【作者】 闫利国； 唐善虎； 王柳； 李思宁； 白菊红； 卢付青； 水旭亭；

【Author】 Yan liguo;Tang shanhu;Wang liu;Li Sining;Bai juhong;Lu fuqing;Shui xuting;College of Life Science and Technology,Southwest University for Nationalities;

【机构】 西南民族大学生命科学与技术学院；

【摘要】 探讨在普通包装和真空包装冻藏条件下的牦牛背最长肌和股二头肌的肌原纤维蛋白氧化变化。结果表明:羰基含量60天时显著增加（P<0.05）,除股二头肌普通包装组在90天保藏时的羰基含量显著升高外,其他处理组都呈下降趋势（P>0.05）;总巯基含量在冻藏60天内总体上升（P<0.05）,60天之后呈下降趋势;采用真空包装的两个处理组的表面疏水性在冷冻贮藏90天以后都比普通包装的低;背最长肌的Ca²⁺-ATPase活性比股二头肌的低,而K⁺-ATPase活性则无显著差异;背最长肌肌原纤维蛋白溶解性在整个试验周期中有显著变化（P<0.05）,股二头肌肌原纤维蛋白溶解性的变化不显著（P>0.05）。此外,冷冻贮藏期间的蛋白质条带发生了变化,肌球蛋白重链和肌动蛋白随着冻藏时间的延长都发生了不同程度的降解。该结果说明,随着冷冻贮藏时间的延长,肌原纤维蛋白发生了氧化。且随时间延长,蛋白氧化越严重,表面疏水性和溶解性越低,总巯基含量、K⁺-ATPase和Ca²⁺-ATPase活性越高。更多还原

【Abstract】 The objectives of this study were to investigate the myofibrillar protein oxidation of longissimus dorsi and biceps femoris in ordinary or vacuum packaging under the frozen storage conditions.Myofibrillar protein extraction,myofibrillar protein K-ATPase activity,Ca²⁺-ATPase activity,total sulfhydryl content,protein solubility,protein carbonyl content and surface hydrophobicity were measured,and the changes of protein electrophoresis were analyzed.The results show that the carbonyl content significantly increased at 60 days（P<0.05）,but decreased in all other treatment groups at 90 days except for a significant increase observed for biceps femoris under ordinary packaging（P>0.05）.The total sulfhydryl content significantly increased in general during the storage period for 60 days（P<0.05） but displayed a decreasing trend on the 60 th onward.For both muscles,hydrophobic surface with ordinary packaging was higher than that with vacuum packaging when the storage period exceeded90 days.Myofibrillar protein Ca²⁺-ATPase activity of longissimus drosi was higher than that of biceps femoris,yet no significant difference in K⁺-ATPase activity was observed.Myofibrillar protein solubility of longissimus drosi changed significantly（P<0.05）,while the changes in myofibrillar protein solubility of biceps femoris were not statistically significant（P>0.05）.Additionally,we found that protein bands changed during frozen storage.Myosin heavy chain and actin were degraded to varying degrees with prolonging the frozen storage time.This study indicates that with prolonged frozen storage time,oxidation occurs on myofibrillar protein of yak meat,which provides a strong basis for further clarifying the mechanism of muscle protein oxidation.更多还原