Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/13134

TitleTailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers
Author(s)Araújo, Rita
Silva, Carla Manuela Pereira Marinho da
O'Neill, Jaime Alexandre Antunes
Micaelo, N. M.
Gübitz, Georg M.
Soares, Cláudio M.
Casal, Margarida
Paulo, Artur Cavaco
KeywordsCutinase
Polyester
Polyamide 6,6
Site-directed mutagenesis
Biocatalysis
Issue dateMar-2007
PublisherElsevier
JournalJournal of Biotechnology
Abstract(s)Cutinase from Fusarium solani pisi was genetically modified near the active site, by site-directed mutagenesis, to enhance its activity towards polyethylene terephthalate (PET) and polyamide 6,6 (PA 6,6) fibers. The mutations L81A, N84A, L182A, V184A and L189A were done to enlarge the active site in order to better fit a larger polymer chain. Modeling studies have shown enhanced free energy stabilization of model substrate tetrahedral intermediate (TI) bound at the enzyme active site for all mutants, for both model polymers. L81A and L182A showed an activity increase of four- and five-fold, respectively, when compared with the wild type, for PET fibers. L182A showed the one- and two-fold higher ability to biodegrade aliphatic polyamide substrates. Further studies in aliphatic polyesters seem to indicate that cutinase has higher ability to recognize aliphatic substrates.
TypeArticle
URIhttp://hdl.handle.net/1822/13134
DOI10.1016/j.jbiotec.2006.12.028
ISSN0168-1656
Publisher versionhttp://www.sciencedirect.com/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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