4.6 Article

Polyester hydrolysis is enhanced by a truncated esterase: Less is more

期刊

BIOTECHNOLOGY JOURNAL
卷 12, 期 8, 页码 -

出版社

WILEY-V C H VERLAG GMBH
DOI: 10.1002/biot.201600450

关键词

Biocatalysis; Enzyme engineering; Modeling; Polymers; Recombinant proteins

资金

  1. European Union [289253, 641942]
  2. Federal Ministry of Science, Research and Economy (BMWFW)
  3. Federal Ministry of Traffic, Innovation and Technology (bmvit)
  4. Styrian Business Promotion Agency SFG
  5. Standortagentur Tirol
  6. Government of Lower Austria
  7. ZIT - Technology Agency of the City of Vienna through the COMET
  8. H2020 Societal Challenges Programme [641942] Funding Source: H2020 Societal Challenges Programme

向作者/读者索取更多资源

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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