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ACS Synthetic biology v.6 no.1, 2017년, pp.19 - 28   SCIE
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Affibody Scaffolds Improve Sesquiterpene Production in Saccharomyces cerevisiae

Tippmann, Stefan (Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, ); Anfelt, Josefine ( Division of Proteomics and Nanobiotechnology, School of Biotechnology, Royal Institute of Technology (KTH), Science for Life Laboratory, SE171 21 Stockholm, ); David, Florian ( Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, ); Rand, Jacqueline M. ( Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, ); Siewers, Verena ( Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, ); Uhlé ( Division of Proteomics and Nanobiotechnology, School of Biotechnology, Royal Institute of Technology (KTH), Science for Life Laboratory, SE171 21 Stockholm, ); n, Mathias ( Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, ); Nielsen, Jens ( Division of Proteomics and Nanobiotechnology, School of Biotechnology, Royal Institute of Technology (KTH), Science for Life Laboratory, SE171 ); Hudson, Elton P. ( );
  • 초록  

    Enzyme fusions have been widely used as a tool in metabolic engineering to increase pathway efficiency by reducing substrate loss and accumulation of toxic intermediates. Alternatively, enzymes can be colocalized through attachment to a synthetic scaffold via noncovalent interactions. Here we describe the use of affibodies for enzyme tagging and scaffolding. The scaffolding is based on the recognition of affibodies to their anti-idiotypic partners in vivo , and was first employed for colocalization of farnesyl diphosphate synthase and farnesene synthase in S.?cerevisiae . Different parameters were modulated to improve the system, and the enzyme:scaffold ratio was most critical for its functionality. Ultimately, the yield of farnesene on glucose Y SFar could be improved by 135% in fed-batch cultivations using a 2-site affibody scaffold. The scaffolding strategy was then extended to a three-enzyme polyhydroxybutyrate (PHB) pathway, heterologously expressed in E.?coli . Within a narrow range of enzyme and scaffold induction, the affibody tagging and scaffolding increased PHB production 7-fold. This work demonstrates how the versatile affibody can be used for metabolic engineering purposes. Graphic Abstract ACS Electronic Supporting Info


  • 주제어

    affibodies .   isoprenoids .   biofuels .   PHB .   yeast .   metabolic engineering.  

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