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TitleExploring PEGylated and immobilized laccases for catechol polymerization
Author(s)Jing Su
Noro, Jennifer Martins
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
Polyethylene glycol
Issue dateDec-2018
JournalAMB Express
CitationJing Su; Jennifer Noro; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur, Exploring PEGylated and immobilized laccases for catechol polymerization. AMB Express, 8(1), 134, 2018. doi: 10.1186/s13568-018-0665-5
Abstract(s)Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV--Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced.
Publisher version
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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