We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Manufacturing of the highly active thermophile PETases PHL7 and PHL7mut3 using Escherichia coli
Summary
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.