肌原纤维
提丁
变性(裂变材料)
肌球蛋白
化学
溶解度
食品科学
肌浆
星云素
肌节
温柔
持水量
色谱法
生物化学
生物
内分泌学
心肌细胞
内质网
有机化学
核化学
作者
Robyn D. Warner,R. G. Kauffman,Marion L. Greaser
出处
期刊:Meat Science
[Elsevier]
日期:1997-03-01
卷期号:45 (3): 339-352
被引量:357
标识
DOI:10.1016/s0309-1740(96)00116-7
摘要
The relationship between post-mortem traits of muscle proteins and water loss traits was investigated using 84 pork loins representing the four quality traits of PSE, RSE (reddishpink, soft, exudative), RFN (reddish-pink, firm, non-exudative) and DFD. Protein solubility measurements (sarcoplasmic, myofibrillar and total) were lower and myosin denaturation (quantified by myofibrillar ATPase activity) was higher for PSE samples compared with samples from the other quality classes. RSE samples were similar to RFN samples in protein solubility and myosin denaturation, although RSE had lower values then DFD samples for protein solubility measurements. RFN samples had lower drip, thaw, cook and total water loss than RSE samples and all water loss traits were lowest for DFD samples and highest for PSE samples. Insoluble phosphorylase was the only characteristic that differentiated among PSE, RSE and RFN samples. SDS-PAGE and Western blots indicated that in PSE and RSE samples, the myofibrillar protein titin was less degraded and nebulin was more degraded compared with RFN and DFD samples. SDS-PAGE of extracted and unextracted myofibrils showed that the reduced myofibrillar solubility of PSE samples was caused by decreased extractability of the myosin heavy chain in these samples. In conclusion, although RSE samples have unacceptably high water loss, muscle protein denaturation was minimal and did not explain the low water-holding capacity.
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