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Manufacturing of the highly active thermophile PETases PHL7 and PHL7mut3 using Escherichia coli
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This study develops scalable production of two high-performing thermophilic PETases—PHL7 and LCC—using the yeast Komagataella phaffii (Pichia pastoris) as an expression host, optimizing fermentation conditions for high-yield secretion. Both enzymes retain strong PET-degrading activity at elevated temperatures, making them candidates for industrial enzymatic plastic recycling processes. The work demonstrates that K. phaffii is an effective platform for manufacturing thermostable plastic-degrading enzymes at quantities relevant for scale-up.
In this research, we present an optimized process for the extracellular production of thermophile and highly active PETases PHL7 and PHL7mut3, eliminating the need for costly purification steps. These advancements support large-scale enzymatic recycling, contributing to solving the global plastic waste crisis.
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Process development for PETase production and purification
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Researchers developed a production and purification process for PETase, an enzyme capable of breaking down polyethylene terephthalate (PET) plastic biologically, as an alternative to inadequate mechanical and chemical recycling methods for mixed and contaminated PET waste. The study addresses the global plastic pollution crisis by advancing the scalability of enzymatic PET degradation as a sustainable recycling pathway.
Increased cytoplasmic expression of PETase enzymes in E. coli.
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Researchers optimized the production of PETase — an enzyme that breaks down PET plastic — in E. coli bacteria, achieving higher yields of active enzyme using a bioreactor. Improving enzyme production methods is a key step toward scaling up biological plastic recycling to address PET pollution in the environment.
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties
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Researchers discovered a new enzyme from a soil bacterium that can break down PET plastic — the material in most plastic bottles — at both room temperature and elevated heat, then engineered an improved version that degrades PET powder almost completely within half a day at 55°C. This dual-temperature capability makes it more practical than existing enzymes for industrial-scale plastic recycling and could help address the global PET waste problem.
Discovery and mechanism-guided engineering of BHET hydrolases for improved PET recycling and upcycling
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Researchers identified and engineered two enzymes — called BHETases — that efficiently break down PET plastic (the kind used in bottles and packaging) into its chemical building blocks, achieving up to seven times better output than leading existing enzymes. By coupling these improved enzymes in a two-step system, the team demonstrated a path toward true closed-loop PET recycling.
An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
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This review examines the discovery and engineering of PET-degrading enzymes including PETase and cutinase variants, discussing protein engineering strategies to improve catalytic efficiency and thermostability for practical biodegradation of polyethylene terephthalate plastic waste.
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.