食品科学 ›› 2021, Vol. 42 ›› Issue (4): 87-93.doi: 10.7506/spkx1002-6630-20191212-138

• 食品化学 • 上一篇    下一篇

鳕鱼皮明胶肽硒复合物的制备及结构表征

吴佳南,孙娜,林松毅,吴汶飞   

  1. (1.大连工业大学食品学院,辽宁?大连 116034;2.国家海洋食品工程技术研究中心,辽宁?大连 116034)
  • 出版日期:2021-02-25 发布日期:2021-02-25
  • 基金资助:
    辽宁省博士科研启动基金计划项目(2019-BS-017)

Preparation and Structural Characterization of Peptide-Selenium Complex from Hoki (Macruronus novaezelandiae) Skin Gelatin

WU Jianan, SUN Na, LIN Songyi, WU Wenfei   

  1. (1. School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China; 2. National Engineering Research Center of Seafood, Dalian 116034, China)
  • Online:2021-02-25 Published:2021-02-25

摘要: 以新西兰鳕鱼皮为原料,提取鳕鱼皮明胶并酶解获得鳕鱼皮明胶肽,以亚硒酸钠为硒源,制备并筛选出硒结合量较高的肽硒复合物,对其进行结构表征。结果显示,鳕鱼皮明胶胃蛋白酶酶解物的硒结合含量最高(13.61 μg/mg),因此将其用于制备鳕鱼皮明胶肽硒复合物;鳕鱼皮明胶肽与硒结合后,紫外光谱吸收峰强度增大且红移,荧光光谱吸收峰由波长311 nm迁移到355 nm且荧光强度减弱,表明鳕鱼皮明胶肽与硒结合产生新的物质;基于粒径分布、原子力显微镜、扫描电子显微镜、X射线衍射分析,鳕鱼皮明胶肽硒复合物呈现为纳米晶体结构,主要是由于鳕鱼皮明胶肽上的羧基和氨基与硒发生了结合反应,使得β-折叠结构转变为α-螺旋结构和β-转角结构,从而使得结构更加紧凑有序。本研究制备了一种新型的肽硒复合物,为实现鱼皮高值化利用提供了新途径。

关键词: 鳕鱼皮;明胶肽;硒;肽硒复合物;结构表征

Abstract: In this study, gelatin was extracted from the skin of New Zealand hoki (Macruronus novaezelandiae), and was further hydrolyzed enzymatically to produce peptides. Peptide-selenium complexes were prepared by using sodium selenite as a selenium source and the one with high selenium-binding capacity was selected and structurally characterized. The results indicated that the pepsin hydrolysate had the highest calcium binding capacity (13.61 μg/mg) and was thus used to peptide-selenium complexes. After selenium binding, the UV absorption intensity of the peptides increased, accompanied by a red shift in the maximum wavelength, and the fluorescence absorption peak shifted from 311 to 355 nm together with a weakening of the fluorescence intensity. These phenomena indicated the production of a new complex from selenium binding to the peptides. Based on particle size distribution measurement, atomic force microscopy (AFM), scanning electron microscopy (SEM), and X-ray diffraction analysis, the peptide-selenium complex had a nanocrystalline structure. The binding reaction of carboxyl and amino groups in the peptides with selenium transformed the secondary protein from β-sheet to α-helix and β-turn, thereby making the structure more compact and orderly. This study provides a new approach for high-value utilization of fish skin.

Key words: hoki skin; gelatin polypeptide; selenium; peptide-selenium complex; structural characterization

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