Title |
Exploring PEGylated and immobilized laccases for catechol polymerization
|
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Published in |
AMB Express, August 2018
|
DOI | 10.1186/s13568-018-0665-5 |
Pubmed ID | |
Authors |
Jing Su, Jennifer Noro, Jiajia Fu, Qiang Wang, Carla Silva, Artur Cavaco-Paulo |
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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Mendeley readers
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Student > Master | 5 | 20% |
Student > Ph. D. Student | 3 | 12% |
Student > Bachelor | 2 | 8% |
Researcher | 2 | 8% |
Other | 1 | 4% |
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Materials Science | 1 | 4% |
Other | 1 | 4% |
Unknown | 10 | 40% |