孟瑞龙, 章绍兵. 酸性pH偏移协同超声处理对花生蛋白结构与功能性质的影响[J]. 河南工业大学学报自然科学版, 2024, 45(4): 11-18. DOI: 10.16433/j.1673-2383.202402260003
    引用本文: 孟瑞龙, 章绍兵. 酸性pH偏移协同超声处理对花生蛋白结构与功能性质的影响[J]. 河南工业大学学报自然科学版, 2024, 45(4): 11-18. DOI: 10.16433/j.1673-2383.202402260003
    MENG Ruilong, ZHANG Shaobing. Effect of acidic pH-shifting combined with sonication on the structural and functional properties of peanut protein[J]. Journal of Henan University of Technology(Natural Science Edition), 2024, 45(4): 11-18. DOI: 10.16433/j.1673-2383.202402260003
    Citation: MENG Ruilong, ZHANG Shaobing. Effect of acidic pH-shifting combined with sonication on the structural and functional properties of peanut protein[J]. Journal of Henan University of Technology(Natural Science Edition), 2024, 45(4): 11-18. DOI: 10.16433/j.1673-2383.202402260003

    酸性pH偏移协同超声处理对花生蛋白结构与功能性质的影响

    Effect of acidic pH-shifting combined with sonication on the structural and functional properties of peanut protein

    • 摘要: 为进一步改善花生蛋白功能特性,以水剂法提取的花生蛋白为研究对象,考察了pH 1.5和 2.5偏移或结合超声处理对花生蛋白结构与功能性质的影响。结果表明:与未处理蛋白相比,经不同方式处理后花生蛋白的亚基发生了一定程度的降解,粒径、绝对电位降低,而表面疏水性显著增加;与单独pH偏移处理相比,复合改性使蛋白的结构更加伸展;不同方式处理后的花生蛋白降低油水界面张力的能力增强,乳化活性和稳定性均增加,其中pH 1.5偏移结合超声处理使花生蛋白的乳化稳定性增加了2倍;pH 1.5偏移处理后的蛋白具有最高的弹性模量,可能与其暴露游离巯基含量最高以及绝对电位最低的结构性质有关。pH 1.5偏移或结合超声处理能够显著改善花生蛋白的功能性质。

       

      Abstract: In order to further improve the functional properties of peanut proteins, this paper investigated the effects of pH-shifting at pH 1.5 and pH 2.5 individually or combined with ultrasonic treatment on the structural and functional properties of peanut proteins extracted by aqueous method. The results showed that compared with untreated proteins, the subunits of peanut proteins were degraded to a certain extent after treatment in different ways, and the particle size, absolute potential were decreased, while the surface hydrophobicity was increased significantly. The complex modification resulted in a more stretched structure of the protein compared to the pH-shifting treatment alone. The ability of peanut proteins to reduce the interfacial tension between oil and water was enhanced by different treatments, and both emulsifying activity and stability were increased. The pH-shifting at pH 1.5 combined with sonication increased the emulsifying stability of peanut proteins by a factor of 2. The proteins of pH-shifting at pH 1.5 possessed the highest modulus of elasticity (G'), which may be related to their structural properties of exposing the highest free sulfhydryl content and the lowest absolute potential. The pH-shifting at pH 1.5 or combined with sonication significantly improved the functional properties of peanut proteins.

       

    /

    返回文章
    返回