Exploring PEGylated and immobilized laccases for catechol polymerization

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.This study was supported by Chinese Government Scholarship under China Scholarship Council (No. 201606790036) and Chinese Foundation Key projects of governmental cooperation in international scientific and technological innovation (No. 2016 YFE0115700) and by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI‑01‑0145‑FEDER‑006684) and BioTecNorte operation (NORTE‑01‑0145‑FEDER‑000004) funded by European Regional Development Fund under the scope of Norte2020—Programa Oper‑ acional Regional do Norte. Jennifer Noro also thanks to FCT‑ Fundação para a Ciência e a Tecnologia for funding her scholarship (SFRH/BD/121673/2016). Carla Silva is an investigator FCT (SFRH/IF/00186/2015).info:eu-repo/semantics/publishedVersio