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Enhancing Functional Properties and Protein Structure of Almond Protein Isolate Using High-Power Ultrasound Treatment

文献类型： 外文期刊

作者： Tian, Li 1 ; You, Xinyong 1 ; Zhang, Shulin 1 ; Zhu, Zhenbao 3 ; Yi, Jianhua 3 ; Jin, Gang 4 ;

作者机构： 1.Anyang Inst Technol, Coll Biol & Food Engn, Anyang 455000, Peoples R China

2.Henan Inst Sci & Technol, Coll Hort & Landscape Architecture, Xinxiang 453003, Peoples R China

3.Shaanxi Univ Sci & Technol, Sch Food & Biol Engn, Xian 710021, Peoples R China

4.Guangxi Subtrop Crops Res Inst, Guangxi Key Lab Qual & Safety Control Subtrop Frui, Nanning 530001, Peoples R China

关键词： high-power ultrasound; almond protein isolate; physicochemical protein properties; protein functional properties

期刊名称：MOLECULES （ 影响因子：4.2； 五年影响因子：4.6 ）

ISSN：

年卷期： 2024 年 29 卷 15 期

页码：

收录情况： SCI

摘要： The suitability of a given protein for use in food products depends heavily on characteristics such as foaming capacity, emulsifiability, and solubility, all of which are affected by the protein structure. Notably, protein structure, and thus characteristics related to food applications, can be altered by treatment with high-power ultrasound (HUS). Almonds are a promising source of high-quality vegetable protein for food products, but their physicochemical and functional properties remain largely unexplored, limiting their current applications in foods. Here, we tested the use of HUS on almond protein isolate (API) to determine the effects of this treatment on API functional properties. Aqueous almond protein suspensions were sonicated at varying power levels (200, 400, or 600 W) for two durations (15 or 30 min). The molecular structure, protein microstructure, solubility, and emulsifying and foaming properties of the resulting samples were then measured. The results showed that HUS treatment did not break API covalent bonds, but there were notable changes in the secondary protein structure composition, with the treated proteins showing a decrease in alpha-helices and beta-turns, and an increase in random coil structures as the result of protein unfolding. HUS treatment also increased the number of surface free sulfhydryl groups and decreased the intrinsic fluorescence intensity, indicating that the treatment also led to alterations in the tertiary protein structures. The particle size in aqueous suspensions was decreased in treated samples, indicating that HUS caused the dissociation of API aggregates. Finally, treated samples showed increased water solubility, emulsifying activity, emulsifying stability, foaming capacity, and foaming stability. This study demonstrated that HUS altered key physicochemical characteristics of API, improving critical functional properties including solubility and foaming and emulsifying capacities. This study also validated HUS as a safe and environmentally responsible tool for enhancing desirable functional characteristics of almond proteins, promoting their use in the food industry as a high-quality plant-based protein.

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