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Molecular docking analysis of PET with MHET
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Researchers performed molecular docking analysis of PET polymer with mono(2-hydroxyethyl) terephthalic acid (MHET), investigating how the enzyme from Ideonella sakaiensis 201-F6 — a bacterium capable of degrading a thin PET film in six weeks — might be optimized to improve catalytic efficiency and expand substrate specificity for enzymatic plastic degradation.
An estimated 311 million tons of plastics are produced annually worldwide; 90% of these are derived from petrol. A considerable portion of these plastics is used for packaging (such as drinking bottles), but only ~14% is collected for recycling. Most plastics degrade extremely slowly, thus constituting a major environmental hazard, especially in the oceans, where microplastics are a matter of major concern. One potential solution for this problem is the synthesis of degradable plastics from renewable resources. From the microbial consortium, the researchers isolated a unique bacterium Ideonella sakaiensis 201-F6 that could almost completely degrade a thin film of PET in a short span of six weeks at 30°C. The objective of the present study is to identify the ligands that may be exploited to improve catalysis and expand substrate specificity and thus significantly advance enzymatic plastic polymer degradation.
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Characterization and engineering of a two-enzyme system for plastics depolymerization
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A 1.6 Å resolution crystal structure of MHETase — the second enzyme in Ideonella sakaiensis's PET-degrading two-enzyme system — revealed a PETase-like core capped by a lid domain, and computational and biochemical analysis confirmed a canonical serine hydrolase mechanism, enabling rational engineering of the PET recycling pathway.
In silico binding affinity analysis of microplastic compounds on PET hydrolase enzyme target of Ideonella sakaiensis
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Researchers used computer simulations to test whether a bacterial enzyme (PET hydrolase from Ideonella sakaiensis) could break down six types of plastic, finding it most effective against polycarbonate and polyethylene terephthalate (PET) and least effective against PVC, informing which plastics this microbe might help degrade in the environment.
Insight on recently discovered PET polyester-degrading enzymes, thermostability and activity analyses
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Researchers reviewed the enzymatic machinery of Ideonella sakaiensis and related microorganisms for PET degradation, detailing how PETase and MHETase cooperatively hydrolyze the polymer to terephthalic acid and ethylene glycol at moderate temperatures — and assessing the thermostability and pH tolerances that determine these enzymes' industrial potential.
A mini-review on the role of PETase in polyethylene terephthalate degradation
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This mini-review summarized the structure, performance enhancement approaches, and potential applications of PETase, the enzyme from Ideonella sakaiensis discovered in 2016 that uses PET plastic as a carbon source, alongside MHETase for complete degradation into terephthalic acid and ethylene glycol. The review highlighted progress in enzyme engineering for improved PETase activity and discussed applications in bioremediation and recycling, identifying it as a key candidate for addressing the global plastic waste problem through biological degradation.
Explorations of Polyethylene Terephthalate (PET) Hydrolase for addressing PET Plastic Pollution
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This review explores the biology of PETase enzymes and their potential for addressing PET plastic pollution, covering the discovery of Ideonella sakaiensis and subsequent enzyme engineering efforts. Developing efficient PET-degrading enzymes is a promising biotechnological strategy for reducing plastic pollution at scale.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.