Atomic force microscopy nanoscale analysis: Impact of storage conditions on surface properties of whey protein powders
| Autor: | Sofiane El-Kirat-Chatel, Colin Ray, Claire Gaiani, Rana Omar, Marcela Alexander, Grégory Francius, Loubiana Cvetkovska, Jennifer Burgain |
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| Přispěvatelé: | Laboratoire d'Ingénierie des Biomolécules (LIBio), Université de Lorraine (UL), Institut Universitaire de France (IUF), Ministère de l'Education nationale, de l’Enseignement supérieur et de la Recherche (M.E.N.E.S.R.), Laboratoire de Chimie Physique et Microbiologie pour les Matériaux et l'Environnement (LCPME), Institut de Chimie du CNRS (INC)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Arla Foods Ingredients, IMPACT Biomolécules, ANR-15-IDEX-0004,LUE,Isite LUE(2015) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Surface (mathematics)
Whey protein Materials science 010304 chemical physics General Chemical Engineering [SDV]Life Sciences [q-bio] Force spectroscopy 04 agricultural and veterinary sciences General Chemistry Nanoindentation 040401 food science 01 natural sciences chemistry.chemical_compound 0404 agricultural biotechnology chemistry Chemical engineering 0103 physical sciences Particle Denaturation (biochemistry) Lactose Nanoscopic scale ComputingMilieux_MISCELLANEOUS Food Science |
| Zdroj: | Food Hydrocolloids Food Hydrocolloids, Elsevier, 2021, 118, pp.106801. ⟨10.1016/j.foodhyd.2021.106801⟩ |
| ISSN: | 0268-005X 1873-7137 |
| DOI: | 10.1016/j.foodhyd.2021.106801⟩ |
| Popis: | Dairy powders are usually subjected to environmental variations during storage and/or shipment that strongly impact their chemical, nutritional and structural features. Nevertheless, these modifications are rarely investigated at the particle surface level, which represents the interface in contact with air, water, materials or other powders and directly influences powder functionalities. In this paper, atomic force microscopy (AFM) is used in imaging, nanoindentation and force spectroscopy modes to investigate the evolution of the surface properties such as the hydrophobicity and stiffness of whey protein powders at the nanoscale after controlled storage conditions. Our results evidenced that surface modifications are more enhanced by high storage temperature than storage time (for the same storage energy) and correspond to an increase of both surface hydrophobicity and heterogeneity. The strong impact of residual lactose in the powder (around 1.5% lactose) is also highlighted on these phenomena by performing surface comparisons with a reference powder (β-lactoglobulin) without lactose. This reference powder permitted the discrimination between surface protein denaturation and surface lactosylation. |
| Databáze: | OpenAIRE |
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