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標題: 不同嫩度台灣土雞股二頭肌之蛋白質表現差異
Differential protein expression in Biceps femoris muscles with different tenderness in Taiwan country chickens
作者: 吳鍺湘
Che-Hsiang Wu
關鍵字: 股二頭肌;嫩度;台灣土雞;蛋白質體;Biceps femoris muscle;tenderness;proteome;Taiwan country chickens
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台灣土雞之肉質具有豐富的風味與嚼勁,受到消費者的喜好,在市場上有重要的地位。嫩度(tenderness)是消費者購買肉品時考慮的重要因素之一,直接影響消費者接受度。蛋白質體技術(proteomic technology)應用於肉品科學中,多在改善牛肉與豬肉品質,但應用於禽肉之研究甚少,故本研究之目的在探討不同嫩度台灣土雞股二頭肌(Biceps femoris)之蛋白質差異表現,以期作為改善土雞肉品質之參考生物標誌。試驗使用16與20週齡畜試土雞近親品系L11各10隻,屠宰後取其股二頭肌,測定截切值、膠原蛋白含量及可溶性膠原蛋白百分比等與嫩度相關之性狀,將數值依加權公式計算後得到之嫩度排名,各取前後三名肌肉樣品進行蛋白質體分析。二維電泳分析結果顯示定量分析的355個蛋白質點中,有69個點在不同嫩度的樣品表現量具顯著差異。胜肽質量指紋分析(peptide mass fingerprinting)可成功鑑定其中66個點之身分,其分屬於40個不同蛋白質,此差異表現蛋白質主要位於細胞質(35%)與細胞骨架(13%),與蛋白質結合(23%)、及離子結合(18%)等分子功能有關,且參與代謝(23%)及生物調節(18%)等生物過程。16週齡雞隻股二頭肌之phosphoglucomutase-1、phosphoglycerate mutase 1、aconitate hydratase及triosephosphate isomerase在嫩度較高者表現量較高;20週齡雞隻股二頭肌之pyruvate kinase在嫩度較高者表現量較高,這些蛋白質皆與糖解代謝有關。不同週齡雞隻間之beta-enolase、desmin及skeletal myosin heavy chain在嫩度較高的組別表現量較高,這些蛋白質主要參與能量代謝與肌肉結構變化,故推測可能會影響屠宰後肌肉轉變為肉過程之變化。綜合本研究結果可推測台灣土雞股二頭肌嫩度可能與糖解代謝及肌肉結構相關之蛋白質有關。

Taiwan country chickens (TCCs) which have intense flavors and superior textures satisfy the preference of consumers, and play an important role in the poultry market. Tenderness is one of the most important meat characteristics for the consumers, thus affect the acceptability of products to the consumers. Most proteomic studies in meat science focus on the factors affecting the meat quality of cattles and pigs, whereas few studies concern about chicken meat quality. Therefore, the current study was to investigate the differential protein expressions in thigh (Biceps femoris) muscles of TCCs with different tenderness and to explore the candidate biomarkers for improving meat characteristics in chickens. The B. femoris muscles from male Livestock Research Institute line 11 (LRI L11) at 16- and 20-wk-age were applied. The tenderness of B. femoris muscles was determined by measuring the shear force, collagen content, and soluble collagen percentage and ranked by different formulas. The B. femoris muscles with superior and worst three tenderness respectively were subjected to further proteomic analysis. The results show that there were 69 protein spots expressed differentially among all the 355 quantified protein spots. A total of 66 differentially expressed protein spots were identified by peptide mass fingerprinting and belonged to the 40 different proteins. These differentially expressed proteins which mainly located in cytoplasm (35%) and cytoskeleton (13%), involved in the molecular functions of protein binding (23%) and ion binding (18%). Most of them were participated in the biological processes of metabolic process (23%) and biological regulation process (18%). Phosphoglucomutase-1, phosphoglycerate mutase 1, aconitate hydratase, and triosephosphate isomerase were significantly upregulated in B. femoris muscles with higher tenderness in 16-wk-old TCCs. Pyruvate kinase was significantly upregulated in B. femoris muscle with higher tenderness in 20-wk-old TCCs. These proteins were related to glycolysis. Beta-enolase, desmin, and skeletal myosin heavy chain, which participated in energy metabolism and muscle structure, were significantly upregulated in B. femoris muscles with higher tenderness in both 16- and 20-wk-old TCCs. In conclusion, results of this study suggested that the tenderness of B. femoris muscles of TCCs may be associated with the proteins which related to the glycolysis muscle structure.
Rights: 同意授權瀏覽/列印電子全文服務,2020-07-21起公開。
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