Abstract: We undertook this study in order to determine the shelling efficiency of scallops with ultrahigh pressure (UHP) and its impact on the structure of scallop adductor muscle (the 2 mm thick segment contacting with the shell) as studied by Raman spectroscopy and scanning electron microscopy (SEM). It was found that the main-chain structure and side-chain conformations of adductor muscle protein were greatly affected by UHP treatment. Notably, at 200 and 300 MPa, the intensity of the characteristic peaks of adductor muscle protein was increased, but the degree of protein denaturation was not very obvious. When the pressure was greater than 200 MPa, the oxygen atoms of the hydroxyl group on the benzene ring of tyrosine residues were gradually transformed from a hydrogen bond donor to a hydrogen bond acceptor, I850 cm-1/I830 cm-1 ratio was decreased, the buried tryptophan residues were gradually exposed to a polar environment, and the conformation of the disulfide bond was reduced. In conclusion, UHP can impact on the structure of scallop adductor muscle, which will provide a theoretical basis and technical support for the industrial production of scallop products and even other shellfish products.

Key words: scallop; ultrahigh pressure; interfacial adductor muscle; protein structure