Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Rational redesign of FAST-PETase via a "locking" strategy for efficient PET depolymerization.

Journal of hazardous materials - 1 May 2026

Qu Zhi, Tian Zongyang, Guo Zehui, Sun Yan

Abstract excerpt

Extensive accumulation of polyethylene terephthalate (PET) plastic waste causes serious pollution to the global environment, and developing superior PET hydrolases is vital for the enzymatic degradation and biorecycling of PET. Here, we propose a "locking" strategy for the rational redesign of FAST-PETase, one of the best-performing PETase variants reported so far, to further improve its performance. The best...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biodegradation, Environmental
Share to Hydrolases
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Identifiers

PMID: 41931896
DOI: 10.1016/j.jhazmat.2026.141883

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rational redesign of FAST-PETase via a "locking" strategy for efficient PET depolymerization.PMID 41931896Read ↗

Molecular Insights into the Enhanced Activity and/or Thermostability of PET Hydrolase by D186 Mutations.Semantic proximity Read ↗

Engineering of enhanced thermal stability of bis (2-hydroxyethyl) terephthalate (BHET) hydrolase from Stenotrophomonas pavanii for polyethylene terephthalate (PET) degradation.Semantic proximity Read ↗

Characterization and engineering of a two-enzyme system for plastics depolymerization.Semantic proximity Read ↗

Emerging Strategies in Polyethylene Terephthalate Hydrolase Research for Biorecycling.Semantic proximity Read ↗

Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations.Semantic proximity Read ↗

Ancestral Sequence Reconstruction Identifies Structural Changes Underlying the Evolution of Ideonella sakaiensis PETase and Variants with Improved Stability and Activity.Semantic proximity Read ↗

The effect of double (S238F/W159H) mutations on the structure and dynamics of PET degrading enzyme.Semantic proximity Read ↗

Efficient thermophilic polyethylene terephthalate hydrolase enhanced by cross correlation-based accumulated mutagenesis strategy.Semantic proximity Read ↗

Structure and Energetics of PET-Hydrolyzing Enzyme Complexes: A Systematic Comparison from Molecular Dynamics Simulations.Semantic proximity Read ↗

Rationality-informed protein evolution enables enhancement of PET hydrolase activity.Semantic proximity Read ↗

Structural bioinformatics-based protein engineering of thermo-stable PETase from Ideonella sakaiensis.Semantic proximity Read ↗

Protein engineering of stable IsPETase for PET plastic degradation by Premuse.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.