Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers

Rita Araújo, Carla Silva, Alexandre O'Neill, Nuno Micaelo, Georg Guebitz, Cláudio M. Soares, Margarida Casal, Artur Cavaco-Paulo

Research output: Contribution to journalArticle

103 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)849-857
Number of pages9
JournalJournal of Biotechnology
Volume128
Issue number4
DOIs
Publication statusPublished - 10 Mar 2007

Keywords

  • Biocatalysis
  • Cutinase
  • Polyamide 6,6
  • Polyester
  • Site-directed mutagenesis

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