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Exploring PEGylated and immobilized laccases for catechol polymerization
Jing Su1,2, Jennifer Noro2, Jiajia Fu1
1International Joint Research Laboratory for Textile and Fiber Bioprocesses, Jiangnan University, Wuxi, 214122, China.
Abstract:
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.
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