Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors
Maximizing space⁻time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (<i>R</i>)-selective a...
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MDPI AG
2019-02-01
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author | Theo Peschke Patrick Bitterwolf Silla Hansen Jannis Gasmi Kersten S. Rabe Christof M. Niemeyer |
author_facet | Theo Peschke Patrick Bitterwolf Silla Hansen Jannis Gasmi Kersten S. Rabe Christof M. Niemeyer |
author_sort | Theo Peschke |
collection | DOAJ |
description | Maximizing space⁻time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (<i>R</i>)-selective alcohol dehydrogenase from <i>Lactobacillus brevis</i> (LbADH), that was used for stereoselective reduction of 5-nitrononane-2,8-dione. The LbADH contained a genetically encoded streptavidin (STV)-binding peptide to enable self-immobilization on STV-coated surfaces. The purified enzyme was immobilized by physisorption or chemisorption as monolayers on the flow channel walls, on magnetic microbeads in a packed-bed format, or as self-assembled all-enzyme hydrogels. Moreover, a multilayer biofilm with cytosolic-expressed LbADH served as a whole-cell biocatalyst. To enable cross-platform comparison, STY values were determined for the various reactor modules. While mono- and multilayer coatings of the reactor surface led to STY < 10, higher productivity was achieved with packed-bed reactors (STY ≈ 100) and the densely packed hydrogels (STY > 450). The latter modules could be operated for prolonged times (>6 days). Given that our approach should be transferable to other enzymes, we anticipate that compartmentalized microfluidic reaction modules equipped with self-immobilizing biocatalysts would be of great utility for numerous biocatalytic and even chemo-enzymatic cascade reactions under continuous flow conditions. |
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spelling | doaj.art-1334d6dd09f84188bef0c213356ff4b92022-12-22T03:58:52ZengMDPI AGCatalysts2073-43442019-02-019216410.3390/catal9020164catal9020164Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow ReactorsTheo Peschke0Patrick Bitterwolf1Silla Hansen2Jannis Gasmi3Kersten S. Rabe4Christof M. Niemeyer5Karlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyKarlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyKarlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyKarlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyKarlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyKarlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, GermanyMaximizing space⁻time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (<i>R</i>)-selective alcohol dehydrogenase from <i>Lactobacillus brevis</i> (LbADH), that was used for stereoselective reduction of 5-nitrononane-2,8-dione. The LbADH contained a genetically encoded streptavidin (STV)-binding peptide to enable self-immobilization on STV-coated surfaces. The purified enzyme was immobilized by physisorption or chemisorption as monolayers on the flow channel walls, on magnetic microbeads in a packed-bed format, or as self-assembled all-enzyme hydrogels. Moreover, a multilayer biofilm with cytosolic-expressed LbADH served as a whole-cell biocatalyst. To enable cross-platform comparison, STY values were determined for the various reactor modules. While mono- and multilayer coatings of the reactor surface led to STY < 10, higher productivity was achieved with packed-bed reactors (STY ≈ 100) and the densely packed hydrogels (STY > 450). The latter modules could be operated for prolonged times (>6 days). Given that our approach should be transferable to other enzymes, we anticipate that compartmentalized microfluidic reaction modules equipped with self-immobilizing biocatalysts would be of great utility for numerous biocatalytic and even chemo-enzymatic cascade reactions under continuous flow conditions.https://www.mdpi.com/2073-4344/9/2/164enzymesflow biocatalysisimmobilization techniquesstereoselective reactionsbiomaterialsmicro reactors |
spellingShingle | Theo Peschke Patrick Bitterwolf Silla Hansen Jannis Gasmi Kersten S. Rabe Christof M. Niemeyer Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors Catalysts enzymes flow biocatalysis immobilization techniques stereoselective reactions biomaterials micro reactors |
title | Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors |
title_full | Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors |
title_fullStr | Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors |
title_full_unstemmed | Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors |
title_short | Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors |
title_sort | self immobilizing biocatalysts maximize space time yields in flow reactors |
topic | enzymes flow biocatalysis immobilization techniques stereoselective reactions biomaterials micro reactors |
url | https://www.mdpi.com/2073-4344/9/2/164 |
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