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Surface engineering of polyester-degrading enzymes to improve efficiency and tune specificity.
Biundo, Antonino; Ribitsch, Doris; Guebitz, Georg M.
  • Biundo A; Austrian Centre of Industrial Biotechnology (ACIB), Tulln an der Donau, Austria.
  • Ribitsch D; Austrian Centre of Industrial Biotechnology (ACIB), Tulln an der Donau, Austria. doris.ribitsch@acib.at.
  • Guebitz GM; Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences (BOKU), Tulln an der Donau, Austria. doris.ribitsch@acib.at.
Appl Microbiol Biotechnol ; 102(8): 3551-3559, 2018 Apr.
Article en En | MEDLINE | ID: mdl-29511846
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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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Bacterias / Carboxilesterasa Idioma: En Año: 2018 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Bacterias / Carboxilesterasa Idioma: En Año: 2018 Tipo del documento: Article