Polyester hydrolysis is enhanced by a truncated esterase: Less is more |
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Authors: | Antonino Biundo Doris Ribitsch Georg Steinkellner Karl Gruber Georg M. Guebitz |
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Affiliation: | 1. Institute of Environmental Biotechnology, University of Natural Resources and Life Science (BOKU), Tulln an der Donau, Austria;2. Austrian Centre for Industrial Biotechnology (ACIB), Tulln an der Donau, Austria;3. Institute of Molecular Bioscience, University of Graz, Graz, Austria |
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Abstract: | An esterase from Clostridium botulinum (Cbotu_EstA) previously reported to hydrolyze the biodegradable polyester poly(butylene adipate‐co‐terephthalate) was redesigned to improve the hydrolysis of synthetic polyesters. Increased activity was indeed observed for del71Cbotu_EstA variant, which performed activity on the widespread polyester polyethylene terephthalate, which was not able to be attacked by the wild‐type enzyme Cbotu_EstA. Analysis of the 3D structure of the enzyme showed that removing 71 residues at the N‐terminus of the enzyme exposed a hydrophobic patch on the surface and improved sorption of hydrophobic polyesters concomitantly facilitating the access of the polymer to the active site. These results show a new route for enhancing enzyme activity for hydrolysis and modification of polyesters. |
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Keywords: | Biocatalysis Enzyme engineering Modeling Polymers Recombinant proteins |
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