Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella)

Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella)
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草鱼(Ctenopharyngodon idella)皮肤中胃蛋白酶可溶性胶原蛋白的分离和部分表征

DOI:
10.1016/j.foodchem.2006.09.053
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发表时间:
2007-01-01
期刊:
影响因子:
8.8
通讯作者:
Wu, Xiaohua
Wu, Xiaohua
中科院分区:
农林科学1区
文献类型:
--
作者:
Zhang, Yan;Liu, Wentao;Wu, Xiaohua

文献摘要

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从草鱼(Ctenophyngodon Idella)的皮肤中提取胃溶胶原蛋白,得率为46.6%(干重)。电泳图谱表明,该胶原蛋白含有α1和α2链,与小牛皮胶原蛋白相似。草鱼皮胶原蛋白的亚氨基酸含量远低于哺乳动物胶原蛋白,其转变温度和变性温度分别仅为24.6℃和28.4℃。经胰酶和V8酶消化的胶原蛋白的肽谱显示与牛皮胶原蛋白和其他鱼皮胶原蛋白不同的多肽片段,表明氨基酸序列和胶原蛋白的构象不同。此外,冷冻干燥草鱼皮胶原蛋白海绵与小牛皮胶原蛋白海绵一样,具有均匀规则的网络结构。这些结果表明,草鱼皮具有作为胶原蛋白补充来源的潜力。(C)2006爱思唯尔有限公司。保留所有权利。
Pepsin-soluble collagen was extracted from the skin of grass carp (Ctenopharyngodon idella) with a yield of 46.6%, on a dry weight basis. Electrophoretic patterns showed that the collagen contained alpha 1 and alpha 2 chains, similar to those of calf skin collagen. The imino acid content of the collagen from grass carp skin was much lower than those of mammalian's collagens, as also were the transition temperature and denaturation temperature which were only 24.6 degrees C and 28.4 degrees C respectively. Peptide maps of the collagen digested by trypsin and V8 protease showed different peptide fragments from those of calf skin collagen and other fish skin collagens, suggesting differences in amino acid sequences and collagen conformation. In addition, the lyophilized collagen sponge from grass carp skin had a uniform and regular network structure, just like calf skin collagen sponge. These results suggest that grass carp skin has potential for use as a supplementary source of collagen. (c) 2006 Elsevier Ltd. All rights reserved.