Enhancing emulsification properties of pea protein isolate: Impact of heat treatment and soy hull polysaccharides on conformational modification and stability

IF 7.7 1区化学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

International Journal of Biological Macromolecules Pub Date : 2025-01-19 DOI:10.1016/j.ijbiomac.2025.140106

Xiuzhi Cao , Shengnan Wang , Yunfei Yu , Lu Han , He Liu

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Abstract

In order to investigate the effect of conformational change in pea protein isolate (PPI) on its emulsification properties, soy hull polysaccharides (SHP) were added to modify the conformation following heat treatment at 70–100 °C to improve emulsification. The results of UV and fluorescence spectroscopy indicated that the heat treatment exposed the amino acid residues to a more hydrophobic environment. The mean volume diameter (d_4,3) of PPI was reduced from 67.25 ± 3.31 to 45.50 ± 0.62 μm, and secondary structure of protein became more ordered. The addition of SHP enhanced the adsorption of protein at the oil-water interface and reduced the interfacial tension. Interestingly, SHP decreased the short-term (12h) thermal stability index (TSI) from 3.5 to 2.8 in PPI/SHP emulsion treated at 100 °C. These findings validated that heat treatment combined with SHP modification can improve the emulsification of PPI, which positively impacts the development of pea-based products for high temperatures applications.

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提高豌豆分离蛋白的乳化性能：热处理和大豆壳多糖对构象修饰和稳定性的影响。

为了研究豌豆分离蛋白（PPI）的构象变化对其乳化性能的影响，在70-100 ℃热处理后，加入大豆壳多糖（SHP）对其构象进行修饰，以改善其乳化效果。紫外光谱和荧光光谱结果表明，热处理使氨基酸残基暴露在更疏水的环境中。PPI的平均体积直径（d4,3）由67.25 ± 3.31 μm降至45.50 ± 0.62 μm，蛋白质二级结构更加有序。SHP的加入增强了蛋白质在油水界面的吸附，降低了界面张力。有趣的是，在100 °C下处理的PPI/SHP乳液中，SHP将短期（12h）热稳定性指数（TSI）从3.5降低到2.8。这些发现验证了热处理与SHP改性相结合可以改善PPI的乳化，这对高温应用的豌豆基产品的开发具有积极的影响。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

International Journal of Biological Macromolecules 生物-生化与分子生物学

CiteScore

13.70

自引率

9.80%

发文量

2728

审稿时长

64 days

期刊介绍： The International Journal of Biological Macromolecules is a well-established international journal dedicated to research on the chemical and biological aspects of natural macromolecules. Focusing on proteins, macromolecular carbohydrates, glycoproteins, proteoglycans, lignins, biological poly-acids, and nucleic acids, the journal presents the latest findings in molecular structure, properties, biological activities, interactions, modifications, and functional properties. Papers must offer new and novel insights, encompassing related model systems, structural conformational studies, theoretical developments, and analytical techniques. Each paper is required to primarily focus on at least one named biological macromolecule, reflected in the title, abstract, and text.