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
发布时间：2019-06-25 08:49
【摘要】：对不同p H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p H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,p H 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p H 6.0时其清除1,1-二苯基-2-三硝基苯肼自由基、O_2~-·、·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。
[Abstract]:The fluorescence spectra and antioxidant properties of soybean protein peptide casein non-phosphate peptide (casein non-phosphopeptides-soybean peptide complex,CNPSPC) prepared under different pH values were analyzed. The results showed that with the increase of pH value, the intensity of CNPSPC residues buried in hydrophobic environment exposed to the molecular surface was gradually lower than that of raw protein before assembly, and the polarity of Trp residues in the microenvironment decreased. The fluorescence spectrum analysis of thiosulfon T showed that the fluorescence intensity of CNPSPC was the highest under the preparation of, p H 6.0, and the content of 尾-fold structure of CNPSPC might be the highest. The assembly changes the microenvironment of the Trp residues of CNPSPC in the spatial structure, and changes the molecular conformational of CNPSPC. Compared with casein non-phosphate peptide (casein non-phosphopeptides,CNPP) and soybean protein peptide (soybean peptide,SP), the antioxidant capacity of CNPSPC was improved. At pH 6.0, the scavenging capacity of 1-diphenyl-2-trinitrophenylhydrazide radical, O 鈮，
本文编号：2505557
[Abstract]:The fluorescence spectra and antioxidant properties of soybean protein peptide casein non-phosphate peptide (casein non-phosphopeptides-soybean peptide complex,CNPSPC) prepared under different pH values were analyzed. The results showed that with the increase of pH value, the intensity of CNPSPC residues buried in hydrophobic environment exposed to the molecular surface was gradually lower than that of raw protein before assembly, and the polarity of Trp residues in the microenvironment decreased. The fluorescence spectrum analysis of thiosulfon T showed that the fluorescence intensity of CNPSPC was the highest under the preparation of, p H 6.0, and the content of 尾-fold structure of CNPSPC might be the highest. The assembly changes the microenvironment of the Trp residues of CNPSPC in the spatial structure, and changes the molecular conformational of CNPSPC. Compared with casein non-phosphate peptide (casein non-phosphopeptides,CNPP) and soybean protein peptide (soybean peptide,SP), the antioxidant capacity of CNPSPC was improved. At pH 6.0, the scavenging capacity of 1-diphenyl-2-trinitrophenylhydrazide radical, O 鈮，
本文编号：2505557
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