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頁籤選單縮合
題名 | 不同離子強度的氯化鈉緩衝液抽出之吳郭魚、劍旗魚魚肉抽出液之乳化特性 |
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作者姓名(中文) | 陳榮輝; 陳建宏; 蔡震壽; | 書刊名 | 食品科學 |
卷期 | 21:5 1994.10[民83.10] |
頁次 | 頁396-406 |
分類號 | 411.38 |
關鍵詞 | 乳化特性; 魚肉抽出液; 離子強度; 吳郭魚; 劍旗魚; Emulsifying properties; Meat extracts; Ionic strength; Tilapia; Swordfish; |
語文 | 中文(Chinese) |
中文摘要 | 小同的離子強度(μ在0.1-2.0之間)的緩衝液抽出的吳郭魚或劍旗魚魚肉抽出物的抽出物的乳化活性不同,但與使用之魚種沒有差別,在μ為0.1時抽出的二種魚肉抽出物的乳化活性 EA 值均在為0.2。但在μ為0.3-2.0 時抽出的二種魚種抽出物的 EA 值均約在0.7-0.8。不同離子強度(μ為0.1-2.0)抽出的二種抽出物的乳化物安定性(ES)則不太受離子強度大小的影響(ES為0.7-0.8)。從參予與未參子乳化的蛋白質量的變化與蛋白質電泳分佈圖結果顯示,在低蛋白質濃度的抽出物中肌凝蛋白質(myosin)之乳化活性高於肌動蛋白質(actin)且高於水溶性蛋白質。分析乳化物加熱後的乳化物安定性及抽出物加熱前後相對琉水性的變化,發現水溶性蛋白質在受熱後,疏水基大量曝露,而提高其乳化物安定性。 |
英文摘要 | Extracts of tilapia or swordfish extracted with NaCI buffers of different ionic strength (between 0.1-2.0) showed differences in emulsifying activity (EA), but no difference between fish species. At an ionic strength (μ) of 0.1, EA values were small being about 0.2. As μ increased to 0.3-2.0, the EA values increased to 0.7-0.8. At a μ between 0.1 and 2.0 ES values were about 0.7-0.8 indicating that ES values were not affected by the changes of buffers' ionic strength in the range studied. The results of protein distribution in emulsion layer and unemulsified layer and the pattern of electrophoresis of original extracts and their corresponding residues after emulsifing measurement, showed that priorities of proteins in extracts participating in the interface were in the order of myoin>actin> sarcoplasmic proteins when the protein concentration in the extract was low. The ES values and surface hydrophobicities data obtained before and after heat treatment showed that after heating, water soluble proteins were the proteins that contributed to the increase in ES value due to exposure of more hydrophobic groups. |
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