Cofactor Regeneration for Enzyme-Catalysed Synthesis

Chenault, H. Keith; Simon, Ethan S.; Whitesides, G. M.

doi:10.1080/02648725.1988.10647849

Cited by 197 publications

(128 citation statements)

References 263 publications

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“…Indeed, diol product was formed for up to 4 hours indicating the effective retainment of the entrapped cofactor inside the hydrogel over 16 reactor column volumes. The obtained total turnover number of NADP(H) (TTNNADP(H)) was clearly in the economically feasible range 37 and even more then 3-fold higher than those recently reported for a self-sufficient heterogeneous biocatalyst, based on bead-bound ketoreductases with electrostatically co-immobilized NAD(P)H 38,39 . To the best of our knowledge, the TTNNADP(H) of >3400 observed here is the highest value ever reported for flow processes in devices lacking supportive membranes.…”

Section: Resultsmentioning

confidence: 90%

Self-assembling all-enzyme hydrogels for biocatalytic flow processes

Peschke

Gallus

Bitterwolf

et al. 2017

Preprint

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______________________________________________________________We describe the construction of binary self-assembling all-enzyme hydrogels that are comprised entirely of two tetrameric globular enzymes, the stereoselective dehydrogenase LbADH and the cofactor-regenerating glucose 1-dehydrogenase GDH. The enzymes were genetically fused with a SpyTag or SpyCatcher domain, respectively, to generate two complementary homo-tetrameric building blocks that polymerise under physiological conditions into porous hydrogels. The biocatalytic gels were used for the highly stereoselective reduction of a prochiral diketone substrate where they showed the typical behaviour of the coupled kinetics of coenzyme regenerating reactions in the substrate channelling regime. They effectively sequestrate the NADPH cofactor even under continuous flow conditions. Owing to their sticky nature, the gels can be readily mounted in simple microfluidic reactors without the need for supportive membranes. The reactors revealed extraordinary high space-time yields with nearly quantitative conversion (>95%), excellent stereoselectivity (d.r. > 99:1), and total turnover numbers of the expensive cofactor NADP(H) that are amongst the highest values ever reported. ______________________________________________________________

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Section: Resultsmentioning

confidence: 90%

Self-assembling all-enzyme hydrogels for biocatalytic flow processes

Peschke

Gallus

Bitterwolf

et al. 2017

Preprint

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“…From an industrial point of view, this would be too expensive. Hence, in situ NADPH regeneration from its oxidized counterpart (NADP + ) is required [124][125][126][127][128].…”

Section: Introductionmentioning

confidence: 99%

“…NADPH can be regenerated enzymatically by complementing the in vitro system with additional enzymatic reactions or by using substrate-coupled reaction systems. The latter system employs enzymes that use both NADP + and NADPH and that are able to catalyze the synthesis of the desired product from one substrate and cofactor regeneration with another substrate [124,130,132]. However, reduced productivity compared to systems without in situ regeneration and problems associated with enzyme stability make these options unattractive.…”

Section: Introductionmentioning

confidence: 99%

Thermococcus kodakarensis : the key to affordable biohydrogen production

Spaans¹

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“…In a six-day synthesis of D-lactate, a NADH turnover of 36,000 was reached with no loss of activity [8]. The glucose dehydrogenase from Bacillus cereus accepts either NAD + or NADP + [3]. Like FDH, the cost of glucose dehydrogenase is a disadvantage.…”

Section: Enzyme-catalyzed Regeneration Of the Cofactormentioning

confidence: 99%

“…Several substrate/enzyme couples have proved efficient. Exhaustive reviews of these techniques have already been proposed elsewhere [2,3]. The formate/formate dehydrogenase (FDH) method seems to give the best results at the moment, and large scale applications have been foreseen [4].…”

Section: Enzyme-catalyzed Regeneration Of the Cofactormentioning

confidence: 99%

Membrane electrochemical reactors (MER) for NADH regeneration in HLADH-catalysed synthesis: comparison of effectiveness

Délécouls-Servat

Bergel

Basseguy

2004

Bioprocess Biosyst Eng

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Two membrane electrochemical reactors (MER) were designed and applied to HLADH-catalysed reduction of cyclohexanone to cyclohexanol. The regeneration of the cofactor NADH was ensured electrochemically, using either methyl viologen or a rhodium complex as electrochemical mediator. A semipermeable membrane (dialysis or ultra-filtration) was integrated in the filter-press electrochemical reactor to confine the enzyme(s) as close as possible to the electrode surface. When methyl viologen was used, the transformation ratio of cyclohexanone varied from 0 to 65% depending on the internal arrangement of the reactor. Matching the reactor configuration to the reaction system was essential in this case. With the rhodium complex, the ultra-filtration MER was tested in continuous and recycling configurations. The best conditions led to 100% transformation of 0.1 L volume of 0.1 M cyclohexanone after 70 h with the recycling mode. Finally, the performances of the reactors are discussed with respect to different evaluations of the production yields.

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Cofactor Regeneration for Enzyme-Catalysed Synthesis

Cited by 197 publications

References 263 publications

Self-assembling all-enzyme hydrogels for biocatalytic flow processes

Self-assembling all-enzyme hydrogels for biocatalytic flow processes

Thermococcus kodakarensis : the key to affordable biohydrogen production

Membrane electrochemical reactors (MER) for NADH regeneration in HLADH-catalysed synthesis: comparison of effectiveness

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