食品科学 ›› 2018, Vol. 39 ›› Issue (1): 36-41.doi: 10.7506/spkx1002-6630-201801005

• 基础研究 • 上一篇    下一篇

尖吻鲈鱼鳞和鱼皮胶原蛋白的提取及其理化特性分析

廖 伟,夏光华,李 川,仇昶旭,李永成,申铉日*   

  1. 海南大学食品学院,海南 海口 570228
  • 出版日期:2018-01-15 发布日期:2018-01-05
  • 基金资助:
    国家自然科学基金地区科学基金项目(31260376)

Extraction and Characterization of Collagen from Scales and Skin of Asian Seabass

LIAO Wei, XIA Guanghua, LI Chuan, QIU Changxu, LI Yongcheng, SHEN Xuanri*   

  1. College of Food Science and Technology, Hainan University, Haikou 570228, China
  • Online:2018-01-15 Published:2018-01-05

摘要: 以尖吻鲈鱼鳞和鱼皮为原料,提取并分离纯化酶溶性胶原蛋白,通过十二烷基硫酸钠-聚丙烯酰胺凝胶 电泳(sodium dodecyl sulfate-polyacrylamide gel electropheresis,SDS-PAGE)、氨基酸组成分析、差示扫描量热 (differential scanning calorimetry,DSC)、傅里叶变换红外光谱、X射线衍射和Zeta电位以及溶解度研究,分析 和比较了其主要理化性质。冷冻干燥后鱼鳞和鱼皮胶原蛋白得率(干质量)分别为2.3 g/100 g和47.3 g/100 g; SDS-PAGE结果显示两种胶原蛋白构型均为[α1(Ⅰ)]2α2(Ⅰ),初步判断属于Ⅰ型胶原蛋白;DSC结果显示鱼鳞和鱼 皮胶原蛋白热变性温度(Td)分别为37.54 ℃和36.74 ℃;傅里叶变换红外光谱和X射线衍射结果显示胶原蛋白经 胃蛋白酶处理后仍能保持其完整的三股螺旋结构;Zeta电位结果显示鱼鳞和鱼皮胶原蛋白等电点分别为pH 6.40和 pH 6.64;溶解度研究结果显示两种胶原蛋白在酸性条件和低NaCl质量浓度下均表现出良好的溶解性。

关键词: 尖吻鲈, 鱼鳞, 鱼皮, 胶原蛋白, 氨基酸

Abstract: Pepsin-soluble collagen was extracted from the scales and skin of Asian seabass, and their physicochemical properties were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), amino acid composition analysis, differential scanning calorimetry (DSC), Fourier transform infrared (FT-IR) spectroscopy, X-ray diffraction, zeta potential and solubility measurement. The yields of scale collagen and skin collagen were 2.3 and 47.3 g/100 g (dry weight), respectively. The SDS-PAGE profile showed that both collagens contained [α1(I)]2α2(I) and were characterized as type I collagen. DSC indicated that denaturation temperatures (Td) of scale and skin collagen were 37.54 and 36.74 ℃, respectively. Based on FT-IR spectra and X-ray diffraction spectra, after pepsin treatment, the triple-helical structure of the collagens was still intact. Zeta potential studies indicated that scale and skin collagen had a net charge of zero at pH 6.40 and 6.64, respectively. Both collagens exhibited high solubility under acidic and low salt concentration conditions.

Key words: Asian seabass, scale, skin, collagen, amino acid

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