从日本和越南的海洋鱼类鳞片中分离和鉴定酸溶性胶原蛋白。
Isolation and characterization of acid-soluble collagen from the scales of marine fishes from Japan and Vietnam.
机构信息
Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Japan.
出版信息
Food Chem. 2014 Apr 15;149:264-70. doi: 10.1016/j.foodchem.2013.10.094. Epub 2013 Oct 30.
Acid-soluble collagen (ASC) was successfully extracted from the scales of lizard fish (Saurida spp.) and horse mackerel (Trachurus japonicus) from Japan and Vietnam and grey mullet (Mugil cephalis), flying fish (Cypselurus melanurus) and yellowback seabream (Dentex tumifrons) from Japan. ASC yields were about 0.43-1.5% (on a dry weight basis), depending on the species. The SDS-PAGE profile showed that the ASCs were type I collagens, and consisted of two different α chains, α1 and α2, as well as a β component. ASC of horse mackerel from Vietnam contained a higher imino acid level than that from Japan. ASC denaturation temperature (Td) ranged from 26 to 29 °C, depending on fish species and imino acid content (p<0.01). Maximal solubility of individual collagens was observed at pHs 1-3. Collagen solubility decreased sharply at NaCl concentrations >0.4M, regardless of fish type.
成功从来自日本的蜥蜴鱼（ Saurida 属）和马鲛鱼（ Trachurus japonicus ）以及来自日本的乌鱼（ Mugil cephalis ）、飞鱼（ Cypselurus melanurus ）和黄鳍鲷（ Dentex tumifrons ）的鳞片，以及来自越南的马鲛鱼中提取出酸溶性胶原蛋白（ ASC ）。 ASC 的得率约为 0.43-1.5%（干重基础），具体取决于物种。 SDS-PAGE 图谱显示， ASCs 为 I 型胶原蛋白，由两种不同的 α 链，即 α1 和 α2 以及 β 成分组成。来自越南的马鲛鱼 ASC 中的亚氨基酸水平高于来自日本的 ASC 。 ASC 的变性温度（ Td ）范围为 26 至 29°C，具体取决于鱼类物种和亚氨基酸含量（ p<0.01 ）。在 pH 值为 1-3 时，各胶原蛋白的最大溶解度。无论鱼类类型如何，在 NaCl 浓度>0.4M 时，胶原蛋白的溶解度都会急剧下降。
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