Improving the Enzymatic Cascade of Reactions for the Reduction of CO2 to CH3OH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression
Abstract
:1. Introduction
- Make enzymes more robust, i.e., methods of immobilization that also facilitate enzymes recovery and recycling;
- Increase the availability of CO2 in solution either by adding specific enzymes that drive the hydration/dehydration process or by using materials capable of capturing CO2;
- In situ and non-in situ methods that allow selective regeneration of the cofactor or even reduce or eliminate the cofactor itself, using artificial cofactors or adopting a direct electron transfer.
2. The Dehydrogenases
2.1. Formate Dehydrogenase
2.2. Formaldehyde Dehydrogenase
2.3. Alcohol Dehydrogenase
3. Study of Reaction Conditions
3.1. Enzymes Immobilization and Co-Immobilization
Immobilization Matrix | Immobilized Enzymes | Note/Key Outcome | Ref. |
---|---|---|---|
SiO2 sol–gel | FateDH, FaldDH, ADH | Yield-free enzymes = 10–20% Yield-immobilized enzymes = 40–90% | [45] |
SiO2 sol–gel | FateDH, FaldDH, ADH | Yield-free enzymes = 98.1% Yield-immobilized enzymes = 92.1% | [46] |
ALG-SiO2, hybrid gel | FateDH, FaldDH, ADH | Yield-free enzymes = 98.8% Yield-immobilized enzymes = 98.1% | [47] |
PS NPs | FateDH, FaldDH, ADH | Yield-free enzymes = 12%. Yield-immobilized enzymes = 127% (80% initial activity retained after 11 cycles). Enzymatic regeneration with GDH | [48] |
Capsules-in-bead scaffold | FateDH, FaldDH, ADH | Immobilized enzymes were more active than free enzymes when a free cofactor was presented. | [49] |
Titania–protamine particles | FateDH, FaldDH, ADH | Yield-free enzymes = 5–10%. Yield immobilized enzymes = 35–60% (50% initial activity retained after 10 cycles) | [50] |
ALG-SiO2, hybrid gel | FateDH, FaldDH, ADH | Yield-immobilized enzymes = 100% (external reg.) Yield-immobilized enzymes = 80% (with in situ reg.) Chemical regeneration with SDT | [8] |
Phospholipids–silica nanocapsules | FateDH, FaldDH, ADH | Free enzymes = 0.06 mmol MeOH/genzyme. Immobilized enzymes = 0.88 mmol MeOH/genzyme Free with PtDH = 0.16 mmol MeOH/genzyme Immobilized enzyme with PtDH = 4.30 mmol MeOH/genzyme. Enzymatic regeneration with PtDH | [18] |
Hybrid microcapsules | FateDH, FaldDH, ADH | Yield free enzymes = 35.5%. Yield immobilized enzymes = 71.6% (52.6% initial activity retained after 9 cycles) | [21] |
Flat-sheet polymeric membranes | FateDH, FaldDH, ADH | Free enzymes: [MeOH] = 0.5 mM Co-immobilized enzymes: [MeOH] = 0.6 mM mMSeq-immobilized enzymes: [MeOH] = 0.7 mM Enzymatic regeneration with GDH and glutamate | [29] |
CF electrode with alginate matrix | FateDH, FaldDH, ADH | Electrochemical CO2 reduction to methanol around 0.15 ppm. Faradaic efficiencies of around 10%. No NADH but direct electron transfer | [51] |
PS nanofibrous membrane | FateDH | Free enzymes: [Formate] = 0.6 mM Immobilized enzymes: [Formate] = 0.3 mM (53% initial activity retained after 8 cycles) Electrochemical regeneration | [34] |
Magnetic NPs | FateDH, FaldDH, ADH | Stepwise scheme led to only a 2.3% yield of methanol per NADH; batch system under CO2 pressure, the combination of the four immobilized enzymes increased the methanol yield by 64-fold | [52] |
