l‐Arginine and l‐lysine can weaken the intermolecular interactions of main myofibrillar proteins: the roles in improving the tenderness of pork Longissimus lumborum muscle

Abstract

This work aims at investigating the mechanisms underlying the effects of L-arginine and L-lysine on the tenderness of pork Longissimus lumborum muscle. The results indicated that on day 7, L-arginine and L-lysine were able to decrease the shear force from 71.47 to 27.59 or 32.53 N, but raise the myofibrillar fragmentation index from 70.93 to 88.2 or 92.4, compared to the control. Additionally, L-arginine inhibited the degradation of desmin, troponin-T and titin; while L-lysine inhibited the degradation of desmin, troponin-T, titin and nebulin. L-Arginine, especially L-lysine alleviated the Z-disc damage, while accelerated the M-line damage. L-Arginine and L-lysine promoted the extraction of myosin, titin and some unidentified proteins, decreased ionic bonds but increased hydrophobic interactions. The results suggest that the weakening of the intermolecular interactions between main myofibrillar proteins by L-arginine or L-lysine may play crucial roles in improving meat tenderness. The finding may broaden the way to tenderise meat.

Effect of ultrasound‐assisted L‐lysine treatment on pork meat quality and myofibrillar protein properties during postmortem aging

“…Furthermore, the impact of their combined application on the biochemical reactions, protein characteristics, and the formation of final meat quality during post-mortem maturation remained unclear. Myofibrillar proteins, the main constituent of muscle protein, were major contributors to the quality of meat and meat products (Chen et al, 2023;Guo et al, 2022;Yan et al, 2018). Therefore, this paper aimed to comprehensively investigate the influence of ultrasound-assisted Lys treatment on the properties of MPs and the overall pork meat quality during the post-mortem aging process, and explore the relationship between changes in MPs properties and meat quality.…”