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.
Highlights
Laccases are multicopper proteins considered as one of the most promiscuous enzymes since they can catalyze a broad spectrum of aromatic compounds and their derivatives (Strong and Claus 2011)
Aktaş and co-workers studied the kinetics of laccase polymerization reaction and confirmed that a general enzyme kinetics saturation response was observed for catechol substrate during their oxidation, which is probably due to the reduced laccase stability or to a drop in the dissolved oxygen concentration (Aktaş and Tanyolaç 2003b)
The catalytic activity decreases after immobilization due to lower mobility of the catalysts which has some molecular space occupied by the epoxy support
Summary
Laccases are multicopper proteins considered as one of the most promiscuous enzymes since they can catalyze a broad spectrum of aromatic compounds and their derivatives (Strong and Claus 2011). This makes laccases promising biocatalysts for applications in biotechnological processes, including the detoxification of industrial effluents, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization, medicine and cosmetic ingredients (Kunamneni et al 2008). Several studies have highlighted the identification of reaction products generated by the degradation of phenolic contaminants in water by laccases, lacking information about the NMR of the final structures obtained (Asadgol et al 2014; Catherine et al 2016; Majeau et al 2010; Shin-ya et al 2005)
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