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Mechanism-Based Design of Efficient PET Hydrolases.
Wei, Ren; von Haugwitz, Gerlis; Pfaff, Lara; Mican, Jan; Badenhorst, Christoffel P S; Liu, Weidong; Weber, Gert; Austin, Harry P; Bednar, David; Damborsky, Jiri; Bornscheuer, Uwe T.
Afiliação
  • Wei R; Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
  • von Haugwitz G; Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
  • Pfaff L; Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
  • Mican J; Loschmidt Laboratories, Department of Experimental Biology and RECETOX, Faculty of Science, Masaryk University, 625 00 Brno, Czech Republic.
  • Badenhorst CPS; International Clinical Research Center, St. Anne's University Hospital and Faculty of Medicine, Masaryk University, 656 91 Brno, Czech Republic.
  • Liu W; Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
  • Weber G; Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West 7th Avenue, Tianjin Airport Economic Area, Tianjin, 300308, China.
  • Austin HP; Macromolecular Crystallography, Helmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Straße 15, D-12489 Berlin, Germany.
  • Bednar D; Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
  • Damborsky J; Loschmidt Laboratories, Department of Experimental Biology and RECETOX, Faculty of Science, Masaryk University, 625 00 Brno, Czech Republic.
  • Bornscheuer UT; International Clinical Research Center, St. Anne's University Hospital and Faculty of Medicine, Masaryk University, 656 91 Brno, Czech Republic.
ACS Catal ; 12(6): 3382-3396, 2022 Mar 18.
Article em En | MEDLINE | ID: mdl-35368328
ABSTRACT
Polyethylene terephthalate (PET) is the most widespread synthetic polyester, having been utilized in textile fibers and packaging materials for beverages and food, contributing considerably to the global solid waste stream and environmental plastic pollution. While enzymatic PET recycling and upcycling have recently emerged as viable disposal methods for a circular plastic economy, only a handful of benchmark enzymes have been thoroughly described and subjected to protein engineering for improved properties over the last 16 years. By analyzing the specific material properties of PET and the reaction mechanisms in the context of interfacial biocatalysis, this Perspective identifies several limitations in current enzymatic PET degradation approaches. Unbalanced enzyme-substrate interactions, limited thermostability, and low catalytic efficiency at elevated reaction temperatures, and inhibition caused by oligomeric degradation intermediates still hamper industrial applications that require high catalytic efficiency. To overcome these limitations, successful protein engineering studies using innovative experimental and computational approaches have been published extensively in recent years in this thriving research field and are summarized and discussed in detail here. The acquired knowledge and experience will be applied in the near future to address plastic waste contributed by other mass-produced polymer types (e.g., polyamides and polyurethanes) that should also be properly disposed by biotechnological approaches.

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2022 Tipo de documento: Article