We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Insights into the Enhancement of the Poly(ethylene terephthalate) Degradation by FAST-PETase from Computational Modeling
AI summary Read the abstract
"Researchers used classical and quantum mechanical/molecular mechanics simulations to reveal why the engineered enzyme FAST-PETase degrades PET plastic far more efficiently than its parent enzyme PETase, tracing the enhancement to a single N233K mutation that increases the basicity of a catalytic residue and lowers the energy barrier for the rate-limiting acylation step by over 4 kcal/mol. These findings provide molecular-level design principles for engineering even more effective plastic-degrading enzymes."
Polyethylene terephthalate (PET) is the most abundant polyester plastic, widely used in textiles and packaging, but, unfortunately, it is also one of the most discarded plastics after one use. In the last years, the enzymatic biodegradation of PET has sparked great interest owing to the discovery and subsequent mutation of PETase-like enzymes, able to depolymerize PET. FAST-PETase is one of the best enzymes hitherto proposed to efficiently degrade PET, although the origin of its efficiency is not completely clear. To understand the molecular origin of its enhanced catalytic activity, we have carried out a thorough computational study of PET degradation by the FAST-PETase action by employing classical and hybrid (QM/MM) molecular dynamics (MD) simulations. Our findings show that the rate-limiting reaction step for FAST-PETase corresponds to the acylation stage with an estimated free energy barrier of 12.1 kcal mol–1, which is significantly smaller than that calculated for PETase (16.5 kcal mol–1) and, therefore, supports the enhanced catalytic activity of FAST-PETase. The origin of this enhancement is mainly attributed to the N233K mutation, which, although sited relatively far from the active site, induces a chain folding where the Asp206 of the catalytic triad is located, impeding that this residue sets effective H-bonds with its neighboring residues. This effect makes Asp206 hold a more basic character compared to the wild-type PETase and boosts the interaction with the protonated His237 of the catalytic triad in the transition state of acylation, with the consequent decrease of the catalytic barrier and acceleration of the PET degradation reaction.
More Papers Like This
The Action of Plastic Degrading Enzyme is Accelerated Mainly Due to an Increase in Thermal Stability Rather Than by Inherent Catalytic Effect
AI summary Read the abstract
Researchers used computational simulations to investigate why the engineered FAST-PETase enzyme breaks down PET plastic more efficiently than its wild-type counterpart, finding that enhanced thermal stability — rather than direct catalytic improvements — is the primary driver of its superior performance at elevated temperatures.
Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review
AI summary Read the abstract
This systematic review examined the role of mutations in engineering PET-degrading enzymes including TfCut2, IsPETase, and LCC across 20 studies, integrating molecular dynamics simulations with experimental findings. The review identifies key residue hotspots enhancing catalytic performance and thermostability, demonstrating MD simulations as powerful tools guiding targeted mutation strategies for enzymatic plastic degradation.
Single Distal Mutation Enhances Activity of known PETases via Stabilisation of PET-binding
AI summary Read the abstract
This study identified a highly active PET-degrading enzyme called Fast_2.9 through ultra-high-throughput screening, and discovered that a single distal S269T mutation improves activity by up to 400-fold over wildtype across most known PETases. The engineered enzyme can degrade multiple post-consumer PET substrates including polyester textiles within as little as two days, offering strong potential for plastic biodegradation at industrial scale.
From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets
AI summary Read the abstract
Researchers used computational and structural analyses to decode how PET polymer chains enter and bind within the active sites of plastic-degrading hydrolase enzymes, providing mechanistic insights that could guide engineering of more efficient PETase variants for industrial recycling applications.
Probing Enzymatic PET Degradation: Molecular Dynamics Analysis of Cutinase Adsorption and Stability
AI summary Read the abstract
This study used all-atom molecular dynamics simulations to reveal that the LCC-ICCG cutinase enzyme binds to PET plastic surfaces primarily through hydrophobic and aromatic interactions, with minimal structural changes to the enzyme and a 24% reduction in enzyme-water hydrogen bonds upon adsorption, clarifying key initial steps of enzymatic PET degradation.
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.