Microwave heating (MW), as a sustainable food processing approach, has advantages in reducing surimi wastewater, saving energy, and enhancing the gelling properties of surimi gels. However, the molecular forces involved in microwave-induced gels and promotion mechanism are not well understood. In this study, an equivalent energy input model between MW and conventional water bath heating (WB) was established, aggregation behavior and changes in redox proteomics were investigated during MW treatment. The morphology of myofibrillar proteins (MPs) studied by transmission electron microscopy and atomic force microscopy showed that the proteins in WB group is more inclined to irregular cluster aggregation, while microwaves make the molecules tend to be homogeneous, dispersive, and small-scale aggregation, which has been proved to be related to the electrostatic distribution on the protein surface. Moreover, MW could significantly facilitate disulfide bonds formation, resulting a strengthening covalent bonds crosslinking. Further analysis of redox proteomics revealed that a larger number of MPs were found to be highly susceptible to oxidation under microwave irradiation. Notably, MW caused oxidative modifications of cysteine residue at the head of myosin, revealing the enhancement mechanism of MP gelation by excess cysteine cross-linking. Overall, these results clearly indicated that the disulfide bond and electrostatic interaction play an indispensable role in the aggregation process of myofibrillar proteins, and providing a further understanding of the microwave-induced gelling mechanism, which could be meaningful for the green surimi-based products fabrication.

Microwave-induced specific aggregation behavior myofibrillar proteins

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