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Exploring PEGylated and immobilized laccases for catechol polymerization.

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.

SUBMITTER: Su J

PROVIDER: S-EPMC6104406 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Exploring PEGylated and immobilized laccases for catechol polymerization.

Su Jing J Noro Jennifer J Fu Jiajia J Wang Qiang Q Silva Carla C Cavaco-Paulo Artur A

AMB Express 20180822 1

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 spec ...[more]

PMID: 30136217

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