研究报告

三文鱼(Salmo salar)鱼皮胶原的制备及表征

  • 叶童 ,
  • 何建林 ,
  • 李玉霜 ,
  • 张兴坤 ,
  • 郜希媛 ,
  • 陈俊德
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  • 1(上海海洋大学 食品学院,上海,200120)
    2(自然资源部第三海洋研究所,自然资源部海洋生物资源开发利用工程技术创新中心,福建 厦门,361001)
硕士研究生(陈俊德研究员为通信作者,E-mail:jdchen@tio.org.cn)

收稿日期: 2021-12-24

  修回日期: 2022-02-18

  网络出版日期: 2023-04-14

基金资助

国家自然科学基金(42076120);国家自然科学基金(41676129)

Preparation and characterization of salmon (Salmo salar) skin collagen

  • YE Tong ,
  • HE Jianlin ,
  • LI Yushuang ,
  • ZHANG Xingkun ,
  • GAO Xiyuan ,
  • CHEN Junde
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  • 1(College of Food Science, Shanghai Ocean University, Shanghai 200120, China)
    2(Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361001, China)

Received date: 2021-12-24

  Revised date: 2022-02-18

  Online published: 2023-04-14

摘要

该研究以三文鱼(Salmo salar)加工副产物鱼皮为原料开发了一种海洋源胶原。利用酸法提取,盐析透析纯化制备胶原,通过SDS-PAGE和光谱鉴定其结构,在此基础上分析其理化性质、流变特性、功能特性以及细胞相容性。结果表明,三文鱼鱼皮胶原为典型 Ⅰ 型胶原,且保留了完整的三螺旋结构。鱼皮胶原热变性温度为22.3 ℃;鱼皮胶原乳化性为65.91~755.97 m2/g,高于牛皮胶原(28.4~56.2 m2/g)和鲵肌浆蛋白(0.6 ~3.38 m2/g);乳化稳定性为3.50 min,高于蒙古牛骨胶原(0.8 min)和军曹鱼鱼皮胶原(0.2 min),可作为乳化剂用于面包生产;起泡性为16.56%~77.79%,高于酪蛋白(3.95%~10.15%)和米糠浓缩蛋白(5.2%~10.03%);泡沫稳定性(13%)高于大鲵肌浆蛋白(5%)和牛皮胶原(10%),可用于啤酒、乳制品生产。MC3T3-E1细胞在0.4 mg/mL的胶原溶液中相对增殖率为111.6%,优于罗非鱼鱼皮胶原。研究表明,三文鱼鱼皮胶原具有替代市场主流胶原产品的开发潜力。

本文引用格式

叶童 , 何建林 , 李玉霜 , 张兴坤 , 郜希媛 , 陈俊德 . 三文鱼(Salmo salar)鱼皮胶原的制备及表征[J]. 食品与发酵工业, 2023 , 49(6) : 71 -78 . DOI: 10.13995/j.cnki.11-1802/ts.030497

Abstract

This study aimed to develop a kind of marine-origin collagen from fish skin, which was a by-product of salmon (Salmo salar) processing. The collagen was prepared by acid extraction and purified by salting out and dialysis. Its structure was identified by SDS-PAGE and spectroscopy, based on the physical and chemical properties, rheological properties, functional properties, and cytocompatibility of the collagen were analyzed. The experimental results showed that the salmon fish skin collagen was a typical type I collagen and retained an intact triple helix structure. The thermal denaturation temperature of fish skin collagen was 22.3 ℃, and the emulsification of fish skin collagen (65.91-755.97 m2/g) was higher than that of bovine collagen (28.4-56.2 m2/g) and salamander myosin (0.6-3.38 m2/g), and the emulsification stability (3.50 min) was higher than that of Mongolian bovine collagen (0.8 min) and cobia fish skin collagen (0.2 min), which could be used as an emulsifier for bread production. The foaming property (16.56%-77.79%) was higher than casein (3.95%-10.15%) and rice bran protein concentrate (5.2%-10.03%), and the foam stability(13%) was higher than salamander muscle plasma protein (5%) and bovine hide collagen (10%), which could be used for beer and dairy products production. The relative proliferation rate of MC3T3-E1 cells in 0.4 mg/mL collagen solution was 111.6%, which was better than tilapia skin collagen. Therefore, salmon skin collagen has the development potential to replace the mainstream collagen products in the market.

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