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  • Title: Modulating the aggregation of myofibrillar protein to alleviate the textural deterioration of protein gels at high temperature: The effect of hydrophobic interactions.
    Author: Chen B, Guo J, Xie Y, Zhou K, Li P, Xu B.
    Journal: Food Chem; 2021 Mar 30; 341(Pt 2):128274. PubMed ID: 33038801.
    Abstract:
    In this study, the strategy of utilizing a model hydrophobic molecule, octenyl succinic anhydride (OSA), to inhibit over-aggregation of MP during heating, aiming to alleviate high temperature-induced textural deterioration of MP gels, was proposed, and a series of experiments were conducted to verify the effectiveness. The results showed that the effect was positively dependent on the concentrations of OSA. The addition of OSA at a concentration of 4 g/kg to 24 g/kg delayed the gelation temperature of MP, as confirmed by the DSC results, and inhibited the aggregation of MP through hydrophobic interactions between OSA and MP, as revealed by fluorescence and FTIR spectroscopy. Furthermore, when the concentration of OSA increased from 4 g/kg to 12 g/kg, the controlled aggregation of MP improved the gel properties of MP formed at high temperature, but when the concentration reached 24 g/kg, the protein aggregation was too inhibited to form developed gel networks.
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