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Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
Nikola Gligorijevic1, Tamara Lujic2, Tamara Mutic2
1Center 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.
International Journal of Biological Macromolecules
|April 13, 2024
Summary
Microplastics in food bind to ovalbumin, a key egg protein, altering its structure and properties. This interaction affects protein stability and behavior, with implications for food safety and digestion.
Area of Science:
- Food Science and Technology
- Environmental Science
- Biochemistry
Background:
- Microplastics (MPs) are emerging food contaminants.
- MPs can interact with food matrices and proteins during digestion.
- Ovalbumin is a major protein in chicken egg white.
Purpose of the Study:
- To investigate the adsorption of ovalbumin onto polystyrene (PS) and polyethylene terephthalate (PET) microplastics.
- To determine how microplastic properties (size, type) and environmental conditions (pH) affect ovalbumin adsorption.
- To analyze the structural and functional alterations of ovalbumin upon adsorption to microplastics.
Main Methods:
- Studied ovalbumin adsorption to PS and PET microplastics of varying sizes (110-260 μm).
- Investigated adsorption under acidic (pH 3) and neutral (pH 7) conditions.
- Analyzed changes in ovalbumin secondary and tertiary structures using spectroscopic methods.
- Characterized the protein corona (soft and hard) formed around microplastics.
Main Results:
- Ovalbumin adsorption was higher for smaller MPs, PS > PET, and at pH 3 > pH 7.
- Microplastics induced changes in ovalbumin's tertiary structure (loosening at pH 3, tightening at pH 7) but not significantly in secondary structure in bulk solution.
- The protein corona consisted of full-length ovalbumin (soft corona) and fragments (hard corona).
- Soft corona ovalbumin at pH 7 showed preserved thermostability and proteolytic stability but reduced fibril formation.
- Structural changes in soft corona ovalbumin mimicked heat-induced changes (80°C).
Conclusions:
- Microplastics readily bind to ovalbumin, forming a protein corona.
- Adsorption alters ovalbumin's structure and functional properties, including stability and aggregation behavior.
- These findings highlight potential risks of microplastic contamination in food, affecting protein integrity and safety.
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