Atomic force microscopy nanoscale analysis: Impact of storage conditions on surface properties of whey protein powders

Gaïani, Claire; Omar, Rana; El-Kirat-Chatel, Sofiane; Cvetkovska, Loubiana; Alexander, Marcela; Ray, Colin; Burgain, Jennifer; Francius, Grégory

doi:10.1016/j.foodhyd.2021.106801

Cited by 8 publications

References 39 publications

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pH‐induced changes in IgE molecules measured by atomic force microscopy

Hu,

Wang,

Jiang

et al. 2024

Microscopy Res & Technique

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The environment surrounding proteins is tightly linked to its dynamics, which can significantly influence the conformation of proteins. This study focused on the effect of pH conditions on the ultrastructure of Immunoglobulin E (IgE) molecules. Herein, the morphology, height, and area of IgE molecules incubated at different pH were imaged by atomic force microscopy (AFM), and the law of IgE changes induced by pH value was explored. The experiment results indicated that the morphology, height and area of IgE molecules are pH dependent and highly sensitive. In particular, IgE molecules were more likely to present small‐sized ellipsoids under acidic conditions, while IgE molecules tend to aggregate into large‐sized flower‐like structures under alkaline conditions. In addition, it was found that the height of IgE first decreased and then increased with the increase of pH, while the area of IgE increased with the increase of pH. This work provides valuable information for further study of IgE, and the methodological approach used in this study is expected to developed into AFM to investigate the changes of IgE molecules mediated by other physical and chemical factors.Research Highlights The ultrastructure of IgE molecules is pH dependent and highly sensitive. IgE molecules were tend to present small‐sized ellipsoids under acidic pH. Alkaline pH drives IgE self‐assembly into flower‐like aggregates.

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