Actomyosins are the main functional proteins of scallop adductor muscle proteins and they play a key role in the quality of shellfish products.Actomyosins were extracted from the adductor muscle of scallop(Patinopecten yessoensis).Effects of heating temperature and time on the α-helix content,surface hydrophobicity,reactive sulfhydryl content and turbidity of scallop actomyosins were investigated.The experiment results showed that in the heating process the α-helix and peptide chains unfolded,residues of hydrophobic amino acid exposed,surface hydrophobicity of protein enhanced.At the same time,heat treatment converted reactive sulfhydryl into disulfide key,proteins gathered together,and the turbidity increased.The changes in these parameters accelerated as heating temperature increased.A conclusion can be induced that the thermal denaturation process of scallop adductor muscle actomyosins was accompanied with peptide chains despiralization and random aggregation.