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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.
The flexibility and the low production costs offered by plastics have made them crucial to society. Unfortunately, due to their resistance to biological degradation, plastics remain in the environment for an extended period of time, posing a growing risk to life on earth. Synthetic treatments of plastic waste damage the environment and may cause damage to human health. Bacterial and fungal isolates have been reported to degrade plastic polymers in a logistic safe approach with the help of their microbial cell enzymes. Recently, the bacterial strain Ideonella sakaiensis (201-F6) was discovered to break down and assimilate polyethylene terephthalate (PET) plastic via metabolic processes at 30 °C to 37 °C. PETase and MHETase enzymes help the bacterium to accomplish such tremendous action at lower temperatures than previously discovered enzymes. In addition to functioning at low temperatures, the noble bacterium's enzymes have amazing qualities over pH and PET plastic degradation, including a shorter period of degradation. It has been proven that using the enzyme PETase, this bacterium hydrolyzes the ester linkages of PET plastic, resulting in production of terephthalic acid (TPA), nontoxic compound and mono-2-hydroxyethyl (MHET), along with further depolymerization of MHET to release ethylene glycogen (EG) and terephthalic acid (TPA) by the second enzyme MHETase. Enzymatic plastic degradation has been proposed as an environmentally friendly and long-term solution to plastic waste in the environment. As a result, this review focuses on the enzymes involved in hydrolyzing PET plastic polymers, as well as some of the other microorganisms involved in plastic degradation.
More Papers Like This
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.
Biodegradation of PET: Current Status and Application Aspects
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This review covered the current status of PET biodegradation, focusing on the discovery and mechanism of PET hydrolytic enzymes from Ideonella sakaiensis and the pathway from enzyme identification to potential bioremediation application. The authors assess progress toward commercializing enzymatic PET degradation and identify remaining technical barriers for large-scale plastic waste management.
Current advances in the structural biology and molecular engineering of PETase
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The study reviews advances in the structural biology and molecular engineering of PETase, an enzyme from the bacterium Ideonella sakaiensis that can break down PET plastic at moderate temperatures. Researchers discuss efforts to enhance the enzyme's activity and thermal stability through protein engineering, which could lead to more efficient and environmentally friendly PET recycling strategies.
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.
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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.