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Original research — experimental, observational, or case-control study. Direct primary evidence.
Gut & Microbiome
Human Health Effects
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Effects of Polypropylene and Polyethylene Terephthalate Microplastics on Trypsin Structure and Function
International Journal of Molecular Sciences2025
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.
Scientists investigated how polypropylene and PET microplastics interact with trypsin, a key digestive enzyme, and with meat proteins during digestion. They found that while microplastics did bind to the enzyme and slightly altered its structure, the effects on actual protein digestion were minimal at realistic concentrations. The study suggests that the amounts of microplastics typically present in the human gut are unlikely to significantly interfere with how we digest meat proteins.
Ingestion is one of the main exposure routes of humans and animals to microplastics (MPs). During digestion, MPs can interact with both gastrointestinal enzymes and food proteins. This study investigated the adsorption of trypsin onto polypropylene (PP) and polyethylene terephthalate (PET) MPs, the influence of MPs on trypsin structure and activity, and the 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 the adsorption and desorption of protein through time. Trypsin adsorption onto MPs results in slight structural changes in the SC and bulk solution, while a trypsin fraction residing in the HC loses 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 the 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, the corona on PP and PET MP is composed of BME sarcoplasmic proteins and allergenic α-Gal-carrying proteins.