Effects of microwave and water bath heating on the interactions between myofibrillar protein from beef and ketone flavour compounds

Abstract

AbstractThis paper presents the effects of microwave on the structure changes of myofibrillar protein compared with traditional water bath heating method. Under microwave or water bath heating conditions, α‐helix conformation of myofibrillar protein was converted into β‐turn, β‐sheet and randomly coiled structures gradually. T he fluorescence intensity of myofibrillar protein exhibited a marked red shift of the maximum absorption wavelength after microwave or water bath treatment. Total sulfhydryls groups and surface hydrophobicity contents were increased with progressing microwave or water bath treatment time. Results indicated that the thermal effects of microwave dominated the structure changes of myofibrillar protein, and microwaving also had an apparent influence on myofibrillar protein structure compared with water bath heating due to its nonthermal effects, and thus affecting the retention and release of ketone flavour compounds.