肌节
肌球蛋白
肌动蛋白
肉的嫩度
肌原纤维
温柔
生物物理学
解剖
肌肉收缩
化学
肌丝
生物
生物化学
食品科学
心肌细胞
细胞生物学
作者
Per Ertbjerg,Eero Puolanne
出处
期刊:Meat Science
[Elsevier]
日期:2017-05-19
卷期号:132: 139-152
被引量:243
标识
DOI:10.1016/j.meatsci.2017.04.261
摘要
The basic contractile unit of muscle, the sarcomere, will contract as the muscle goes into rigor post-mortem. Depending on the conditions, such as the rate of pH decline, the cooling rate and the mechanical restraints on the muscles, this longitudinal shortening will result in various post-mortem sarcomere lengths as well as lateral differences in the distances between the myosin and actin filaments. This shortening is underlying the phenomena described as rigor contraction, thaw rigor, cold shortening and heat shortening. The shortening in combination with the molecular architecture of the sarcomere as defined by the myosin filaments and their S-1 and S-2 units, the interaction with the actin filaments, and the boundaries formed by the Z-disks will subsequently influence basic meat quality traits including tenderness and water-holding capacity. Biochemical reactions from proteolysis and glycogen metabolism interrelate with the sarcomere length in a complex manner. The sarcomere length is also influencing the eating quality of cooked meat and the water-holding in meat products.
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