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PEGylation Greatly Enhances Laccase Polymerase Activity
Author(s) -
Su Jing,
Noro Jennifer,
Loureiro Ana,
Martins Madalena,
Azoia Nuno G.,
Fu Jiajia,
Wang Qiang,
Silva Carla,
CavacoPaulo Artur
Publication year - 2017
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201700849
Subject(s) - laccase , pegylation , ethylene glycol , chemistry , catechol , peg ratio , polymerization , catalysis , enzyme , organic chemistry , combinatorial chemistry , polymer chemistry , polyethylene glycol , polymer , finance , economics
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.