Publicação

The effect of high-energy environments on the structure of laccase-polymerized poly(catechol)

Ver documento

Detalhes bibliográficos
Resumo:The laccase polymerization of catechol was performed using different reactors namely a water bath (WB), an ultrasonic bath (US) and a high-pressure homogenizer (HPH). The total content of free OH and the MALDI-TOF spectra of polymers obtained demonstrated that reactions are favored in the presence of high-energy environments. Higher conversion yields and polymerization degrees (DP) were obtained after polymerization using US or HPH. Molecular dynamic simulation studies supported these findings by revealing a more open enzyme active site upon environments with high molecular agitation. The higher mass transport generated by US and HPH is the main feature responsible for a higher substrate accessibility to the enzyme which contributed to produce longer polymers.
Autores principais:Jing Su
Outros Autores:Castro, T.; Noro, Jennifer Martins; Fu, Jiajia; Wang, Qiang; Silva, C.; Cavaco-Paulo, Artur
Assunto:Catechol Polymerization Laccase Ultrasonic bath High-pressure homogenizer
Ano:2018
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso aberto
Instituição associada:Universidade do Minho
Idioma:inglês
Origem:RepositóriUM - Universidade do Minho
Descrição
Resumo:The laccase polymerization of catechol was performed using different reactors namely a water bath (WB), an ultrasonic bath (US) and a high-pressure homogenizer (HPH). The total content of free OH and the MALDI-TOF spectra of polymers obtained demonstrated that reactions are favored in the presence of high-energy environments. Higher conversion yields and polymerization degrees (DP) were obtained after polymerization using US or HPH. Molecular dynamic simulation studies supported these findings by revealing a more open enzyme active site upon environments with high molecular agitation. The higher mass transport generated by US and HPH is the main feature responsible for a higher substrate accessibility to the enzyme which contributed to produce longer polymers.