L-lysine enhances pork color through antioxidant activity and myoglobin conformational changes

Abstract

This study aimed to investigate the effect of L-lysine (Lys) on the color of pork and reveal the possible mechanism. The results showed that the L* and a* values increased from 53.69 to 56.32, 56.39, and 56.47, and from 12.93 to 13.21, 13.24, and 13.52 with the addition of 0.1 %, 0.15 % and 0.2 % Lys, respectively. Meanwhile, the oxymyoglobin (Fe2+) levels increased from 21.14 % to 22.63 %, 23.83 %, and 23.53 %, while the metmyoglobin (Fe3+) levels decreased from 44.69 % to 40.28 %, 41.21 %, and 41.63 % with the addition of 0.1 %, 0.15 % and 0.2 % Lys, respectively. Additionally, the addition of Lys increased total sulfhydryl and active sulfhydryl contents, and decreased the levels of reactive oxygen species (ROS) (P<0.05). The particle size and the absolute value of the ζ-potential increased with the addition of Lys, reaching maximum values of 534.39 nm and −13.73 mV, respectively. The molecular dynamics results suggested that Lys can bind to myoglobin (Mb) through hydrophobic interactions and hydrogen bonds, forming a stable Lys-Mb complex, acting as a protective shield to prevent the entry of ROS and other oxidizing agents. Finally, the addition of 0.15 % Lys resulted in the highest surface hydrophobicity, which was 5.79 μg. The multispectral results indicated that Lys primarily induces changes in the secondary and tertiary structures of Mb through interactions with tyrosine residues. These changes stabilized the free-moving rings within the amino acid residues of Mb, thereby improving the structural stability of Mb and ultimately enhancing the color stability of pork. In summary, Lys improved meat color stability through a dual mechanism of antioxidation and interaction with Mb to alter its conformational stability.