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In the present study, egg white protein (EWP) and myofibrillar protein (MP) were mixed in different ratios (0/100, 10/90, 20/80, 30/70, 40/60, 50/50, 100/0 for EWP/MP) and subjected to unheated, preheated (40 • C/30 min), twostep heated (40 • C/30 min, 90 • C/20 min), and one-step heated (90 • C/20 min) treatments to study the thermal aggregation of the two proteins. Their aggregation behavior was characterized by turbidity, active sulfhydryl, degree of protein cross-linking, protein characteristic spectra, and microscopic morphology. The results indicated that for the mixed protein system composed of EWP and MP, the mixed protein aggregation volume was larger and regular at an EWP/MP of 30/70, when the degree of cross-linking was best. When the ratio of EWP/MP was 50/50, the aggregate-protein interaction was dominant, and the excess EWP acted as a barrier to cross-linking and wrapped around the surface of the aggregates to form larger aggregates. Comparing the two-step heated and one-step heated conditions, the former is superior. K E Y W O R D Segg white protein, myofibrillar protein, thermal aggregation Practical Application: The combination of egg white protein and myofibrillar protein can provide a theoretical reference for the protein content in surimi products, and moderate addition has an enhancing effect on surimi protein crosslinking and promotes gel formation. Excessive addition will form aggregates outside the egg white protein wrapping phenomenon, and the quality of surimi gel products will be affected.

The synergistic effects of the combination of ultrahigh pressure (UHP) with allicin on the gel properties, flavor characteristics, and myosin structure of scallops were investigated. The results indicated that chewiness reached maximum, uniform, and dense microstructures at B‐300 MPa, and scallops with favorable gel properties. In addition, the electronic nose and tongue could clearly distinguish the olfactory and gustatory properties of scallops, and the interaction of UHP and allicin increased the variety of volatile compounds in scallops, which mainly included 1‐hydroxy‐2‐propanone, 1‐hexenal, 2‐butanone‐D, and 1‐octen‐3‐ol. The main performance was fruit aroma and a plantlike aroma and mushroomlike odor. UHP and allicin changed the microenvironment of tryptophan residues, and allicin formed larger aggregates by forming disulfides with myosin. The sodium dodecyl sulfate–polyacrylamide gel electrophoresis results could show that myosin had low degradation in B‐300 MPa. Thus, comprehensively viewed, UHP and allicin play a role in gel formation of myosin from obturator muscle at 300 MPa, whereas allicin and myosin form disulfides as the main factor of myosin gelation. Practical Application To enhance the diversity of scallop preparation methods and improve the quality of the obtained product, UHP and allicin treatment result in scallops with satisfactory chewiness and flavor, which provides application prospects for scallop processing.