首页> 外文期刊>Food and Nutrition Sciences >Preparation and Characterisation of Collagen from Freshwater Fish Scales
【24h】

Preparation and Characterisation of Collagen from Freshwater Fish Scales

机译:淡水鱼鳞中胶原蛋白的制备与表征

获取原文
           

摘要

Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.
机译:从废淡水鲤鱼鱼鳞中制备酸溶性胶原蛋白(ASC)和胃蛋白酶溶解的胶原蛋白(PSC)。 SDS-PAGE结果表明,纯化的胶原蛋白由至少两条不同的链组成,这些链与具有(α1)2α2的α链组成的I型胶原蛋白一致。与鲤鱼的普通肌肉I型胶原蛋白,猪真皮的I型胶原蛋白和其他海水鱼胶原蛋白相比,淡水鲤鱼鳞片胶原蛋白的半胱氨酸(Cys-s)相对较高,但变性温度(Td)却比猪真皮低I型胶原蛋白。这些胶原通过UV-Vis光谱在230nm处具有明显的吸收。 X射线光谱分析表明,胶原蛋白保持单螺旋和三螺旋构型,重复间隔(d)的最小值约为4.48λ。和11.87?。因此,为了更有效地利用有限的资源,鲤鱼鳞可以作为提取I型胶原蛋白或明胶的潜在资源。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号