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Biochemical characterization and NMR study of a PET-hydrolyzing cutinase from Fusarium solani pisi

Kristina Naasen Hellesnes, Shunmathi Vijayaraj, View ORCID ProfilePeter Fojan, Evamaria Petersen, View ORCID ProfileGaston Courtade
doi: https://doi.org/10.1101/2022.11.01.514593
Kristina Naasen Hellesnes
1NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Trondheim, Norway
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Shunmathi Vijayaraj
1NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Trondheim, Norway
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Peter Fojan
2Department of Materials and Production, Materials Engineering Group, Aalborg University, Aalborg Ø, Denmark
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Evamaria Petersen
2Department of Materials and Production, Materials Engineering Group, Aalborg University, Aalborg Ø, Denmark
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Gaston Courtade
1NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Trondheim, Norway
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  • For correspondence: gaston.courtade@ntnu.no
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ABSTRACT

In recent years, the drawbacks of plastics have become evident, with plastic pollution becoming a major environmental issue. There is an urgent need to find solutions to efficiently handle plastic waste by using novel recycling methods. Biocatalytic recycling of plastics by using enzyme-catalyzed hydrolysis is one such solution that has gained interest, in particular for recycling polyethylene terephthalate (PET). To provide insights on PET hydrolysis by cutinases, we have here characterized the kinetics of a PET-hydrolyzing cutinase from Fusarium solani pisi (FsC) at different pH values, mapped the interaction between FsC and the PET analog BHET by using NMR spectroscopy, and monitored product release directly and in real time by using time-resolved NMR experiments. We found that primarily aliphatic side chains around the active site participate in the interaction with BHET, and that pH conditions can be used to tune the relative amounts of degradation products. Moreover, we propose that the low catalytic performance of FsC on PET is caused by poor substrate binding combined with product inhibition by MHET. Overall, our results provide insights on obstacles that preclude efficient PET hydrolysis by FsC and suggest future approaches for overcoming these obstacles and generating efficient PET-hydrolyzing enzymes.

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Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • https://github.com/gcourtade/papers/tree/master/2022/FsC-PET

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted November 01, 2022.
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Biochemical characterization and NMR study of a PET-hydrolyzing cutinase from Fusarium solani pisi
Kristina Naasen Hellesnes, Shunmathi Vijayaraj, Peter Fojan, Evamaria Petersen, Gaston Courtade
bioRxiv 2022.11.01.514593; doi: https://doi.org/10.1101/2022.11.01.514593
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Biochemical characterization and NMR study of a PET-hydrolyzing cutinase from Fusarium solani pisi
Kristina Naasen Hellesnes, Shunmathi Vijayaraj, Peter Fojan, Evamaria Petersen, Gaston Courtade
bioRxiv 2022.11.01.514593; doi: https://doi.org/10.1101/2022.11.01.514593

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