Directed evolution of an efficient and thermostable PET depolymerase

The recent discovery of IsPETase, a hydrolytic enzyme that can deconstruct poly(ethylene terephthalate) (PET), has sparked great interest in biocatalytic approaches to recycle plastics. Realization commercial use will require the development robust engineered enzymes meet demands industrial processes. Although rationally PETases have been described, experimentally optimized via directed evolution not previously reported. Here, we describe an automated, high-throughput platform for engineering polymer degrading enzymes. Applying catalytic activity at elevated temperatures as primary selection pressure, thermostable IsPETase variant (HotPETase, Tm = 82.5 °C) was operate glass transition temperature PET. HotPETase depolymerize semicrystalline PET more rapidly than reported and selectively component laminated multimaterial. Structural analysis reveals interesting features emerged improve thermotolerance performance. Our study establishes laboratory useful plastic Enzymes (PET) deconstruction are plastics recycling, but reports on their missing. Now, is affording effectively achieves depolymerization above