Synergistic effect of ultrahigh pressure and allicin on gel properties, flavor characteristics, and myosin structure of the obturator muscle of the scallop (Patinopecten yessoensis).

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.