De novo design of a polycarbonate hydrolase

Laura H. Holst, Niklas G. Madsen, Freja T. Toftgård, Freja Rønne, Ioana Malina Moise, Evamaria I. Petersen*, Peter Fojan*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

1 Citation (Scopus)


Enzymatic degradation of plastics is currently limited to the use of engineered natural enzymes. As of yet, all engineering approaches applied to plastic degrading enzymes retain the natural α/β-fold. While mutations can be used to increase thermostability, an inherent maximum likely exists for the α/β-fold. It is thus of interest to introduce catalytic activity toward plastics in a different protein fold to escape the sequence space of plastic degrading enzymes. Here, a method for designing highly thermostable enzymes that can degrade plastics is described. With the help of Rosetta an active site catalysing the hydrolysis of polycarbonate is introduced into a set of thermostable scaffolds. Through computational evaluation, a potential PCase was selected and produced recombinantly in Escherichia coli. Thermal analysis suggests that the design has a melting temperature of >95C. Activity toward polycarbonate was confirmed using atomic force spectroscopy (AFM), proving the successful design of a PCase.

Original languageEnglish
Article numbergzad022
JournalProtein Engineering, Design and Selection
Publication statusPublished - 2023

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© The Author(s) 2023. Published by Oxford University Press. All rights reserved.


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