食品科学 ›› 2012, Vol. 33 ›› Issue (7): 37-40.doi: 10.7506/spkx1002-6630-201207008

• 基础研究 • 上一篇    下一篇

单环刺螠体壁胶原蛋白的提取及其理化性质

刘志娟,张朝辉*,赵 雪,李八方   

  1. 中国海洋大学食品科学与工程学院
  • 出版日期:2012-04-15 发布日期:2012-04-20
  • 基金资助:
    山东省科技攻关计划项目(2008GG10005008);国家自然科学基金项目(31071631)

Extraction and Physical and Chemical Properties of Collagen from Urechis unicinctus

LIU Zhi-juan,ZHANG Zhao-hui*,ZHAO Xue,LI Ba-fang   

  1. (College of Food Science and Technology, Ocean University of China, Qingdao 266003, China)
  • Online:2012-04-15 Published:2012-04-20

摘要: 采用0.5mol/L醋酸提取,结合NaCl沉淀法从单环刺螠(Urechis unicinctus)的体壁中提取酸溶性胶原蛋白(ASC),并对其理化性质作初步研究。紫外光谱分析表明ASC的特征吸收波长位于228nm,初步推断所提取的蛋白为典型的胶原蛋白;氨基酸组成分析表明ASC为典型的Ⅰ型胶原蛋白;聚丙烯酰胺凝胶电泳(SDS-PAGE)结果表明ASC有两条不同的α链(α1和α2链)、β链和γ链,其胶原蛋白中含有二硫键;傅里叶红外光谱(FTIR)分析表明其存在三螺旋结构;示差扫描量热仪(DSC)分析表明热变性温度(td)和热收缩温度(ts)分别为33.6℃和67.5℃。

关键词: 单环刺螠, 胶原蛋白, 提取, 理化性质

Abstract: Acid-soluble collagen (ASC) was prepared from the body wall of Urechis unicinctus through extraction with 0.5 mol/L acetic acid followed by precipitation with 0.9 mol/L NaCl and its physical and chemical properties were primarily studied. Ultraviolet spectral analysis showed that the characteristic absorption wavelength of ASC was 228 nm, suggesting that it is a typical collagen. Amino acid composition analysis indicated that ASC was a typical type Ⅰcollagen. SDS polyacrylamide gel electrophoresis (SDS-PAGE) suggested that ASC contained two alpha chains (α1 and α2), one β chain and oneγ chain. It also contained disulfide bonds. Fourier-transform infrared (FTIR) spectral analysis revealed the existence of helical arrangements in the collagen. The thermal denaturation temperature (td) and the thermal shrinkable temperature (ts) were 33.6 and 67.5 ℃, respectively.

Key words: Urechis unicinctus, collagen, extraction, characterization

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