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Concentration‐dependent inhibition of mesophilic PETases on poly(ethylene terephthalate) can be eliminated by enzyme engineering

DOI: 10.1002/cssc.202202277 DOI Help

Authors: Luisana Avilan (University of Portsmouth) , Bruce R. Lichtenstein (University of Portsmouth) , Gerhard Koenig (University of Portsmouth) , Michael Zahn (University of Portsmouth) , Mark D. Allen (University of Portsmouth) , Liliana Oliveira (University of Portsmouth) , Matilda Clark (University of Portsmouth) , Victoria Bemmer (University of Portsmouth) , Rosie Graham (University of Portsmouth) , Harry P. Austin (University of Greifswald) , Graham Dominick (National Renewable Energy Laboratory, Renewable Resources and Enabling Sciences Center) , Christopher W. Johnson (National Renewable Energy Laboratory, Renewable Resources and Enabling Sciences Center) , Gregg T. Beckham (National Renewable Energy Laboratory, Renewable Resources and Enabling Sciences Center) , John Mcgeehan (University of Portsmouth) , Andrew R. Pickford (University of Portsmouth)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chemsuschem

State: Published (Approved)
Published: February 2023
Diamond Proposal Number(s): 17212

Abstract: Enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). PETase from Ideonella sakaiensis (IsPETase) is capable of PET hydrolysis under mild conditions but suffers from concentration-dependent inhibition. Here, we report that this inhibition is dependent on incubation time, the solution conditions and PET surface area. Furthermore, this inhibition is evident in other mesophilic PET-degrading enzymes to varying degrees, independent of the level of PET depolymerization activity. The inhibition has no clear structural basis, but moderately thermostable IsPETase variants exhibit reduced inhibition, and the property is completely absent in the highly thermostable HotPETase, previously engineered by directed evolution, which our simulations suggest results from reduced flexibility around the active site. This work highlights a limitation in applying natural mesophilic hydrolases for PET hydrolysis, and reveals an unexpected positive outcome of engineering these enzymes for enhanced thermostability.

Journal Keywords: IsPETase; mesophilic enzymes; interfacial biocatalysis; inhibition; PET hydrolase

Diamond Keywords: Plastics; Enzymes; Biodegradation

Subject Areas: Biology and Bio-materials, Chemistry, Environment

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 22/02/2023 10:32

Discipline Tags:

Earth Sciences & Environment Biotechnology Biochemistry Catalysis Chemistry Structural biology Engineering & Technology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)