Catalytic mechanisms, engineering, and cascade biocatalysis of mono(2-hydroxyethyl) terephthalate hydrolases for efficient PET depolymerization: A review.
Lu Q, Zhou H, Chen W, Li X, Yang H
Plastic Biodegradation
Every plastic bottle in your recycling bin has a better chance of actually becoming a new product — not landfill — as enzymes get efficient enough to fully dissolve PET plastic into reusable ingredients.
A common plastic used in bottles and food packaging tends to get stuck halfway through the breakdown process when microbes try to digest it, leaving behind a stubborn middle compound. Researchers are now engineering specialized proteins that chew through that stuck compound, completing the job and releasing clean raw materials. Combining two of these protein tools in sequence has dramatically sped up the whole recycling process.
Key Findings
A bottleneck compound called MHET accumulates during plastic breakdown and blocks the enzymes doing the work — new MHET hydrolase enzymes solve this specific problem
The bacterium Ideonella sakaiensis produces a key enzyme (IsMHETase) whose structure and catalytic mechanism have now been mapped in detail, enabling targeted protein engineering
Combining PET-degrading and MHET-degrading enzymes in a coordinated two-step cascade system significantly improves complete depolymerization efficiency compared to either enzyme alone
chevron_right Technical Summary
Scientists are developing better enzymatic tools to break down plastic water bottles and food containers into reusable chemical building blocks, getting closer to truly circular plastic recycling.
Abstract Preview
Polyethylene terephthalate (PET) is a widely used synthetic polyester produced from terephthalic acid (TPA) and ethylene glycol (EG), and its environmental accumulation has become a global concern....
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