食品科学 ›› 2017, Vol. 38 ›› Issue (19): 100-106.doi: 10.7506/spkx1002-6630-201719017

• 基础研究 • 上一篇    下一篇

乙酸溶胀-挤压提取对罗非鱼真皮胶原蛋白理化性质的影响

鲍虹蕾1,杨 敏1,刘文文1,何沁峰1,崔改泵2,陈 伟3,胡建恩1,武 龙1,*   

  1. 1.大连海洋大学食品科学与工程学院,辽宁 大连 116023;2.中国农业科学技术出版社,北京 100081; 3.中国科学院大连化学物理研究所,辽宁 大连 116023
  • 出版日期:2017-10-15 发布日期:2017-09-29
  • 基金资助:
    国家海洋局海洋公益性行业科研专项(201505030-3);辽宁省大学生创新创业训练计划项目(201510158000006)

Physical and Chemical Properties of Tilapia (Oreochromis niloticus) Dermis Collagen Acetic Acid Swelling and Extrusion

BAO Honglei1, YANG Min1, LIU Wenwen1, HE Qinfeng1, CUI Gaibeng 2, CHEN Wei 3, HU Jianen1, WU Long1,*   

  1. 1. College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, China; 2. China Agricultural Science and Technology Press, Beijing 100081, China; 3. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
  • Online:2017-10-15 Published:2017-09-29

摘要: 以磷酸预处理辅助实现罗非鱼皮真皮与表皮的分离,采用低温乙酸溶胀法提取真皮中的胶原蛋白,并对所 得胶原蛋白样品进行理化性质分析。结果表明,在4 ℃环境中,以0.006 mol/L磷酸、50 g/L料液处理鱼皮3 h,可获 得最佳真皮、表皮分离效果。所得真皮在4 ℃环境中,以0.035 mol/L乙酸溶液(料液质量浓度为100 g/L)溶胀处理 6 h,挤压后可得羟脯氨酸质量分数为7.9%的真皮胶原蛋白样品,提取得率达27.6%(干基)。凝胶电泳结果分析表 明,所得样品主要含有α1、α2和β链,由紫外光谱分析结果可知其最大吸收在230 nm波长附近,符合典型Ⅰ型胶原 蛋白特征;衰减全反射傅里叶变换红外光谱分析结果显示其三螺旋结构得到较好地保留。样品热变性温度及热收缩 温度分别为29.2 ℃和55.0 ℃。研究结果为鱼皮资源的高效开发利用以及高品质胶原蛋白的制备提供了理论参考。

关键词: 罗非鱼皮, 真皮, 表皮, 溶胀, 提取

Abstract: Tilapia skin was pretreated with 0.006 mol/L phosphoric acid at a solid to liquid ratio of 50 g/L for 3 h at 4 ℃ to facilitate the separation of dermis and epidermis. The dermis was treated with 0.035 mol/L acetic acid at a solid to liquid ratio of 100 (g/L) for 6 h at 4 ℃ to fully swell it, washed and extruded to obtain collagen. The results showed that tilapia dermis collagen contained 7.9% of hydroxyproline, and the collagen yield was as high as 27.6% (on a dry basis). The collagen mainly consisted of α1, α2 and β polypeptide chains according to sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis, with maximum UV absorbance at 230 nm, complying with the characteristics of type Ⅰ collagen. The attenuated total reflectance Fourier transform infrared (ATR FT-IR) spectrum proved the presence of the triple-helix structure of collagen. The thermal denaturation temperature and shrinkage temperature of the collagen were 29.2 ℃ and 55.0 ℃, respectively. The study provides an alternative approach to the extraction of high-quality collagen and consequently efficient utilization of fish processing byproducts.

Key words: tilapia skin, dermis, epidermis, swelling, extraction

中图分类号: