Document details

Exploring PEGylated and immobilized laccases for catechol polymerization

Author(s): Jing Su ; Noro, Jennifer Martins ; Fu, Jiajia ; Wang, Qiang ; Silva, Carla ; Cavaco-Paulo, Artur

Date: 2018

Persistent ID: https://hdl.handle.net/1822/55732

Origin: RepositóriUM - Universidade do Minho

Subject(s): Laccase; Polyethylene glycol; Immobilization; PEGylation; Polymerization


Description

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.

Document Type Journal article
Language English
Contributor(s) Universidade do Minho
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