
Journal of Hazardous Materials, Journal Year: 2024, Volume and Issue: 481, P. 136540 - 136540
Published: Nov. 16, 2024
Language: Английский
Journal of Hazardous Materials, Journal Year: 2024, Volume and Issue: 481, P. 136540 - 136540
Published: Nov. 16, 2024
Language: Английский
Journal of Hazardous Materials, Journal Year: 2025, Volume and Issue: unknown, P. 137441 - 137441
Published: Jan. 1, 2025
Language: Английский
Citations
2Advanced Science, Journal Year: 2025, Volume and Issue: unknown
Published: Feb. 7, 2025
Polyurethane (PUR), the fifth most prevalent synthetic polymer, substantially contributes to global plastic waste problem. Biotechnology-based recycling methods have recently emerged as innovative solutions disposal and sparked interest among scientific communities industrial stakeholders in discovering designing highly active plastic-degrading enzymes. Here, ligand-free crystal structure of UMG-SP2, a metagenome-derived urethanase with depolymerization activities, at 2.59 Å resolution, well its (co-)structures bound suicide hydrolase inhibitor short-chain carbamate substrate 2.16 2.40 resolutions, respectively, is reported. Structural analysis molecular dynamics simulations reveal that flexible loop L3 consisting residues 219-226 crucial for regulating hydrolytic activity UMG-SP2. The semi-rational redesign UMG-SP2 reveals superior variants, A141G Q399A, exhibiting over 30.7- 7.4-fold increased activities on polyester-PUR methylene diamine derivative PUR, compared wild-type enzyme. These findings advance understanding structure-function relationship PUR-hydrolyzing enzymes, which hold great promise developing effective PUR processes mitigating environmental footprint waste.
Language: Английский
Citations
1Biotechnology Advances, Journal Year: 2025, Volume and Issue: unknown, P. 108544 - 108544
Published: Feb. 1, 2025
Language: Английский
Citations
1JACS Au, Journal Year: 2024, Volume and Issue: 4(10), P. 4000 - 4012
Published: Sept. 26, 2024
Plastic-degrading enzymes facilitate the biocatalytic recycling of poly(ethylene terephthalate) (PET), a significant synthetic polymer, and substantial progress has been made in utilizing PET hydrolases for industrial applications. To fully exploit potential these enzymes, deeper mechanistic understanding followed by targeted protein engineering is essential. Through advanced molecular dynamics simulations free energy analysis methods, we elucidated complete pathway from initial binding two hydrolases-the thermophilic leaf-branch compost cutinase (LCC) polyester hydrolase 1 (PES-H1)-to an amorphous substrate, ultimately leading to chain entering active site hydrolyzable conformation. Our findings indicate that nonspecific driven polar hydrophobic interactions. We demonstrate subsequent entry into can occur via one three key pathways, identifying barriers related both PET-PET PET-enzyme interactions, as well specific residues highlighted through
Language: Английский
Citations
5Polymers, Journal Year: 2024, Volume and Issue: 16(23), P. 3368 - 3368
Published: Nov. 29, 2024
The integration of machine learning (ML) into material manufacturing has driven advancements in optimizing biopolymer production processes. ML techniques, applied across various stages production, enable the analysis complex data generated throughout identifying patterns and insights not easily observed through traditional methods. As sustainable alternatives to petrochemical-based plastics, biopolymers present unique challenges due their reliance on variable bio-based feedstocks processing conditions. This review systematically summarizes current applications techniques aiming provide a comprehensive reference for future research while highlighting potential enhance efficiency, reduce costs, improve product quality. also shows role algorithms, including supervised, unsupervised, deep
Language: Английский
Citations
5Ecotoxicology and Environmental Safety, Journal Year: 2025, Volume and Issue: 289, P. 117640 - 117640
Published: Jan. 1, 2025
As a global environmental challenge, plastic pollution raises serious ecological and health concerns owing to the excessive accumulation of waste, which disrupts ecosystems, harms wildlife, threatens human health. Polyethylene terephthalate (PET), one most commonly used plastics, has contributed significantly this growing crisis. This study offers solution for by identifying novel PET-degrading enzymes. Using combined approach computational analysis metagenomic workflow, we identified diverse array genes enzymes linked degradation. Our 1305,282 unmapped genes, 36,000 CAZymes, 317 plastizymes in soil samples were heavily contaminated with plastic. We extended our training machine learning models discover candidate To overcome scarcity known enzymes, Generative Adversarial Network (GAN) model dataset augmentation pretrained deep Evolutionary Scale Language Model (ESM) generate sequence embeddings classification. Finally, 21 identified. These further validated through active site analysis, amino acid composition 3D structure comparison. Additionally, isolated bacterial strains from soils extracted demonstrate their potential remediation. highlights importance biotechnological solutions pollution, emphasizing scalable, cost-effective processes integration methods.
Language: Английский
Citations
0ACS Sustainable Chemistry & Engineering, Journal Year: 2025, Volume and Issue: unknown
Published: Jan. 29, 2025
Language: Английский
Citations
0ACS Sustainable Chemistry & Engineering, Journal Year: 2025, Volume and Issue: unknown
Published: Feb. 3, 2025
Language: Английский
Citations
0Nature Chemical Engineering, Journal Year: 2025, Volume and Issue: unknown
Published: Feb. 17, 2025
Language: Английский
Citations
0Environmental Science & Technology Letters, Journal Year: 2025, Volume and Issue: unknown
Published: March 19, 2025
Management of polyethylene terephthalate (PET) plastic waste remains a challenge. PET-hydrolyzing enzymes (PHEs) such as IsPETase and variants like FAST-PETase demonstrate promising PET depolymerization capabilities at ambient temperatures can be utilized to recycle upcycle waste. Whole-cell biocatalysts displaying PHEs on their surface offer high efficiency, reusability, stability for depolymerization. However, efficacy in fully breaking down is hindered by the necessity two enzymes: PETase MHETase. Current whole-cell systems either display only one enzyme or struggle with performance when larger MHETase–PETase chimera. We developed Saccharomyces cerevisiae-based biocatalyst complete into its constituent monomers no accumulation intermediate products. Leveraging cellulosome-inspired trifunctional protein scaffoldin displayed yeast surface, we co-immobilized MHETase, forming multi-enzyme cluster. This achieved 30 °C, yielding 4.95 mM terephthalic acid (TPA) tested film. Furthermore, showed improved ability binding multiple sites scaffoldin. The whole cells had added advantage retained activity over reusability cycles. breakthrough marks step toward circular economy.
Language: Английский
Citations
0