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Herein, we report for the first time that a previous PEGylation of laccase enhances the polymerase activity 3\u2010fold compared with the reaction of the native enzyme, as confirmed by UV\/Vis spectroscopy. The polymerization of catechol increased only 1.5\u2010fold if poly(ethylene glycol) (PEG) was added to the medium reaction. Molecular\u2010dynamics 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.<\/jats:p>","DOI":"10.1002\/cctc.201700849","type":"journal-article","created":{"date-parts":[[2017,6,22]],"date-time":"2017-06-22T09:42:37Z","timestamp":1498124557000},"page":"3888-3894","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["PEGylation Greatly Enhances Laccase Polymerase Activity"],"prefix":"10.1002","volume":"9","author":[{"given":"Jing","family":"Su","sequence":"first","affiliation":[{"name":"International Joint Research Laboratory for Textile and Fiber Bioprocesses Jiangnan University  Wuxi 214122 China"},{"name":"Centre of Biological Engineering University of Minho, Campus de Gualtar  4710-057 Braga Portugal"}]},{"given":"Jennifer","family":"Noro","sequence":"additional","affiliation":[{"name":"Centre of Biological Engineering University of Minho, Campus de Gualtar  4710-057 Braga 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