The present findings indicate that myofibrillar protein of grass carp is susceptible to γ-irradiation, as evidenced by the qualitative and structural changes of protein.
After γ-irradiation, emulsifying activity index, emulsion stability index and sulphydryl group content of myofibrillar protein decreased. Surface hydrophobicity increased from 0 kGy to 6 kGy but decreased as the dose increased. High-molecular myosin heavy chains in the SDS-PAGE patterns initially decreased slightly from 0 kGy to 4 kGy and then significantly decreased from 6 kGy to 10 kGy. Results indicated that myofibrillar protein was dominated by unfolding first and then protein crosslinking played a major role. These stages are involved in a two-stage process. Future research may provide theoretical reference for the identification of irradiated fish products