【摘要】：對(duì)不同p H值條件下制備的大豆蛋白肽-酪蛋白非磷酸肽組裝產(chǎn)物(casein non-phosphopeptides-soybean peptide complex,CNPSPC)的熒光光譜及抗氧化性進(jìn)行分析。結(jié)果表明,隨著p H值增加,CNPSPC埋藏在疏水環(huán)境中的Trp殘基暴露到分子表面的強(qiáng)度逐漸低于組裝前的原料蛋白,且Trp殘基所處的微環(huán)境極性有所降低。硫磺素T熒光光譜分析表明,p H 6.0的制備條件下,CNPSPC熒光強(qiáng)度最大,此時(shí)CNPSPC的β-折疊結(jié)構(gòu)含量可能最多。組裝改變了CNPSPC的Trp殘基在空間結(jié)構(gòu)中所處的微環(huán)境,使CNPSPC的分子構(gòu)象發(fā)生改變。與酪蛋白非磷酸肽(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時(shí)其清除1,1-二苯基-2-三硝基苯肼自由基、O_2~-·、·OH能力達(dá)到最大,分別提高到組裝前大豆蛋白的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，

本文編號(hào)：2505557