AI Article Synopsis
- - This study investigates the effects of high-intensity ultrasound (HIU) combined with hydrogen peroxide (HO) on preventing the thermal aggregation of myofibrillar proteins (MPs) in water.
- - Results showed that adding HO disrupts certain molecular bonds in the proteins and alters cysteine to thiol derivatives, which helps reduce protein aggregation.
- - HIU, especially with 200 μmol/g of HO, was found to significantly improve the thermal stability of MPs by making it easier for protein structures to release buried sulfhydryl groups.
Article Abstract
This study was aimed at evaluating the potential of high-intensity ultrasound (HIU, 450 W for 10 min) combined with hydrogen peroxide (HO) having various concentrations (0, 50, 100, 200, 400, 800 μmol/g protein) to inhibit the thermal aggregation behavior of myofibrillar proteins (MPs) in water. The results indicated that the addition of HO interfered with the intermolecular sulfhydryl-disulfide interchange and inhibited the disulfide bond cross-linking. The HO-mediated conversion of cysteine to thiol derivatives appeared to be the primary mechanism of this effect. The HIU combined with HO, especially at the HO concentration of 200 μmol/g, corresponded to a more significant inhibitory effect than that of only HO, which attributed to the dissociation of the filamentous myosin structure that led to an enhanced accessibility of the buried sulfhydryl groups. In conclusion, these findings provide direct evidence for the role of HIU combined with HO in improving the thermal stability of MPs.
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| http://dx.doi.org/10.1016/j.foodchem.2021.130756 | DOI Listing |
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