This study shows biodegradation of BHET by Schizophyllum commune, implying cutinase-like enzymes boost enzymatic activity.
The accumulation of polyethylene terephthalate (PET) in the environment demands efficient microbial strategies for its degradation. This study evaluates the biodegradation potential of Schizophyllum commune BNT39 toward bis(2-hydroxyethyl) terephthalate (BHET), a major PET intermediate, and PET itself. Clear halos on BHET-agar plates indicated extracellular hydrolytic activity. In liquid culture, thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) analyses revealed a three-phase degradation profile characterized by rapid BHET hydrolysis, transient dimer accumulation, and subsequent conversion to terephthalic acid (TPA). BHET was reduced by approximately 96% within seven days, while TPA accumulation reached 0.8 mg/mL after 30 days of incubation. Although PET degradation was limited, TPA was consistently detected as the principal product, with no BHET or MHET intermediates. To explore strategies for enhancing enzymatic activity, apple-derived cutin, PET, BHET, and polycaprolactone (PCL) were tested as inducers. Cutin markedly stimulated extracellular enzyme production, suggesting activation of cutinase-like enzymes. Overall, S. commune BNT39 demonstrates the ability to transform PET-related substrates, with cutin emerging as a promising natural stimulant to enhance enzymatic depolymerization. Future studies should focus on enzyme purification, activity profiling, and reaction optimization near PET’s glass transition temperature, where the polymer becomes more accessible for enzymatic attack.
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Martínez et al. (2025) studied this question.
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