A5060171750- Microplastics and Plastic Pollution
- biodegradable polymer synthesis and properties
- Recycling and Waste Management Techniques
- Enzyme Catalysis and Immobilization
- Ionic liquids properties and applications
- Phase Equilibria and Thermodynamics
- Graphene and Nanomaterials Applications
- Additive Manufacturing and 3D Printing Technologies
- Effects and risks of endocrine disrupting chemicals
- Biofuel production and bioconversion
- Aluminum Alloys Composites Properties
- Polyamine Metabolism and Applications
- Enzyme Production and Characterization
- Aluminum Alloy Microstructure Properties
- Enzyme Structure and Function
- Polymer crystallization and properties
- Microbial Metabolic Engineering and Bioproduction
- Amino Acid Enzymes and Metabolism
- Protein Structure and Dynamics
- Thermochemical Biomass Conversion Processes
- Water Quality Monitoring and Analysis
- Bioeconomy and Sustainability Development
- Extraction and Separation Processes
- Catalysis and Oxidation Reactions
- Enzyme-mediated dye degradation
Universität Greifswald
2019-2025
Peking University
2024
Grinm Advanced Materials (China)
2021-2022
Ansteel (China)
2009-2022
Leipzig University
2012-2021
Nanjing Tech University
2021
Shandong University
2012-2021
RWTH Aachen University
2021
Institute of Process Engineering
2021
Beijing University of Chemical Technology
2021
In this study cutinases from Thermobifida cellulosilytica DSM44535 (Thc_Cut1 and Thc_Cut2) fusca DSM44342 (Thf42_Cut1) hydrolyzing poly(ethylene terephthalate) (PET) were successfully cloned expressed in E.coli BL21-Gold(DE3). Their ability to hydrolyze PET was compared with other enzymes natural polyesters, including the PHA depolymerase (ePhaZmcl) Pseudomonas fluorescens two T. KW3. The three isolated are very similar (only a maximum of 18 amino acid differences) but yet had different...
Polyethylene terephthalate (PET) is one of the most important synthetic polymers used today. Unfortunately, accumulate in nature and to date no highly active enzymes are known that can degrade it at high velocity. Enzymes involved PET degradation mainly α- β-hydrolases, like cutinases related (EC 3.1.1). Currently, only a small number such well characterized. In this work, search algorithm was developed identified 504 possible hydrolase candidate genes from various databases. A further...
Polyethylene terephthalate (PET) is the most important mass-produced thermoplastic polyester used as a packaging material. Recently, thermophilic hydrolases such TfCut2 from Thermobifida fusca have emerged promising biocatalysts for an eco-friendly PET recycling process. In this study, postconsumer food containers are treated with and show weight losses of more than 50% after 96 h incubation at 70 °C. Differential scanning calorimetry analysis indicates that high linear degradation rates...
Biocatalysis can enable a closed-loop recycling of post-consumer PET waste.
Over 359 million tons of plastics were produced worldwide in 2018, with significant growth expected the near future, resulting global challenge end-of-life management. The recent identification enzymes that degrade previously considered non-biodegradable opens up opportunities to steer plastic recycling industry into realm biotechnology. Here, sequential conversion post-consumer polyethylene terephthalate (PET) two types bioplastics is presented: a medium chain-length polyhydroxyalkanoate...
Recent studies on the enzymatic degradation of synthetic polyesters have shown potential polyester hydrolases from thermophilic actinomycetes for modifying or degrading polyethylene terephthalate (PET). TfCut2 Thermobifida fusca KW3 and LC-cutinase (LCC) isolated a compost metagenome are remarkably active with high sequence structural similarity. Both enzymes exhibit an exposed site in substrate binding groove located at protein surface. By exchanging selected amino acid residues involved...
TfCut2 from Thermobifida fusca KW3 and the metagenome-derived LC-cutinase are bacterial polyester hydrolases capable of efficiently degrading polyethylene terephthalate (PET) films. Since enzymatic PET hydrolysis is inhibited by degradation intermediate mono-(2-hydroxyethyl) (MHET), a dual enzyme system consisting hydrolase immobilized carboxylesterase TfCa was employed for films at 60°C. HPLC analysis reaction products obtained after 24 h showed an increased amount soluble with lower...
Polyethylene terephthalate (PET) is a mass-produced synthetic polyester contributing remarkably to the accumulation of solid plastics waste and pollution in natural environments. Recently, bioremediation using engineered enzymes has emerged as an eco-friendly alternative approach for future plastic circular economy. Here we genetically thermophilic anaerobic bacterium, Clostridium thermocellum, enable secretory expression cutinase (LCC), which was originally isolated from plant compost...
Thermophilic polyester hydrolases (PES-H) have recently enabled biocatalytic recycling of the mass-produced synthetic polyethylene terephthalate (PET), which has found widespread use in packaging and textile industries. The growing demand for efficient PET prompted us to solve high-resolution crystal structures two metagenome-derived enzymes (PES-H1 PES-H2) notably also complex with various substrate analogues. Structural analyses computational modeling using molecular dynamics simulations...
Enzymatic degradation and recycling can reduce the environmental impact of plastics. Despite decades research, no enzymes for efficient hydrolysis polyurethanes have been reported. Whereas ester bonds in polyester-polyurethanes by cutinases is known, urethane polyether-polyurethanes remained inaccessible to biocatalytic hydrolysis. Here we report discovery urethanases from a metagenome library constructed soil that had exposed polyurethane waste many years. We then demonstrate use urethanase...
Polyurethanes (PU) are widely used synthetic polymers. The growing amount of PU industrially has resulted in a worldwide increase plastic wastes. related environmental pollution as well the limited availability raw materials based on petrochemicals requires novel solutions for their efficient degradation and recycling. polyester Impranil DLN by hydrolases LC cutinase (LCC), TfCut2, Tcur1278 Tcur0390 was analyzed using turbidimetric assay. highest hydrolysis rates were obtained with TfCut2...
Abstract Thermomonospora curvata is a thermophilic actinomycete phylogenetically related to Thermobifida fusca that produces extracellular hydrolases capable of degrading synthetic polyesters. Analysis the genome T. DSM43183 revealed two genes coding for putative polyester Tcur1278 and Tcur0390 sharing 61% sequence identity with enzymes. Mature proteins were cloned expressed in Escherichia coli TOP10. exhibited an optimal reaction temperature against p-nitrophenyl butyrate at 60°C 55°C,...
Abstract Several bacterial polyester hydrolases are able to hydrolyze the synthetic polyethylene terephthalate (PET). For an efficient enzymatic degradation of PET, reaction temperatures close glass transition temperature polymer need be applied. The esterases TfH, BTA2, Tfu_0882, TfCut1, and TfCut2 produced by thermophilic actinomycete Thermobifida fusca exhibit PET‐hydrolyzing activity. However, these enzymes not sufficiently stable in this range for post‐consumer PET materials. addition...