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Selected Publication:

Biundo, A; Ribitsch, D; Steinkellner, G; Gruber, K; Guebitz, GM; .
(2017): Polyester hydrolysis is enhanced by a truncated esterase: Less is more.
Biotechnol J. 2017; 12(8): FullText FullText_BOKU

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.
Authors BOKU Wien:
Biundo Antonino
G├╝bitz Georg
Ribitsch Doris
Find related publications in this database (using NML MeSH Indexing)
Biodegradable Plastics/chemistry*;Biodegradation, Environmental*;Catalytic Domain/drug effects;Clostridium botulinum/chemistry;Clostridium botulinum/enzymology;Esterases/chemistry*;Esterases/metabolism;Hydrolysis;Molecular Conformation*;Polyesters/chemistry;Polyethylene Terephthalates/chemistry;

Find related publications in this database (Keywords)
Enzyme engineering
Recombinant proteins

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