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Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization
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This study characterized a marine-derived enzyme (PET2) capable of breaking down PET plastic under mild conditions, assessing its efficiency for enzymatic recycling. Enzyme-based PET recycling could prevent plastic waste from fragmenting into the microplastics that accumulate in oceans and organisms.
Enzymatic polyethylene terephthalate (PET) recycling processes are gaining interest for their low environmental impact, use of mild conditions, and specificity. Furthermore, PET hydrolase enzymes are continuously being discovered and engineered. In this work, we studied a PET hydrolase (PET2), initially characterized as an alkaline thermostable lipase. PET2 was produced in a fusion form with a 6-histidine tag in the N-terminal. The PET2 activity on aromatic terephthalate and new indole-based polyesters was evaluated using polymers in powder form. Compared with IsPETase, an enzyme derived from Ideonella sakaiensis, PET2 showed a lower PET depolymerization yield. However, interestingly, PET2 produced significantly higher polybutylene terephthalate (PBT) and polyhexylene terephthalate (PHT) depolymerization yields. A clear preference was found for aromatic indole-derived polyesters over non-aromatic ones. No activity was detected on Akestra™, an amorphous copolyester with spiroacetal structures. Docking studies suggest that a narrower and more hydrophobic active site reduces its activity on PET but favors its interaction with PBT and PHT. Understanding the enzyme preferences of polymers will contribute to their effective use to depolymerize different types of polyesters.
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Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyesters Depolymerization
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Researchers characterized a marine enzyme (PET2) capable of breaking down PET plastic and related polyester materials under relatively mild conditions. Discovering and engineering enzymes that can degrade PET could help address the massive accumulation of PET microplastics in ocean environments.
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Researchers reviewed marine microorganism-derived enzymes capable of degrading plastics such as PET, finding that since the first plastic-degrading enzyme was discovered in 2005, extensive bioprospecting and protein engineering efforts have identified a growing toolkit of biocatalysts with potential for industrial recycling applications.
Plastic-Degrading Enzymes from Marine Microorganisms and Their Potential Value in Recycling Technologies
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This review catalogues plastic-degrading enzymes discovered in marine microorganisms, including PETases, cutinases, and laccases, and examines their potential for biotechnological applications in plastic waste remediation. Marine environments are highlighted as a rich but underexplored reservoir of enzymatic diversity with promising industrial relevance.
Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields
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This review distinguished between enzymatic PET surface modification (useful for fiber treatment) and enzymatic PET degradation (needed for waste management), cataloguing the hydrolases capable of each function and the conditions required. The authors evaluate the prospects for deploying PET-degrading enzymes in industrial plastic waste streams.
Enzymatic Degradation of PET plastic
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This study tested commercial-grade enzymes for degrading PET plastic and found that enzymatic degradation was effective at laboratory scale but faced challenges for real-world application. Scaling up enzymatic PET recycling could reduce the persistence of plastic waste that eventually fragments into microplastics in the environment.
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