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Original research — experimental, observational, or case-control study. Direct primary evidence.
Gut & Microbiome
Human Health Effects
Remediation
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Effects of Polypropylene and Polyethylene Terephthalate Microplastics on Trypsin Structure and Function
Preprints.org2025
2 citations
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Score: 58
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0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Researchers investigated how polypropylene and PET microplastics interact with trypsin, a key digestive enzyme, and whether this affects the digestion of meat proteins. They found that while some trypsin molecules lost most of their activity after binding tightly to microplastic surfaces, the overall effect on protein digestion was minimal at realistic exposure levels. The study suggests that the concentrations of microplastics typically encountered in the gut are unlikely to significantly impair the digestion of meat proteins.
Ingestion is one of the main exposure routes of humans to microplastics (MPs). During digestion, MPs can interact with both gastrointestinal enzymes and food proteins. This study investigated adsorption of trypsin to polypropylene (PP) and polyethylene terephthalate (PET) MPs, the influence of MPs on trypsin structure and activity, and in vitro trypsin digestibility of bovine meat extract (BME) sarcoplasmic proteins and BME α-Gal-carrying allergens (α-GalA) in the presence of PP and PET MPs. Trypsin, BME and α-GalA proteins interact with MPs resulting in the formation of a soft (SC) and hard (HC) corona. This interaction is dynamic, leading to adsorption and desorption of protein through time. Trypsin adsorption to MPs results in slight structural changes in SC and bulk solution, while a trypsin fraction residing in the HC lost most of its specific activity. The presence of MPs slightly slows down the digestibility of proteins with a mass of 38 kDa, while it does not affect digestion of α-GalA. According to our results, it is unlikely that realistic concentrations of MPs in the intestine would have significant effects on meat extract proteins and allergens digestibility by trypsin. We confirmed that during trypsin digestion, corona on PP and PET MP is composed of BME sarcoplasmic proteins and allergenic α-Gal-carrying proteins.