Polymer grafting from a metallo-centered enzyme improves activity in non-native environments

Marina Kovaliov, Borui Zhang, Dominik Konkolewicz, Katarzyna Szcześniak, Stefa Jurga, Saadyah Averick

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Metallo-centered enzymes have found applications in environmental remediation, green synthesis and sensors. These enzymes destabilize at extreme pH, elevated temperature or high-organic-content conditions. For these enzymes to find more widespread adoption and use, stabilization in non-native conditions is critical. We report the impact of grafting polymers from the surface of laccase, a metalloenzyme with a Cu active site, modified with a polymerization-initiating species ligated to the protein's lysine residues. Initiators for continuous activator regeneration atom transfer radical polymerization was used to graft a small library of polymers from the protein. The impact of polymer grafting on enzyme activity as a function of pH, temperature or organic solvent was determined. While polymer grafting from laccases was found to increase enzymatic activity, we found that grafting high-molecular-weight dimethylaminoethyl methacrylate displayed the greatest enhancement to catalytic activity. The results demonstrate that polymer grafting can improve laccase activity in native and non-native conditions.

Original languageEnglish
Pages (from-to)775-782
Number of pages8
JournalPolymer International
Volume70
Issue number6
DOIs
StatePublished - Jun 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2020 Society of Industrial Chemistry

Funding

SA gratefully acknowledges the Army Research Office (award no. 68271‐CH) Young Investigator Program (W911NF‐17‐1‐0015) and the Neuroscience Institute at AHN for funding.

FundersFunder number
Army Research OfficeW911NF‐17‐1‐0015, 68271‐CH
Neuroscience Institute, University of Tennessee

    Keywords

    • ATRP
    • biocatalysis
    • biohybrid
    • protein–polymer hybrid

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