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Surface engineering of polyester-degrading enzymes to improve efficiency and tune specificity

Journal

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 102, Issue 8, Pages 3551-3559

Publisher

SPRINGER
DOI: 10.1007/s00253-018-8850-7

Keywords

Carboxylesterases; Polyesters; Enzyme engineering; Hydrolysis; PET; Polyesterases

Funding

  1. Federal Ministry of Science, Research and Economy (BMWFW)
  2. Federal Ministry of Traffic, Innovation and Technology
  3. Styrian Business Promotion Agency
  4. Standortagentur Tirol
  5. Government of Lower Austria
  6. ZIT - Technology Agency of the City of Vienna through the COMET-Funding Program

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Certain members of the carboxylesterase superfamily can act at the interface between water and water-insoluble substrates. However, nonnatural bulky polyesters usually are not efficiently hydrolyzed. In the recent years, the potential of enzyme engineering to improve hydrolysis of synthetic polyesters has been demonstrated. Regions on the enzyme surface have been modified by using site-directed mutagenesis in order to tune sorption processes through increased hydrophobicity of the enzyme surface. Such modifications can involve specific amino acid substitutions, addition of binding modules, or truncation of entire domains improving sorption properties and/or dynamics of the enzyme. In this review, we provide a comprehensive overview on different strategies developed in the recent years for enzyme surface engineering to improve the activity of polyester-hydrolyzing enzymes.

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