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Food & Water
Gut & Microbiome
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Small polystyrene microplastics interfere with the breakdown of milk proteins during static in vitro simulated human gastric digestion
Environmental Pollution2023
25 citations
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Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count.
Score: 55
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0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Maria Krishna de Guzman,
Tamara Lujic,
Tamara Lujic,
Maria Krishna de Guzman,
Nikola Gligorijević,
Lukas Wimmer,
Lukas Wimmer,
Tamara Lujic,
Tamara Lujic,
Nikola Gligorijević,
Dragana Stanić-Vučinić,
Nikola Gligorijević,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Tamara Lujic,
Maria Krishna de Guzman,
Lukas Wimmer,
Tamara Lujic,
Tamara Lujic,
Lukas Wimmer,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Lukas Wimmer,
Tanja Ćirković Veličković
Lukas Wimmer,
Lukas Wimmer,
Tanja Ćirković Veličković
Maria Krishna de Guzman,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Dragana Stanić-Vučinić,
Nikola Gligorijević,
Nikola Gligorijević,
Tamara Vasović,
Lukas Wimmer,
Tamara Vasović,
Tamara Vasović,
Lea Ann Dailey,
Tamara Lujic,
Lukas Wimmer,
Tamara Lujic,
Lukas Wimmer,
Tamara Vasović,
Tamara Vasović,
Dragana Stanić-Vučinić,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Lea Ann Dailey,
Lea Ann Dailey,
Lea Ann Dailey,
Lea Ann Dailey,
Maria Krishna de Guzman,
M. D. Gasparyan,
M. D. Gasparyan,
Tanja Ćirković Veličković
Dragana Stanić-Vučinić,
Tamara Lujic,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Lea Ann Dailey,
Tanja Ćirković Veličković
Lea Ann Dailey,
Lukas Wimmer,
Dragana Stanić-Vučinić,
Lukas Wimmer,
Tamara Lujic,
Lea Ann Dailey,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Dragana Stanić-Vučinić,
Maria Krishna de Guzman,
Lea Ann Dailey,
Maria Krishna de Guzman,
Lea Ann Dailey,
Lea Ann Dailey,
Tamara Vasović,
Tamara Vasović,
Lea Ann Dailey,
Dragana Stanić-Vučinić,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Lea Ann Dailey,
Lea Ann Dailey,
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
Sam Van Haute,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Sam Van Haute,
Tanja Ćirković Veličković
Lea Ann Dailey,
Tanja Ćirković Veličković
Tanja Ćirković Veličković
Lea Ann Dailey,
Lea Ann Dailey,
Tanja Ćirković Veličković
Lea Ann Dailey,
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Tamara Lujic,
Lukas Wimmer,
Lukas Wimmer,
Lukas Wimmer,
Lukas Wimmer,
Lea Ann Dailey,
Tanja Ćirković Veličković
Summary
Researchers found that small polystyrene microplastics interfere with the digestion of milk proteins in a simulated human stomach environment. The microplastics adsorbed the digestive enzyme pepsin onto their surface, reducing its activity and slowing the breakdown of proteins like casein and whey. The study suggests that microplastic contamination in food could impair normal digestive processes in the human gut.
Human ingestion of microplastics (MPs) is common and inevitable due to the widespread contamination of food items, but implications on the gastric digestion of food proteins are still unknown. In this study, the interactions between pepsin and polystyrene (PS) MPs were evaluated by investigating enzyme activity and conformation in a simulated human gastric environment in the presence or absence of PS MPs. The impact on food digestion was also assessed by monitoring the kinetics of protein hydrolysis through static in vitro gastric digestion of cow's milk contaminated with PS. The binding of pepsin to PS showed that the surface chemistry of MPs dictates binding affinity. The key contributor to pepsin adsorption seems to be π-π interactions between the aromatic residues and the PS phenyl rings. During quick exposure (10 min) of pepsin to increasing concentrations (222, 2219, 22188 particles/mL) of 10 μm PS (PS10) and 100 μm PS (PS100), total enzymatic activities were not affected remarkably. However, upon prolonged exposure at 1 and 2 h, preferential binding of pepsin to the small, low zeta-potential PS caused structural changes in the protein which led to a significant reduction of its activity. Digestion of cow's milk mixed with PS10 resulted in transient accumulation of larger peptides (10-35 kDa) and reduced bioavailability of short peptides (2-9 kDa) in the gastric phase. This, however, was only observed at extremely high PS10 concentration (0.3 mg/mL or 5.46E+05 particles/mL). The digestion of milk peptides, bound preferentially over pepsin within the hard corona on the PS10 surface, was delayed up to 15 min in comparison to bulk protein digestion. Intact caseins, otherwise rapidly digested, remained bound to PS10 in the hard corona for up to 15 min. This work presents valuable insights regarding the interaction of MPs, food proteins, and pepsin, and their dynamics during gastric digestion.