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

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

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 sta...

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Enhanced cutinase-catalyzed hydrolysis of polyethylene terephthalate by covalent fusion to hydrophobins.

Cutinases have shown potential for hydrolysis of the recalcitrant synthetic polymer polyethylene terephthalate (PET). We have shown previously that the rate of this hydrolysis can be enhanced by the addition of hydrophobins, small fungal proteins that can alter the physicochemical properties of surfaces. Here we have investigated whether the PET-hydrolyzing activity of a bacterial cutinase from...

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Enhanced cutinase - catalyzed hydrolysis of polyethylene terephthalate 1 by covalent fusion to hydrophobins 2 3

1Austrian Centre of Industrial Biotechnology ACIB, 8010 Graz, Austria 8 2 Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, 9 Vienna, 3430 Tulln, Austria 10 3 Microbiology Group, Research Area Biotechnology and Microbiology, Institute of Chemical 11 Engineering, Vienna University of Technology, 1060 Vienna, Austria. 12 4 Institute of Biotechnology, Uni...

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Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach.

The gene encoding a cutinase homolog, LC-cutinase, was cloned from a fosmid library of a leaf-branch compost metagenome by functional screening using tributyrin agar plates. LC-cutinase shows the highest amino acid sequence identity of 59.7% to Thermomonospora curvata lipase. It also shows the 57.4% identity to Thermobifida fusca cutinase. When LC-cutinase without a putative signal peptide was ...

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ژورنال

عنوان ژورنال: Journal of Biotechnology

سال: 2007

ISSN: 0168-1656

DOI: 10.1016/j.jbiotec.2006.12.028