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肌球蛋白重链同工型表达、钙蛋白酶系统与不同山羊肌肉的品质特性。

Myosin heavy chain isoforms expression, calpain system and quality characteristics of different muscles in goats.

机构信息

Department of Agricultural Education, Faculty of Industrial Education and Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.

Department of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang, Bangkok 10520, Thailand.

出版信息

Food Chem. 2020 Aug 15;321:126677. doi: 10.1016/j.foodchem.2020.126677. Epub 2020 Mar 25.

DOI:10.1016/j.foodchem.2020.126677
PMID:32247180
Abstract

Myosin heavy chain (MHC) isoforms in goat muscles and their possible relationships with meat quality have not been fully elucidated. This study characterized the MHC isoforms in different caprine muscles using sodium dodecyl sulphate glycerol gel electrophoresis (SDS-GGE). The relationships between MHC isoforms, calpain systems and meat quality characteristics of different muscles in goats were examined. Four muscles, namely infraspinatus (IF), longissimus dorsi (LD), psoas major (PM) and supraspinatus (SS) were obtained from ten Boer crossbred bucks (7-10 months old; 26.5 ± 3.5 kg, BW). The percentages of MHC I, MHC IIa and MHC IIx in SS, IF, PM and LD were 47.2, 38.3, 32.1, 11.9; 28.0, 42.1, 33.0, 36.4; and 24.8, 19.6, 34.9 and 51.7, respectively. IF and SS had higher levels of calpastatin, total collagen and insoluble collagen contents than did PM and LD. PM had longer sarcomere length than did other muscles. LD had higher collagen solubility, troponin-T degradation products and glycogen content than did other muscles. These results infer that variable fiber-type composition could account partially for the differences in the physicochemical properties of goat muscles.

摘要

肌球蛋白重链(MHC)同工型在山羊肌肉中的特性及其与肉质的可能关系尚未完全阐明。本研究采用十二烷基硫酸钠甘油凝胶电泳(SDS-GGE)对不同山羊肌肉中的 MHC 同工型进行了特征描述。研究了 MHC 同工型与钙蛋白酶系统以及不同肌肉肉质特性之间的关系。从 10 只布尔杂交公山羊(7-10 月龄;26.5±3.5kg,BW)中获得了 4 块肌肉,分别为冈下肌(IF)、背最长肌(LD)、腰大肌(PM)和冈上肌(SS)。SS、IF、PM 和 LD 中的 MHC I、MHC IIa 和 MHC IIx 的百分比分别为 47.2%、38.3%、32.1%、11.9%;28.0%、42.1%、33.0%、36.4%;24.8%、19.6%、34.9%和 51.7%。IF 和 SS 的钙蛋白酶抑制蛋白、总胶原蛋白和不溶性胶原蛋白含量高于 PM 和 LD。PM 的肌节长度长于其他肌肉。LD 的胶原蛋白溶解度、肌钙蛋白-T 降解产物和糖原含量高于其他肌肉。这些结果表明,不同的纤维类型组成可能部分解释了山羊肌肉理化性质的差异。

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