Developing efficient and promising tenderising techniques for postmortem meat is a heavily researched topic among meat scientists as consumers are willing to pay more for guaranteed tender meat. However, emerging tenderising techniques are not broadly used in the meat industry and, to some degree, are controversial due to lack of theoretical support. Thus, understanding the mechanisms involved in postmortem tenderisation is essential. This article first provides an overview of the relationship of ageing tenderisation and calpain system, as well as proteomics applied to identify protein biomarkers characterizing tenderness. In general, the ageing tenderisation is mediated by multiple biochemical activities, and it can exhibit better palatability and commercial benefit by combining other interventions. The calpain system plays a key role in ageing tenderisation functions by rupturing myofibrils and regulating proteolysis, glycolysis, apoptosis and metabolic modification. Additionally, tenderising techniques from different aspects including exogenous enzymes, chemistry, physics and the combined methods are discussed in depth. Particularly, innovation of home cooking could be recommended to prepare relatively tender meat due to its convenience and ease of operation by consumers. Furthermore, the combined interventions provide better performance in controlled tenderness. Finally, future trends in developing new tenderising techniques, and applied consideration in the meat processing industry are proposed in order to improve meat quality with higher economical value. Graphical

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.