Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/55732

TitleExploring PEGylated and immobilized laccases for catechol polymerization
Author(s)Jing Su
Noro, Jennifer Martins
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
KeywordsLaccase
Polyethylene glycol
Immobilization
PEGylation
Polymerization
Issue dateDec-2018
PublisherSpringer
JournalAMB Express
CitationJing Su; Jennifer Noro; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur, Exploring PEGylated and immobilized laccases for catechol polymerization. AMB Express, 8(1), 134, 2018. doi: 10.1186/s13568-018-0665-5
Abstract(s)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.
TypeArticle
URIhttp://hdl.handle.net/1822/55732
DOI10.1186/s13568-018-0665-5
ISSN2191-0855
e-ISSN2191-0855
Publisher versionhttp://amb-express.springeropen.com/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

Files in This Item:
File Description SizeFormat 
document_48918_1.pdf1,86 MBAdobe PDFView/Open

Partilhe no FacebookPartilhe no TwitterPartilhe no DeliciousPartilhe no LinkedInPartilhe no DiggAdicionar ao Google BookmarksPartilhe no MySpacePartilhe no Orkut
Exporte no formato BibTex mendeley Exporte no formato Endnote Adicione ao seu ORCID