Detalhes bibliográficos
| Resumo: | 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. |
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| Autores principais: | Su, Jing |
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| Outros Autores: | Noro, Jennifer Martins; Loureiro, Ana; Martins, Madalena; Azoia, Nuno G.; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur |
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| Assunto: | laccase polyethylene glycol polymerization template alcohols enzyme catalysis molecular dynamics template synthesis |
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| Ano: | 2017 |
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| País: | Portugal |
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| Tipo de documento: | artigo |
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| Tipo de acesso: | acesso aberto |
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| Instituição associada: | Universidade do Minho |
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| Idioma: | inglês |
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| Origem: | RepositóriUM - Universidade do Minho |
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