ArticleFood chemistry: X2024
Effect of N-ethylmaleimide as a blocker of disulfide bonds formation on the properties of different protein-emulsion MP composite gels.
Article in Food chemistry: X, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
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13 authors.
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Abstract
Three different emulsions of myofibrillar protein (MP), soy protein isolate (SPI) and egg white protein isolate (EPI) were individually mixed with MP sol to form composite gels. N-ethylmaleimide (NEM) was used as a sulfhydryl group blocker to evaluate the effects of sulfhydryl and disulfide bonds on the properties of different protein-emulsion composite gels. The results show that the disulfide bond contents in the MP (SPI, EPI) emulsion composite gel decreased from the initial 2.4 ± 0.1, (2.3 ± 0.2, 1.8 ± 0.4) mol/kg to 0.6 ± 0.1, (0.5 ± 0.3, 0.7 ± 0.1) mol/kg with the NEM content increased. In addition, the microstructure showed that the interfacial protein membrane of the emulsion globules were broken in different degrees, indicating that the interaction between the emulsion and the gel matrix was weakened. Meanwhile, gel strength, water distribution and elastic modulus of the composite gels were reduced with NEM contents increased.
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