Regulation in protein hydrophobicity via whey protein-zein self-assembly for improving the techno-functional properties of protein.

Autor: Shao F; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Zhang Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Wan X; Oil Crops Research Institute, Chinese Academy of Agricultural Sciences, Wuhan 430062, China., Duan Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Institute of Food Physical Processing, Jiangsu University, Zhenjiang 212013, China. Electronic address: dyq101@ujs.edu.cn., Cai M; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Hu K; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Zhang H; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2025 Jan 15; Vol. 463 (Pt 2), pp. 141174. Date of Electronic Publication: 2024 Sep 10.
DOI: 10.1016/j.foodchem.2024.141174
Abstrakt: This work aims to verify the feasibility of improving protein function by regulating its hydrophobicity and reveal the relationship between structure and function. Whey protein (WP) and zein were the source of hydrophilic and hydrophobic polypeptide chains to prepare complex proteins (CPs) with much different structure and function. The results showed that the water- and oil-holding capacities, emulsifying properties and gel properties of CPs can be significantly improved via changing WP-zein ratio. All these can be attributed to the changes in protein hydrophobicity, which not only regulated the binding strength of protein to water and oil, but also modified their molecular structure (surface characteristics, availability of free thiols, α-helix, β-sheet, random coil and the formation of disulfide bonds). Notably, optimal protein hydrophobicity varies greatly among different functional properties. Overall, the techno-functional properties of protein can be improved via tuning its hydrophobicity, which may provide novel sights in protein modification.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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