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Influence and effect mechanism of disulfide bonds linkages between protein-coated lipid droplets and the protein matrix on the physicochemical properties, microstructure, and protein structure of ovalbumin emulsion gels. | LitMetric

Influence and effect mechanism of disulfide bonds linkages between protein-coated lipid droplets and the protein matrix on the physicochemical properties, microstructure, and protein structure of ovalbumin emulsion gels.

Colloids Surf B Biointerfaces

Jiangxi Key Laboratory of Natural Products and Functional Food, Jiangxi Agricultural University, Nanchang 330045, China; Agricultural Products Processing and Quality Control Engineering Laboratory of Jiangxi, Jiangxi Agricultural University, Nanchang 330045, China. Electronic address:

Published: March 2023

AI Article Synopsis

  • * NEM-treated gels exhibited reduced hardness, water holding capacity, and surface hydrophobicity, while showing increased spin-spin relaxation time compared to untreated gels.
  • * Increased NEM concentration correlated with lower free sulfhydryl content and altered gel structure, indicating that disulfide bonds significantly enhance gel hardness and stability by promoting hydrophobic interactions and preventing larger aggregate formation.

Article Abstract

In this study, disulfide bonds between the interfacial protein film formed on the lipid particles and the protein in ovalbumin emulsion gels were blocked with 0, 1, 3, 5 and 10 mM of the N-ethylmaleimide (NEM) to explore the influence and effect mechanism of disulfide bonds between the interfacial proteins on the physicochemical properties, microstructure, and protein structure of sunflower oil-ovalbumin emulsion gels. Ovalbumin emulsion gels with NEM-treated ovalbumin emulsion (N-OE) had lower hardness, free sulfhydryl content, water holding capacity (WHC), and surface hydrophobicity, but higher spin-spin relaxation time (T) than ovalbumin emulsion gels with NEM-treated ovalbumin substrate solution (N-OSS). In addition, N-OE and N-OSS had lower hardness, free sulfhydryl content, WHC and surface hydrophobicity, as well as a more coarse and disordered microstructure than non-NEM treated ovalbumin emulsion gel (control group). The free sulfhydryl content, hardness, WHC, and surface hydrophobicity of the ovalbumin emulsion gels all decreased as the NEM concentration rose (p < 0.05), whereas the amide A band changed to higher wave numbers. These results collectively indicated that the reduction of disulfide between the interfacial layer and the proteins inhibited the hydrophobic effect, the formation of hydrogen bonds, and prevented the formation of larger aggregates. Thus the disulfide bonds between the interfacial proteins contribute to the hardness enhancement and water stabilization of the ovalbumin gel.

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Source
http://dx.doi.org/10.1016/j.colsurfb.2023.113182DOI Listing

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