Boosting the Productivity of H2-Driven Biocatalysis in a Commercial Hydrogenation Flow Reactor Using H2 From Water Electrolysis

Poznansky, Barnabas; Cleary, Sarah; Thompson, Lisa A.; Reeve, Holly A.; Vincent, Kylie A.

doi:10.3389/fceng.2021.718257

Cited by 10 publications

(12 citation statements)

References 41 publications

(51 reference statements)

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“…Multi‐walled carbon nanotubes (MWCNTs) can allow significant improvement of the efficiency of the electroenzymatic synthesis system by tuning some electrochemical properties, e. g., by enhancing the electroactive surface area [35] . On the basis of this opportunity, MWCNTs had been identified as suitable supporting materials for Rh complex immobilization [29,31] . Based on the perspective of combination between fuel cell technology and redox flow technique, a carbon paper (CP) coated with MWCNTs (noted CP‐MWCT) was chosen for the construction of the catalytic layer after comparing it with bucky paper and graphite felt electrodes.…”

Section: Resultsmentioning

confidence: 99%

“…Besides, Vincent and co‐workers have succeeded in coupling the oxidation of hydrogen to the regeneration of NADH catalyzed by hydrogenase and NAD + reductase respectively in a microflow reactor with a volume of 0.2 mL. Direct use of regenerated NADH to the bioconversion of pyruvate catalyzed by lactate dehydrogenase showed an overall lactate production of 500 g lactate g catalyst −1 and a turnover frequency of 1060 min −1 for the NAD + cofactor [29] . Because of the usage of a high amount of NAD + (1.7 mM),TTN for the NAD + cofactor was limited to 35 [29] .…”

Section: Introductionmentioning

confidence: 99%

“…[29] Because of the usage of a high amount of NAD + (1.7 mM),TTN for the NAD + cofactor was limited to 35. [29] Finally, photochemical regeneration of NADH using batch reactors was achieved, but with relatively low TTNs [30] which explains that the photochemical regeneration of NADH in a flow reactor is not yet explored. Batch regeneration of NADH using a Rh complex as mediator exhibited a turnover frequency of 0.46 h À 1 .…”

Section: Introductionmentioning

confidence: 99%

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Hybrid Flow Bioreactor with All Catalysts Immobilized for Enzymatic Electrosynthesis

et al. 2022

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The electrochemical regeneration of the reduced form of nicotinamide adenine dinucleotide cofactor (NADH) was realized in a hybrid flow reactor coupling fuel cell technology and redox flow device, paying attention to the robust immobilization of all catalysts. The rhodium catalyst Rh(Cp✶)(bpy)Cl+ was covalently immobilized on a multi‐walled carbon nanotube (MWCNT) layer and the association with the gas diffusion electrode was carefully optimized. High stability and activity of the electrochemical system were assessed by cyclic voltammetry and amperometry in the flow reactor. Afterwards, the optimal cofactor regeneration was applied to NADH‐dependent biosynthesis using immobilized lactate dehydrogenase for the conversion of pyruvate to lactate in the flow cell in the presence of cofactor concentration as low as 10 μM. 79 % Faradaic efficiency was achieved and remarkable total turnover number (TTN) were reached: 2500, 18000, and 180000, for NADH, Rh complex and L‐lactate dehydrogenase (LDH), respectively.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Hybrid Flow Bioreactor with All Catalysts Immobilized for Enzymatic Electrosynthesis

et al. 2022

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“…Additives or co-factors that improve yields, activity, and productivity [17,44]. Step 6., Reaction mode and reactor design: For example, batch, continuous, solid state or plug flow [45].…”

Section: Conclusion and Future Outlookmentioning

confidence: 99%

Evaluating Enzymatic Productivity—The Missing Link to Enzyme Utility

Siddiqui

Ertan

Poljak

et al. 2022

IJMS

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Kinetic productivity analysis is critical to the characterization of enzyme catalytic performance and capacity. However, productivity analysis has been largely overlooked in the published literature. Less than 0.01% of studies which report on enzyme characterization present productivity analysis, despite the fact that this is the only measurement method that provides a reliable indicator of potential commercial utility. Here, we argue that reporting productivity data involving native, modified, and immobilized enzymes under different reaction conditions will be of immense value in optimizing enzymatic processes, with a view to accelerating biotechnological applications. With the use of examples from wide-ranging studies, we demonstrate that productivity is a measure of critical importance to the translational and commercial use of enzymes and processes that employ them. We conclude the review by suggesting steps to maximize the productivity of enzyme catalyzed reactions.

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“…The enzymatic therapeutic strategy became more realistic after the establishment and increment of genetic engineering technologies that made possible the production of enzymes with the needed characteristics of purity, selectivity and amounts compatible with the clinical use [ 10 ]. The therapeutic potential of enzymes is very high, ranging from metabolic and inflammatory disorders, cardiac problems to even cancer [ 8 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Liposomes as Tools to Improve Therapeutic Enzyme Performance

et al. 2022

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The drugs concept has changed during the last few decades, meaning the acceptance of not only low molecular weight entities but also macromolecules as bioagent constituents of pharmaceutics. This has opened a new era for a different class of molecules, namely proteins in general and enzymes in particular. The use of enzymes as therapeutics has posed new challenges in terms of delivery and the need for appropriate carrier systems. In this review, we will focus on enzymes with therapeutic properties and their applications, listing some that reached the pharmaceutical market. Problems associated with their clinical use and nanotechnological strategies to solve some of their drawbacks (i.e., immunogenic reactions and low circulation time) will be addressed. Drug delivery systems will be discussed, with special attention being paid to liposomes, the most well-studied and suitable nanosystem for enzyme delivery in vivo. Examples of liposomal enzymatic formulations under development will be described and successful pre-clinical results of two enzymes, L-Asparaginase and Superoxide dismutase, following their association with liposomes will be extensively discussed.

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Boosting the Productivity of H2-Driven Biocatalysis in a Commercial Hydrogenation Flow Reactor Using H2 From Water Electrolysis

Cited by 10 publications

References 41 publications

Hybrid Flow Bioreactor with All Catalysts Immobilized for Enzymatic Electrosynthesis

Hybrid Flow Bioreactor with All Catalysts Immobilized for Enzymatic Electrosynthesis

Evaluating Enzymatic Productivity—The Missing Link to Enzyme Utility

Liposomes as Tools to Improve Therapeutic Enzyme Performance

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