Exploring PEGylated and immobilized laccases for catechol polymerization

摘要

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 freeative, free/PEGylated, immobilizedative 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.Electronic supplementary materialThe online version of this article (10.1186/s13568-018-0665-5) contains supplementary material, which is available to authorized users.