为改善蛋白起泡性能,该文以蛋清-大豆分离蛋白复合蛋白为原料,探究了不同菊粉添加量对复合蛋白起泡性能的影响。并对蛋清-大豆分离蛋白-菊粉复合物的粒径分布及ζ-电位、十二烷基硫酸钠-聚丙烯酰氨凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis, SDS-PAGE)、红外光谱、表面疏水性及游离巯基含量进行了分析,对菊粉与复合蛋白结合机理进行了初步探究。结果表明,与空白组相比,添加0.8%的菊粉时,复合蛋白起泡性提高了24.23%,泡沫稳定性提高了25.71%。菊粉改变了复合蛋白的聚集状态,结构变得松散,电位绝对值降低,游离巯基暴露出来。菊粉与之生成结构更加紧凑的小分子复合物,粒径减小。复合物β-折叠含量减少,蛋白质分子发生去折叠,菊粉通过氢键与复合蛋白分子发生非共价相互作用,导致亲水基团增加,表面疏水性下降,分子间相互作用有助于泡沫膜的形成,进而改善了起泡性能。因此,菊粉能够有效改善蛋清-大豆分离蛋白复合蛋白的起泡性能。
Aiming to improve the foaming properties of protein, this study explored the effect of different amounts of inulin on foaming performance of egg white-soy protein isolate compound protein.The study analyzed the particle size distribution, ζ-potential, SDS-PAGE gel electrophoresis, infrared spectroscopy, surface hydrophobicity, and free sulfhydryl content of the egg white-soy protein isolate-inulin complexes, and conducted a preliminary exploration of the binding mechanism of the complexes.The results indicate that compared to the blank group, when 0.8% inulin was added, the foaming characteristics increased by 24.23%, and the foam stability improved by 25.71%.The reason is that inulin causing a change in the aggregation state of the composite protein, making the structure more loose, while the absolute value of the potential decreases and the free sulfhydryl groups are also exposed.Inulin combines with the compound protein to form a small molecular complex with a more compact structure, resulting in a reduction in particle size.Furthermore, there is a decrease in the β-folding content of the complexes, indicating that the protein molecules are unfolding.Inulin interacts with the compound protein molecules through non-covalent hydrogen bonds which is used to, which increases the number of hydrophilic groups in the environment and decreases surface hydrophobicity.These intermolecular interactions contribute to the formation of foam membranes, thereby improving foaming performance.Therefore, inulin can effectively improve the foaming performance of egg white-soy protein isolate compound protein.
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