ZIF-8 entrapped in PVDF microporous asymmetric membrane | FateDH, FaldDH, ADH | Immobilized enzymes without membrane (EMS) = 5 µmol. Immobilized enzymes with membrane (ECMS) = 6 µmol. Disord. Immobilized enzymes with membrane (DEMM) = 7 µmol. Ord. Immobilized enzymes + NADH without membrane (OEMM) = 13 µmol. Ord. Immobilized enzymes + NADH with membrane (OECMM) = 14 µmol. Over 50 % of their original productivity was retained after 12 h of use | [53] |
Titania NPs | ADH | The results revealed that immobilization of enzymes led to higher catalytic. The activity of ADH from 30% to more than 80% of its initial activity after 30 days of storage at 4 °C. (84% initial activity retained after 10 cycles) | [54] |
MOF, NU-1006 | FateDH | Immobilized Enzyme + cofactor Rh: [Formic acid] = 144 mM. Photochemical regeneration with Rh complex | [55] |
Zeolite particles | FateDH | Yield imm. Enzyme = 34–37% | [56] |
MOF, ZIF-8 | FateDH | Compared with the free multienzyme system, formate yield was increased by 4.6-fold. Co-immobilized with CA and enzymatic regeneration with GDH | [57] |
Graphene + CF electrode with alginate matrix | FateDH, FaldDH, ADH | Electrochemical CO2 reduction to methanol around 20 ppm. Faradaic efficiencies of around 12%. No NADH but direct electron transfer | [58] |
MOF, ZIF-8 | FateDH, FaldDH, ADH | Free enzymes: [MeOH] = 0.061 mM. Immobilized enzymes: [MeOH] = 0.320 mM. Immobilized enzymes + NADH regeneration: [MeOH] = 0.742 mM. Electrochemical regeneration with Rh complex-grafted electrode | [59] |
MCF | FateDH, FaldDH, ADH | Catalytic activity-free enzyme systems = 0.3 mmol MeOH/genzyme min. Catalytic activity immobilized enzymes systems = 1.35 mmol MeOH/genzyme min | [60] |
Gold and graphite electrodes | FateDH | Electrochemical CO2 reduction imm. enzyme: [Formate] = 3.7 µM. Faradaic efficiencies of around 100% No NADH but direct electron transfer | [61] |
3.2. Cofactor Regeneration
3.2.1. Enzymatic Regeneration of the Cofactor
3.2.2. Chemical Regeneration of the Cofactor
3.2.3. Photochemical Regeneration
3.2.4. Electrochemical Regeneration of the Cofactor
Regeneration Method | Type of Regenerator | Yield/Key Outcome | Ref. |
---|---|---|---|
Enzymatic regeneration | GDH | YMeOH reached 127% | [48] |
Enzymatic regeneration | GDH | YMeOH reached up to 95.3% | [72] |
Enzymatic regeneration | PTDH or GlyDH | PTDH is 4 times more active than GlyDH, [CH3OH] increases from 0.1 mM without PTDH to 0.9 mM with PTDH | [18] |
Enzymatic regeneration | PTDH | The multienzymatic cascade reaction, along with PTDH, yielded 3.28 mM methanol | [64] |
Enzymatic regeneration | GCDH | Yield of methanol reached 100% after coupling GCDH regeneration | [68] |
Enzymatic regeneration | GCDH-XDH | XDH for NADH regeneration was found to be more efficient than GCDH producing at least 8 mM CH3OH yield | [65] |
Enzymatic regeneration | GDH | Yield of methanol was increased 64-folds compared to the reaction without a regeneration system | [52] |
Enzymatic regeneration | GDH | Formate yield was increased 4.6-fold compared to the reaction with free enzymes | [57] |
Photochemical regeneration | Carbon-containing TiO2/H2/[Cp*Rh(bpy)(H2O)]2+ | NADH conversion reaches 94.29% in the presence of H2 as an electron’s donor | [73] |
