Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties.

Autor: Gligorijevic N; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia; Department of Chemistry, University of Belgrade - Institute of Chemistry, Technology and Metallurgy, National Institute of Republic of Serbia, Belgrade, Serbia., Lujic T; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia., Mutic T; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia., Vasovic T; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia., de Guzman MK; Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea; Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium., Acimovic J; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia., Stanic-Vucinic D; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia., Cirkovic Velickovic T; Center of Excellence for Molecular Food Sciences, Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia; Serbian Academy of Sciences and Arts, Belgrade, Serbia. Electronic address: tcirkov@chem.bg.ac.rs.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 May; Vol. 267 (Pt 2), pp. 131564. Date of Electronic Publication: 2024 Apr 16.
DOI: 10.1016/j.ijbiomac.2024.131564
Abstrakt: Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 °C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.
Competing Interests: Declaration of competing interest All authors confirm no conflict of interest for the publication.
(Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE