赖氨酸
肌球蛋白
精氨酸
化学
离解(化学)
食品科学
生物化学
萃取(化学)
色谱法
氨基酸
有机化学
作者
X.W. Fan,Xun Gao,Cunliu Zhou
标识
DOI:10.1016/j.foodchem.2024.138809
摘要
This study investigated the individual and combined effects of l-arginine, l-lysine, and NaCl on the ultrastructure of porcine myofibrils to uncover the mechanism underlying meat tenderization. Arg or Lys alone shortened A-bands and damaged M-lines, while NaCl alone destroyed Z-lines. Overall, Arg and Lys cooperated with NaCl to destroy the myofibrillar ultrastructure. Moreover, these two amino acids conjoined with NaCl to increase myosin solubility, actin band intensity, and the protein concentration of the actomyosin supernatant. However, they decreased the turbidity and particle size of both myosin and actomyosin solutions, and the remaining activities of Ca2+- and Mg2+-ATPase. The current results revealed that Arg/Lys combined with NaCl to extract myosin and dissociate actomyosin, thereby aggravating the destruction of the myofibrillar ultrastructure. The present results Tprovide a good explanation for the previous phenomenon that Arg and Lys cooperated with NaCl to improve meat tenderness.
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