Photochemical regeneration | P-doped TiO2 nanoparticles/H2O/[Cp*Rh(bpy)(H2O)]2+ | If P to Ti molar ratio is 6%, TiO2 nanoparticle can photo catalytically reproduce 34.6% NADH under visible light | [74] |
Photochemical regeneration | Cobaloxime/TEOA /eosin | NADH conversion reaches a yield of 36% | [75] |
Photochemical regeneration | CCG-IP/TEOA/[Cp*Rh(bpy)(H2O)]2+ | NADH conversion reaches a yield of 38.99% (first cycle) and 36.81% (third cycle) | [76] |
Photochemical regeneration | CrF5(H2O)]2−@TiO2/Water-Glycerol/[Cp*Rh(bpy)H2O]Cl2 | NADH conversion reaches the maximum yield (very close to 100%) | [67] |
Photochemical regeneration | TiO2/EDTA/[Cp*Rh(bpy)(H2O)]2+ | In the presence of 1.5 mg/mL TiO2, the NADH yield reached approximately 90% after 30 min of irradiation | [62] |
Photochemical regeneration | ATCN-DSCN/TEOA/[Cp*Rh(bpy)H2O]2+ | NADH yield of ~74% | [77] |
Photochemical regeneration | Ionic porphyrin (ZnTPyPBr)/TEOA/[Cp*Rh(bpy)(H2O)]2+ | Yield of NADH increase by 17.9% after 1 h, a seven-fold increase in methanol concentration | [68] |
Photochemical regeneration | TiO2/H2O/[Cp*Rh(bpy)(H2O)]2+ | Yield of NADH conversion 45.54% (after 2 h) | [78] |
Electrochemical regeneration | carbon nanofibers cathode | Yield ~ 99% pure 1,4-NADH | [79] |
Electrochemical regeneration | Cu nanorods on glassy carbon | 1,4-NADH conversion yield reaches 67%/with electron mediator [Cp*Rh(bpy)Cl]Cl complex reaches almost 100% | [69] |
Electrochemical regeneration | Ni NP-MWCNT cathode | Yield ~ 98% pure 1,4-NADH | [80] |
Electrochemical regeneration | Cu foam electrode | NADH conversion yield reaches 93–99% 1,4-NADH (active isomer): 75–79% | [34] |
Electrochemical regeneration | DH/Cc-PAA biocathode | Bioactive 1,4-NADH yield: 97–100% Faradaic efficiencies: 78–99% | [70] |
Electrochemical regeneration | Rh modified electrode | NADH conversion yield reaches more than 90% in 20 min | [81] |
Electrochemical regeneration | CuNPS on carbon felt electrode | NADH regeneration yield achieves a maximum of 92.1% | [82] |
Electrochemical regeneration | Rh complex-grafted electrode | Yield NADH ~ 80% 1,4-NADH reaches almost 100% | [59] |
3.3. Cofactor Substitution
3.4. Cofactor Free Use of the Cascade f Reactions
3.5. Coupling of Immobilization and Regeneration Methods: The Results
4. Conclusions and Future Perspectives
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
Abbreviations
References
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Di Spiridione, C.; Aresta, M.; Dibenedetto, A. Improving the Enzymatic Cascade of Reactions for the Reduction of CO2 to CH3OH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression. Molecules 2022, 27, 4913. https://doi.org/10.3390/molecules27154913
Di Spiridione C, Aresta M, Dibenedetto A. Improving the Enzymatic Cascade of Reactions for the Reduction of CO2 to CH3OH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression. Molecules. 2022; 27(15):4913. https://doi.org/10.3390/molecules27154913
Chicago/Turabian StyleDi Spiridione, Carmela, Michele Aresta, and Angela Dibenedetto. 2022. "Improving the Enzymatic Cascade of Reactions for the Reduction of CO2 to CH3OH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression" Molecules 27, no. 15: 4913. https://doi.org/10.3390/molecules27154913