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  1. Artikel: Improved strategies for electrochemical 1,4-NAD(P)H2 regeneration: A new era of bioreactors for industrial biocatalysis

    Morrison, Clifford S / William B. Armiger / David R. Dodds / Jonathan S. Dordick / Mattheos A.G. Koffas

    Biotechnology advances. 2018 Jan., Feb., v. 36, no. 1

    2018  

    Abstract: Industrial enzymatic reactions requiring 1,4-NAD(P)H2 to perform redox transformations often require convoluted coupled enzyme regeneration systems to regenerate 1,4-NAD(P)H2 from NAD(P) and recycle the cofactor for as many turnovers as possible. Renewed ...

    Abstract Industrial enzymatic reactions requiring 1,4-NAD(P)H2 to perform redox transformations often require convoluted coupled enzyme regeneration systems to regenerate 1,4-NAD(P)H2 from NAD(P) and recycle the cofactor for as many turnovers as possible. Renewed interest in recycling the cofactor via electrochemical means is motivated by the low cost of performing electrochemical reactions, easy monitoring of the reaction progress, and straightforward product recovery. However, electrochemical cofactor regeneration methods invariably produce adventitious reduced cofactor side products which result in unproductive loss of input NAD(P). We review various literature strategies for mitigating adventitious product formation by electrochemical cofactor regeneration systems, and offer insight as to how a successful electrochemical bioreactor system could be constructed to engineer efficient 1,4-NAD(P)H2-dependent enzyme reactions of interest to the industrial biocatalysis community.
    Schlagwörter NAD (coenzyme) ; biocatalysis ; bioreactors ; electrochemistry ; enzymatic reactions ; hydrogen ; monitoring
    Sprache Englisch
    Erscheinungsverlauf 2018-01
    Umfang p. 120-131.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 47165-3
    ISSN 0734-9750
    ISSN 0734-9750
    DOI 10.1016/j.biotechadv.2017.10.003
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel ; Online: Improved strategies for electrochemical 1,4-NAD(P)H

    Morrison, Clifford S / Armiger, William B / Dodds, David R / Dordick, Jonathan S / Koffas, Mattheos A G

    Biotechnology advances

    2017  Band 36, Heft 1, Seite(n) 120–131

    Abstract: Industrial enzymatic reactions requiring 1,4-NAD(P) ... ...

    Abstract Industrial enzymatic reactions requiring 1,4-NAD(P)H
    Mesh-Begriff(e) Biocatalysis ; Bioreactors ; Electrochemical Techniques ; NAD/metabolism ; NADP/metabolism ; Oxidation-Reduction ; Oxidoreductases
    Chemische Substanzen NAD (0U46U6E8UK) ; NADP (53-59-8) ; Oxidoreductases (EC 1.-)
    Sprache Englisch
    Erscheinungsdatum 2017-10-10
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 47165-3
    ISSN 1873-1899 ; 0734-9750
    ISSN (online) 1873-1899
    ISSN 0734-9750
    DOI 10.1016/j.biotechadv.2017.10.003
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3730: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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    ab Jg. 2022: Lesesaal (EG)

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  3. Artikel ; Online: Improved soluble expression and use of recombinant human renalase.

    Morrison, Clifford S / Paskaleva, Elena E / Rios, Marvin A / Beusse, Thomas R / Blair, Elaina M / Lin, Lucy Q / Hu, James R / Gorby, Aidan H / Dodds, David R / Armiger, William B / Dordick, Jonathan S / Koffas, Mattheos A G

    PloS one

    2020  Band 15, Heft 11, Seite(n) e0242109

    Abstract: Electrochemical bioreactor systems have enjoyed significant attention in the past few decades, particularly because of their applications to biobatteries, artificial photosynthetic systems, and microbial electrosynthesis. A key opportunity with ... ...

    Abstract Electrochemical bioreactor systems have enjoyed significant attention in the past few decades, particularly because of their applications to biobatteries, artificial photosynthetic systems, and microbial electrosynthesis. A key opportunity with electrochemical bioreactors is the ability to employ cofactor regeneration strategies critical in oxidative and reductive enzymatic and cell-based biotransformations. Electrochemical cofactor regeneration presents several advantages over other current cofactor regeneration systems, such as chemoenzymatic multi-enzyme reactions, because there is no need for a sacrificial substrate and a recycling enzyme. Additionally, process monitoring is simpler and downstream processing is less costly. However, the direct electrochemical reduction of NAD(P)+ on a cathode may produce adventitious side products, including isomers of NAD(P)H that can act as potent competitive inhibitors to NAD(P)H-requiring enzymes such as dehydrogenases. To overcome this limitation, we examined how nature addresses the adventitious formation of isomers of NAD(P)H. Specifically, renalases are enzymes that catalyze the oxidation of 1,2- and 1,6-NAD(P)H to NAD(P)+, yielding an effective recycling of unproductive NAD(P)H isomers. We designed several mutants of recombinant human renalase isoform 1 (rhRen1), expressed them in E. coli BL21(DE3) to enhance protein solubility, and evaluated the activity profiles of the renalase variants against NAD(P)H isomers. The potential for rhRen1 to be employed in engineering applications was then assessed in view of the enzyme's stability upon immobilization. Finally, comparative modeling was performed to assess the underlying reasons for the enhanced solubility and activity of the mutant enzymes.
    Mesh-Begriff(e) Enzyme Stability ; Escherichia coli ; Humans ; Industrial Microbiology/methods ; Monoamine Oxidase/chemistry ; Monoamine Oxidase/genetics ; Monoamine Oxidase/metabolism ; Mutation ; NADP/metabolism ; Protein Domains ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Solubility ; Static Electricity
    Chemische Substanzen Recombinant Proteins ; NADP (53-59-8) ; Monoamine Oxidase (EC 1.4.3.4) ; renalase (EC 1.4.3.4.)
    Sprache Englisch
    Erscheinungsdatum 2020-11-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0242109
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: Rapid, quantitative, solvent-free synthesis of medium-ring diaza heterocycles from diketene–acetone adduct and diamines

    Morrison, Clifford S / Jana B. Lampe / Robby A. Petros / Ronaldo J. Cavazos / Tesia C. Kolodziejczyk

    Tetrahedron letters. 2014 Nov. 26, v. 55, no. 48

    2014  

    Abstract: The synthesis of medium-ring heterocycles remains a challenge largely due to unfavorable energetic factors. We are reporting syntheses of 7–9-member diaza heterocycles that go to completion in 5min, require no solvents, and are quantitative with the only ...

    Abstract The synthesis of medium-ring heterocycles remains a challenge largely due to unfavorable energetic factors. We are reporting syntheses of 7–9-member diaza heterocycles that go to completion in 5min, require no solvents, and are quantitative with the only byproducts being acetone and water. The reaction products could be isolated in pure form by simply placing the mixture under vacuum. The reaction sequence possesses many of the hallmarks of a click reaction.
    Schlagwörter acetone ; byproducts ; chemical reactions ; chemical structure ; diamines ; solvents
    Sprache Englisch
    Erscheinungsverlauf 2014-1126
    Umfang p. 6547-6549.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 204287-3
    ISSN 1873-3581 ; 0040-4039
    ISSN (online) 1873-3581
    ISSN 0040-4039
    DOI 10.1016/j.tetlet.2014.10.007
    Datenquelle NAL Katalog (AGRICOLA)

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 2837: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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    ab Jg. 2022: Lesesaal (EG)

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