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

Paper ID Volume ID Publish Year Pages File Format Full-Text
25325 43567 2007 9 PDF Available
Title
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers
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.

Keywords
Cutinase; Biocatalysis; Polyester; Polyamide 6,6; Site-directed mutagenesis
First Page Preview
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 128, Issue 4, 10 March 2007, Pages 849–857
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering