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Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
International Journal of Biological Macromolecules2024
20 citations
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Score: 55
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0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Tamara Mutić,
Tamara Lujic,
Tamara Mutić,
Nikola Gligorijević,
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Tamara Mutić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Nikola Gligorijević,
Nikola Gligorijević,
Tamara Mutić,
Tamara Mutić,
Tamara Mutić,
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Tanja Ćirković Veličković
Tamara Mutić,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Nikola Gligorijević,
Nikola Gligorijević,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Tamara Vasović,
Tamara Vasović,
Tamara Vasović,
Tamara Vasović,
Tamara Vasović,
Tamara Lujic,
Tamara Lujic,
Tamara Mutić,
Maria Krishna de Guzman,
Tanja Ćirković Veličković
Jelena M. Aćimović,
Tanja Ćirković Veličković
Tamara Mutić,
Tamara Mutić,
Dragana Stanić-Vučinić,
Tamara Mutić,
Jelena M. Aćimović,
Jelena M. Aćimović,
Tamara Lujic,
Tanja Ćirković Veličković
Tamara Mutić,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tamara Lujic,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Jelena M. Aćimović,
Tanja Ćirković Veličković
Jelena M. Aćimović,
Tamara Vasović,
Tamara Vasović,
Tanja Ćirković Veličković
Maria Krishna de Guzman,
Dragana Stanić-Vučinić,
Maria Krishna de Guzman,
Dragana Stanić-Vučinić,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Maria Krishna de Guzman,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Tanja Ćirković Veličković
Summary
Researchers investigated how polystyrene and polyethylene terephthalate microplastics interact with ovalbumin, a common egg protein, under different pH conditions. They found that the microplastics adsorbed the protein and altered its three-dimensional structure, with smaller particles and acidic conditions leading to stronger interactions. The study suggests that microplastic contamination in food could change the structural properties of dietary proteins, potentially affecting how they are digested.
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.