温柔
肌原纤维
化学
肌苷酸
糖酵解
动物科学
最长肌
肉的嫩度
肌苷
食品科学
生物化学
解剖
生物
新陈代谢
酶
基因
核苷酸
作者
Xue Chen,Xin Luo,Lixian Zhu,Rongrong Liang,Pengcheng Dong,Xiaoyin Yang,Lebao Niu,David Hopkins,Shujuan Gao,Yanwei Mao,Yimin Zhang
出处
期刊:Meat Science
[Elsevier]
日期:2022-12-01
卷期号:194: 108976-108976
被引量:4
标识
DOI:10.1016/j.meatsci.2022.108976
摘要
This study investigated the effect of superchilling (-30 °C until the core temperature achieved -3 °C, then stored at -1 °C until 24 h, SC) on the tenderness of hot boned beef M. longissimus lumborum (LL), with very fast chilling (-30 °C until the core temperature achieved 0 °C, then stored at -1 °C until 24 h, VFC) and conventional chilling (0- 4 °C for 24 h, CC) as the controls. The lowest initial shear force values were obtained in SC samples compared to those from the VFC and CC treatments (P < 0.05). Clear freezing damage of muscle fibers and more myofibril fragmentation were found in SC samples compared with the other samples early post-mortem. Moreover, SC samples showed the highest level of inosine 5-monophosphate at 3 h post-mortem (P < 0.05). A reduced glycolysis rate (as evidenced by lactate content) was also found in SC treated samples suggesting little contribution of glycolysis on the tenderization of SC.
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