食品科学 ›› 2017, Vol. 38 ›› Issue (17): 42-46.doi: 10.7506/spkx1002-6630-201717008

• 基础研究 • 上一篇    下一篇

大豆蛋白肽-酪蛋白非磷酸肽组装产物的荧光光谱分析及抗氧化性研究

张 娜1,郭庆启2,黄文秀3,石彦国1,*   

  1. 1.哈尔滨商业大学食品工程学院,黑龙江省食品科学与工程重点实验室,黑龙江 哈尔滨 150076;2.东北林业大学林学院,黑龙江 哈尔滨 150040;3.山东禹王生态食业有限公司,山东 德州 251200
  • 出版日期:2017-09-15 发布日期:2017-09-12
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2016YFD0400400);黑龙江省博士后科研启动项目(LBH-Q15073);哈尔滨市科技局科技创新人才研究专项资金项目(2016RAQXJ146);中国食品科学技术学会食品科技基金项目(2016-002);国家自然科学基金青年科学基金项目(31301602);黑龙江省应用技术研究与开发计划项目(GC13B215;GA14B201)

Fluorescence Spectral Analysis and Antioxidant Effect of Soybean Ploypeptide-Casein Non-Phosphorylated Peptide Assembly

ZHANG Na1, GUO Qingqi2, HUANG Wenxiu3, SHI Yanguo1,*   

  1. 1. Key Laboratory of Food Science and Engineering of Heilongjiang Province, School of Food Engineering,Harbin University of Commerce, Harbin 150076, China; 2. School of Forestry, Northeast Forestry University,Harbin 150040, China; 3. Shandong Yuwang Ecological Food Industry Co. Ltd., Dezhou 251200, China
  • Online:2017-09-15 Published:2017-09-12

摘要: 对不同pH值条件下制备的大豆蛋白肽-酪蛋白非磷酸肽组装产物(casein non-phosphopeptides-soybean peptide complex,CNPSPC)的荧光光谱及抗氧化性进行分析。结果表明,随着pH值增加,CNPSPC埋藏在疏水环境中的Trp残基暴露到分子表面的强度逐渐低于组装前的原料蛋白,且Trp残基所处的微环境极性有所降低。硫磺素T荧光光谱分析表明,pH 6.0的制备条件下,CNPSPC荧光强度最大,此时CNPSPC的β-折叠结构含量可能最多。组装改变了CNPSPC的Trp残基在空间结构中所处的微环境,使CNPSPC的分子构象发生改变。与酪蛋白非磷酸肽(casein non-phosphopeptides,CNPP)和大豆蛋白肽(soybean peptide,SP)相比,CNPSPC的抗氧化能力有所提高,在pH 6.0时其清除1,1-二苯基-2-三硝基苯肼自由基、O2-·、·OH能力达到最大,分别提高到组装前大豆蛋白的3.34、1.12 倍和1.08 倍。

关键词: 大豆蛋白肽, 酪蛋白非磷酸肽, 组装, 荧光光谱, 抗氧化性

Abstract: The fluorescence spectra and antioxidant properties of casein non-phosphopeptides-soybean peptide complex (CNPSPC) prepared under different pH conditions were analyzed. The results showed that with the increase of pH, the content of surface-exposed Trp residues buried in hydrophobic environment in CNPSPC was became lower than in the raw protein, and the microenvironment polarity of Trp residues was decreased. The results of thioflavin T (ThT) fluorescence assay showed that the fluorescence intensity of CNPSPC was maximum at pH 6.0, which represented β-sheet was the dominant secondary structure of CNPSPC. The microenvironment of Trp residues was changed by the assembly, thereby changing the molecular conformation of CNPSPC. Compared with casein non-phosphopeptides (CNPP) and soybean peptide (SP), the antioxidant capacity of CNPSPC was improved. The scavenging activities of CNPSPC against 1,1-diphenyl-2-picrylhydrazyl (DPPH), superoxide anion and hydrolxyl radicals were maximum at pH 6.0, which increased by 3.34, 1.12 and 1.08 times compared to soybean protein respectively.

Key words: soybean polypeptide, casein non-phosphorylated peptide, assembly, fluorescence spectrum, antioxidant activity

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