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The Esterase Gs Derived from Geobacillus sp. JM6 Exhibits Hydrolytic Activity on the PET Model Substrates
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Researchers identified a thermophilic esterase (Gs) from Geobacillus sp. JM6 that effectively degrades BHET, a key PET model substrate, and found that pairing Gs with MHETase enables complete hydrolysis of BHET, offering a new enzymatic resource for biological breakdown of PET plastic.
The continuous increase in demand for polyethylene terephthalate (PET) has drawn global attention to the significant environmental pollution caused by the degradation of PET plastics. Exploring new PET-degrading enzymes is essential for enhancing the degradation efficiency of PET, and esterases and lipases with plastic degradation capabilities have become a focal point of research. In this study, we utilized the ultra-efficient mutant FASTase of the PET-degrading enzyme IsPETase, derived from Ideonella sakaiensis, as a positive control, based on the similarity in enzyme activity and substrate. We investigated the PET model substrate degradation activities of the esterase Gs and lipase GI, both derived from Bacillus spp., as well as the lipase CAI derived from Pseudomonas spp. The results indicated that Gs exhibited excellent bis(2-hydroxyethyl) terephthalate (BHET) degradation activity; however, Gs demonstrated a lack of thermal stability when hydrolyzing BHET. Molecular docking analyses were conducted to identify the key amino acids involved in the degradation of BHET by Gs from a structural perspective. At the same time, GI and CAI showed no BHET degradation activity. The combination of Gs and the mono-2-hydroxyethyl terephthalate (MHET) hydrolase, MHETase, can completely hydrolyze BHET, and Gs also exhibited degradation activity against the PET model substrate bis(benzyloxyethyl) terephthalate and PET nanoparticles. Given the structural similarity between PET hydrolase LCC-ICCG and Gs, this study provides new enzyme resources for advancing the efficient biological enzymatic degradation of PET plastics.
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Enzymatic Degradation of Polyethylene Terephthalate Model Substrates by Esterase E4
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Researchers identified a novel esterase (E4) from Altererythrobacter indicus that degrades polyethylene terephthalate (PET) plastic and its model substrates, retaining activity under high-temperature and high-salt conditions and boosting the activity of a known ultra-efficient PETase when used together, broadening the toolkit for enzymatic plastic recycling.
Unveiling the PET plastics degradation potential of the thermostable EstS1 esterase through integrated biochemical, structural, and morphological analyses
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This study characterized the PET-degrading potential of the thermostable esterase EstS1 from an environmental isolate, finding it degrades 75% of BHET (PET's primary intermediate) within one hour, and determined crystal structures showing BHET binding at the active site. SEM imaging demonstrated significant degradation of crystalline PET film over 15 days in controlled and soil-based conditions, with XPS analysis confirming formation of new chemical bonds on the treated surface, supporting potential for dual degradation of plastic and plasticizers.
Evaluation of Bacillus-Associated Polyethylene Terephthalate (PET) Surfaces For Biodegradation
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Polyethylene terephthalate (PET) is one of the most common plastics, found in bottles and packaging, and it breaks down into persistent microplastics in the environment. This study screened bacteria collected from PET surfaces at a landfill in Malaysia, finding strains with promising esterase activity capable of forming biofilms on PET and beginning to degrade it. The findings point toward biological solutions for breaking down PET microplastics before they spread further into ecosystems.
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Researchers used computational modeling and biochemical assays to characterize a PET-degrading enzyme from Streptomyces bacteria, finding it can break down bis(2-hydroxyethyl) terephthalate, a key PET degradation product, suggesting potential for enzymatic plastic recycling.
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