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

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 condit...

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Bibliographic Details
Published in:Polymer international 2021-06, Vol.70 (6), p.775-782
Main Authors: Kovaliov, Marina, Zhang, Borui, Konkolewicz, Dominik, Szcześniak, Katarzyna, Jurga, Stefa, Averick, Saadyah
Format: Article
Language:English
Subjects:
ATRP
biocatalysis
biohybrid
Catalytic activity
Copper
Enzymatic activity
Enzyme activity
Enzymes
Grafting
High temperature
Laccase
Lysine
Metallography
pH effects
Polymerization
Polymers
Proteins
protein–polymer hybrid
Regeneration
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Summary: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. © 2020 Society of Industrial Chemistry ICAR ATRP was used to grow a small library of polymers from the metallo‐enzyme laccase. The laccase–polymer hybrids displayed superior temperature, solvent and pH stability compared to native laccase.
ISSN:0959-8103
1097-0126
DOI:10.1002/pi.6127