Abstract: Composition and properties of fish muscle protein determines its processing characteristics and product features. In this study,Japanese flounder and turbot muscle were used as research materials,protein pattern of muscle was analyzed using SDS-PAGE,thermal properties and rheological properties were studied with DSC and rheometer. Emulsifying and foaming capability of myofibrillar protein(MFP)were also investigated. It is showed that SDS-PAGE electrophoresis analyses found distinct differences in myosinogen and MFP proteins between Japanese flounder and turbot muscle. Turbot muscle had different bands in a molecular weight range of 20.1 kDa to 44.3 kDa in myosinogen,Japanese flounder showed a different band in MFP proteins at 97.2~66.4 kDa.Different scanning calorimetric(DSC)study showed that the denaturation point of flounder MFP was 39.98℃,higher than that of turbot MFP,which was 37.86℃. A peak was observed in loss modulus of flounder MFP and turbot MFP at range of 30 to 40℃. As protein concentration increased,emulsifying activity index(EAI),emulsifying stability index(ESI),foaming capability(FC)and foaming stability(FS)of myofibrillar protein showed a decreasing trend. It is showed that the ESI of flounder MFP was higher than that of the turbot at low concentration. FS of flounder MFP was higher than that of the turbot at medium and high concentration,the consequence at low concentration was opposite. As protein concentration increased,the foaming properties of turbot tend to be stable. The results showed that the muscle protein patterns with SDS-PAGE,and functional properties for rheological properties,EAI and FC of these two MFP all had significant differences.