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
Xiaokang Fan,Xun Gao,Cunliu Zhou
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2024-02-23
卷期号:446: 138809-138809
被引量:6
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 M- and 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 Ca
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