Nonlinear rheological behavior and quantitative proteomic analysis of wheat aqueous phase protein at the air-water interface
文献类型: 外文期刊
作者: Zhaoshi Chen;Ge Wang;Runkang Qiu;Peiyao Zhao;Hongjie Ren;Aijun Hu;Bei Fan;Liya Liu;Fengzhong Wang
作者机构:
关键词: Foaming properties;Interfacial rheology;Non-starch polysaccharide;Prolamins;Wheat aqueous phase protein
期刊名称: Food Hydrocolloids
ISSN: 0268-005X
年卷期: 2025 年 168 卷
页码:
收录情况: SCIE(2025版) ; ; EI(2025版)
摘要: Air-water interface stabilization plays a pivotal role in foam formation and gas cell stabilization in fermented wheat-based products such as bread. However, the nonlinear interfacial rheological behavior of wheat aqueous phase proteins and its correlation with protein structure remains poorly understood. This study investigated the whole process of film formation and stabilization of wheat aqueous phase protein (WAP) and its ethanol fraction (ES) and non-ethanol fraction (NES) at the air-water interface. The physicochemical characteristics, interfacial adsorption behavior, and nonlinear interfacial rheology of each fraction were evaluated, and proteomic analysis was performed to uncover molecular mechanisms. The results showed that ES exhibited smaller particle size (412.63 ± 44.53 nm) and higher surface hydrophobicity (592.79 ± 32.81), enabling rapid adsorption at the air-water interface, which contributed to its superior foaming capacity (184.73 ± 12.34 %). In contrast, NES exhibited higher viscosity (1.81 ± 0.01 mPa s), which slowed down liquid drainage in the foam's Plateau region, contributing to enhanced foam stability. Interfacial dilatational rheology revealed that ES formed a stiff, solid-like interface, the ES foam with superior resistance to interfacial rupture. The proteomics analysis demonstrated that all sample shared the similar protein components, with prolamins (Gamma gliadin) playing a crucial role in ES foam formation and stabilization. This study provides new insights into the dynamic interfacial behavior of wheat proteins and their roles in foam stabilization, offering theoretical guidance for protein engineering in cereal-based aerated foods.
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