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Polyester hydrolysis is enhanced by a truncated esterase: Less is more
Author(s) -
Biundo Antonino,
Ribitsch Doris,
Steinkellner Georg,
Gruber Karl,
Guebitz Georg M.
Publication year - 2017
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201600450
Subject(s) - polyester , adipate , esterase , hydrolysis , polyethylene terephthalate , cutinase , chemistry , carboxylesterase , sorption , polymer chemistry , enzyme , organic chemistry , materials science , adsorption , composite material
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.