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

期刊

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 102, 期 8, 页码 3551-3559

出版社

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

关键词

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

资金

  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

向作者/读者索取更多资源

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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