Evaluation of ultrasound-assisted L-histidine marination on beef M. semitendinosus: Insight into meat quality and actomyosin properties

The tentative mechanism concerning the improvement of water retention and tenderness in UMH-treated meat On the one hand, ultrasonication disrupted the myofibril integrity, resulting in the preliminary weak connection between actin and myosin. Meanwhile, the changed microstructure provided the opportunity for the filtration of L-histidine to intervene the isoelectric point and conformation of muscle protein, which was accompanied higher pH value for accelerating postmortem ageing with optimized tenderness. On the another hand, the filtrated L-histidine might competitively inhibit the actin-myosin binding by the imidazole group, and combine with the aromatic or acidic residues of myosin molecules. The combination of ultrasound and L-histidine produced smaller particle size of actomyosin with higher solubility, enhancing the cross-linking of myosin tail for the formation of complex structure to well retain water. [Display omitted] •UMH avoided excessive liquid withdrawal and disrupted myofibril integrity.•Lower relaxation times and higher pH value were found in UMH-treated meat.•UMH accelerated postmortem ageing by modifying ATPase and caspase-3 activity.•UMH shield hydrophobic area and competitively inhibited actin-myosin binding.•Complex structure formed by cross-linking of myosin tail improved water retention. This paper aimed to evaluate the effects of ultrasound-assisted L-histidine marination (UMH) on meat quality and actomyosin properties of beef M. semitendinosus. Our results found that UMH treatment effectively avoided excessive liquid withdrawal, and disrupted myofibril integrity by modifying the water distribution and weakening connection of actin-myosin with increased muscle pH. The ultrasound-treated sample provided more opportunity for the filtration of L-histidine to intervene the isoelectric point and conformation of muscle protein. The activated caspase-3 and changes of ATPase activity in UMH-treated meat accelerated the postmortem ageing, and L-histidine might competitively inhibit the actin-myosin binding by the imidazole group. UMH decreased the surface hydrophobicity by shielding hydrophobic area and unfolding the actomyosin structure. In addition, the increased actomyosin solubility with smaller particle size enhanced the SH content for better cross-linking of myosin tail, and formation of heat-set gelling protein structure. Therefore, UMH treatment manifested the potential to improve beef quality.