Journal
CHEMCATCHEM
Volume 9, Issue 20, Pages 3888-3894Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201700849
Keywords
alcohols; enzyme catalysis; molecular dynamics; polymerization; template synthesis
Categories
Funding
- Chinese Government Scholarship under China Scholarship Council [201606790036]
- Chinese Foundation Key projects of governmental cooperation in international scientific and technological innovation [2016 YFE0115700]
- National Natural Science Foundation of China [31470509]
- Fundamental Research Funds for the Central Universities [JUSRP51622A]
- Portuguese Foundation for Science and Technology (FCT) [UID/BIO/04469/2013, POCI-01-0145-FEDER-006684]
- BioTecNorte operation - European Regional Development Fund under the scope of Norte2020Programa Operacional Regional do Norte [NORTE-01-0145-FEDER-000004]
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Laccase catalyzes the oxidation and polymerization of phenolic compounds in the presence of oxygen. Herein, we report for the first time that a previous PEGylation of laccase enhances the polymerase activity 3-fold compared with the reaction of the native enzyme, as confirmed by UV/Vis spectroscopy. The polymerization of catechol increased only 1.5-fold if poly(ethylene glycol) (PEG) was added to the medium reaction. Molecular-dynamics simulations suggest the formation of a miscible complex of polycatechol and PEG, which is responsible to push the reaction forward. In a negative control experiment set, all catalysts were entrapped inside polyacrylamide gels and here the native laccase showed a relatively higher activity. These results suggest that the mobility of PEG is a key feature for the enhancement of the reaction.
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