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豌豆分离蛋白-磷脂混合吸附层的定量分析及界面性质

Quantitative analysis and interfacial properties of mixed pea protein isolate-phospholipid adsorption layer.

机构信息

College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.

Key Laboratory of Fermentation Engineering (Ministry of Education), College of Bioengineering, Hubei University of Technology, Wuhan 430068, China.

出版信息

Int J Biol Macromol. 2023 Mar 31;232:123487. doi: 10.1016/j.ijbiomac.2023.123487. Epub 2023 Feb 1.

DOI:10.1016/j.ijbiomac.2023.123487
PMID:36736980
Abstract

Proteins and low-molecular-weight (LMW) surfactants are widely used for the physical stabilization of many emulsion-based food products. This study investigated the oil-water interfacial behavior between pea protein isolate (PPI) and phospholipid (PL). The emulsions prepared with different concentrations of PPI and PL were stabilized by their synergetic or competitive adsorption at the oil-water interface. In addition, the quantitative proteomics results could illustrate the displacements of proteins by PL. The result showed that the vicilin (7S) could be preferentially displaced by PL. Meanwhile, the results of quartz crystal microbalance with dissipation (QCM-D) indicated the high affinity of legumin (11S) with PL, suggesting that the legumin possessed higher interfacial affinity to prevent interfacial displacement. This research could help us to understand the interaction and competitive adsorption between plant proteins and LMW surfactants profoundly, which could promote the development of plant protein-based emulsion beverage with improved stability.

摘要

蛋白质和低分子量(LMW)表面活性剂广泛用于许多基于乳液的食品的物理稳定性。本研究调查了豌豆分离蛋白(PPI)和磷脂(PL)之间的油水界面行为。通过在油水界面处协同或竞争吸附,用不同浓度的 PPI 和 PL 制备的乳液得到稳定。此外,定量蛋白质组学结果可以说明 PL 对蛋白质的取代。结果表明,菜豆球蛋白(7S)可以优先被 PL 取代。同时,石英晶体微天平耗散(QCM-D)的结果表明,legumin(11S)与 PL 具有高亲和力,表明 legumin 具有更高的界面亲和力以防止界面取代。这项研究可以帮助我们深入了解植物蛋白和 LMW 表面活性剂之间的相互作用和竞争吸附,这可以促进具有改善稳定性的基于植物蛋白的乳液饮料的开发。

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