PEGylation greatly enhances laccase polymerase activity

• Autor(a) principal: Su, Jing
• Data de Publicação: 2017
• Outros Autores: Noro, Jennifer Martins, Loureiro, Ana, Martins, Madalena, Azoia, Nuno G., Fu, Jiajia, Wang, Qiang, Silva, Carla, Cavaco-Paulo, Artur
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: http://hdl.handle.net/1822/58184
• topic: laccase; polyethylene glycol; polymerization; template; alcohols; enzyme catalysis; molecular dynamics; template synthesis; Science & Technology

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.