PEGylation greatly enhances laccase polymerase activity

Abstract

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 by 3-fold comparing with the native enzyme, as confirmed by UV-Vis spectroscopy. The polymerization of catechol increased only 1.5-fold when polyethyleneglycol (PEG) was added to the medium reaction. Molecular dynamic 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 acrylamide 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. ; This study was supported by Chinese GovernmentScholarship under China Scholarship Council (No. 201606790036), Chinese Foundation Key projects of governmental cooperation in international scientific and technological innovation (No.2 016 YFE0115700), the National Natural Science Foundation of China (No.31470509) and the Fundamental Research Funds for the Central Universities (No.JUSRP51622A). This study was also supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE2020 (POCI-01–0145-FEDER-006684) and BioTecNorteoperation (NORTE-01–0145-FEDER-000004) fundedb y EuropeanRegional DevelopmentFund under the scope of Norte2020—Programa Operacional Regional do Norte. ...