
| DOI: | 10.20944/preprints202110.0267.v1 |
| Popis: | To investigate the role of sulfhydryl groups and disulfide bonds in different protein-stabilized emulsions, N-ethylmaleimide (NEM) was used as sulfhydryl-blocking agent to be added in the emulsion. The addition of NEM to block the sulfhydryl groups resulted in a reduction of the content of disulfide bonds formation, which enabled destruction of the internal structure of the protein molecule, and then decreased the restriction of protein membrane on the oil droplets. Furthermore, with NEM content increasing in the emulsion, a reduction of protein emulsifying activity and emulsion stability also occurred. At the same time, the intermolecular interaction of the protein on the oil droplet interface membrane was destroyed, and the emulsion droplet size increased with the NEM content in the emulsion. Although NEM blocking sulfhydryl groups not to form disulfide bonds has similar effects on three types of protein emulsion, the degree of myofibrillar protein (MP), egg-white protein isolate (EPI), and soybean protein isolate (SPI) as emulsifier had a subtle difference. |
| Databáze: | OpenAIRE |
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