Investigating the effects of cyclic topology on the performance of a plastic degrading enzyme for polyethylene terephthalate degradation

Hayes, Heather C. and Luk, Louis Y. P. ORCID: https://orcid.org/0000-0002-7864-6261 2023. Investigating the effects of cyclic topology on the performance of a plastic degrading enzyme for polyethylene terephthalate degradation. Scientific Reports 13 , 1267. 10.1038/s41598-023-27780-4

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Abstract

Agitation is a commonly encountered stress for enzymes during all stages of production and application, but investigations that aim to improve their tolerance using topological engineering have yet to be reported. Here, the plastic-degrading enzyme IsPETase was cyclized in a range of topologies including a cyclic monomer, cyclic dimer and catenane using SpyTag/SpyCatcher technologies, and their tolerance towards different stresses including mechanical agitation was investigated. The cyclic dimer and catenane topologies were less susceptible to agitation-induced inactivation resulting in enhancement of polyethylene terephthalate (PET) degradation. While contrary to conventional belief, cyclic topologies did not improve tolerance of IsPETase towards heat or proteolytic treatment, the close proximity of active sites in the dimeric and catenane variants was found to enhance PET conversion into small soluble products. Together, these findings illustrate that it is worthwhile to explore the topology engineering of enzymes used in heterogeneous catalysis as it improves factors that are often overlooked in homogeneous catalysis studies.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Additional Information:	License information from Publisher: LICENSE 1: URL: http://creativecommons.org/licenses/by/4.0/, Type: open-access
Publisher:	Nature Research
Date of First Compliant Deposit:	24 January 2023
Date of Acceptance:	9 January 2023
Last Modified:	03 May 2023 07:20
URI:	https://orca.cardiff.ac.uk/id/eprint/156202

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