FP7Individual fellowship2013–2015

ELECTROENZEQUEST · BioElectrochemical system for Enzyme catalyzed CO2 sEquestration for the recovery of commercially viable carbonated water and methanol

FP7 — People (Marie Curie Actions)

Duration
2013-05-01 → 2015-04-30
EU contribution
€177,000
Participants
1
Scheme
MC-IIF

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Results in brief

BioElectrochemical system for Enzyme catalyzed CO2 sEquestration for the recovery of commercially viable carbonated water and methanol

The current marie-curie project (ELECTROENZEQUEST) was proposed for the CO2 reduction into methanol using dehydrogenases as cascade on electrode of bioelectrochemical system. Brief objectives include • Immobilization of carbonic anhydrase (CA) on to the electrode and evaluation of its function as anode for electrogenesis in the fuel cell • Bio-electrochemical characterization of the immobilized-CA electrode and optimization of various factors influencing the functional role of CA in CO2 sequestration associated with electrogenesis • Immobilization of Formate dehydrogenase (Fate DH), formaldehyde dehydrogenase (Fald DH) and alcohol dehydrogenase (Alc DH) on an electrode and its introduction as cathode in the operating CA fuel cell • Optimization of factors affecting the fuel cell performance including the functional role of mediators such as NAD+, PQQ, etc., in mediating the electron transfer from the electrode to the substrate and in the conversion of CO2 to methanol during cathodic reduction • The bioprocess during fuel cell operation will be evaluated under optimum conditions for maximum product recovery with lowest possible energy inputs Starting with these objectives, the project was completed successfully with all the objectives. Initially, we tried to study the feasibility of conversion of CO2 into formic acid, using FateDH in free form. After analyzing the results of the first experiment, we tried to immobilize the enzyme onto electrode FateDH. After several trials, we could successfully immobilize the enzyme onto graphite based VITO-CoRETM electrode. Then, we started working on immobilization of CA along with FateDH on same electrode to increase the formic acid productivity and CO2 reduction. Further to that, we immobilized all three enzymes on a single electrode for production of methanol and CA was also added at later stage to increase the productivity. Detailed analysis of each experiment was done in comparison with controls. Immobilization in each experiment was done as follows » TBAB Modified Nafion solution was prepared for e- transfer instead of H+ transfer » Electrode to be immobilized was taken and NR was polymerized on it » Known quantity of Enzyme (one or two) was dissolved in 100 µl of PBS (pH 7,4) in an eppendorf » Added with 50 µl of modified Nafion solution . Gently vertex for 5-10 sec » Place the electrode in a petri plate and pipette out the enzyme-nafion mixture on to the electrode and let it air dried » 100 mM NaNO3 was poured on it after getting dried for equilibration Different experiments were carried out using single enzyme and multiple enzymes. All the results were consolidated and presented as a Table 1 and the Research highlights are as follows • Higher current densities due to the use of VITO based electrodes • Co-factor recycling was achieved without any secondary system • Immobilization brought stability in current densities • Conversion efficiencies based on enzyme activity are good, However, the CO2 supply can be reduced to increase the conversion rate • CA addition helped a lot in increasing the reaction rates. Solubilized CO2 can react more with the enzyme to form high product titre • Specific activities of enzyme before and after the experiment weren’t changed, which indicates the possibility of increasing the reaction time to get more product. Further experiments were continued with three enzymes (FateDH, FaldDH and AlcDH) together on the electrode, where we have observed the ethanol production from CO2 at a rate of 0.6 kg/m3/h. However, when we excluded the FaldDH also, there is no reduction in productivity of ethanol. It was surprising that we got ethanol instead of methanol but based on literature, it is also possible for the production of ethanol directly from formic acid, which is economically more viable. Further research is going on at host organization in this direction.

Data: CORDIS, © European Union

Project objective

Increasing energy demand and depleting fossils has put forward the necessity of searching alternatives. Recently, bioelectricity production through bioelectrochemical systems (BES) has gained prominence in the recent bioenergy scenario due to its sustainable nature. BES is electrochemical devices that convert chemical energy to electricity using biochemical pathways and redox enzymes. Enzymatic fuel cells works with the help of purified enzymes to catalyze the oxidation of fuel at the anode and reduction of the electron acceptor at cathode. Numerous chemical transformations are reported to be catalyzed by redox-active enzymes including both the reduction and oxidation of substrates. However, all these enzymes require pure substrates for their function which is not economic for large scale applications. In the present study, carbon dioxide (CO2) is considered as substrate for both anodic oxidation as well as cathodic reduction that yield carbonated water and methanol respectively. The proposed work signifies the importance of CO2 sequestration in the present scenario of environmental pollution problems such as global warming as well as need of alternative biofuels. The work plan will investigate the feasibility and mechanisms of atmospheric CO2 sequestration through enzyme-cocktails (multiple enzymes at once) at anodic oxidation process to harness bioelectricity along with the carbonated water, having multiple applications, and cathodic reduction for the synthesis of methanol, without using external energy. Carbonic anhydrase (CA) will be used as anodic biocatalyst for sequestering CO2 to generate carbonated water along with generation of protons (H+) and electrons (e-). On the other hand, three enzymes, viz., Formate dehydrogenase (Fate DH), formaldehyde dehydrogenase (Fald DH) and alcohol dehydrogenase (Alc DH), individually and in combination at cathode as terminal electron acceptor for the reduction of H+ and e- coming from anode converting CO2 into methanol.""

Original text from CORDIS.

Participants

  • VLAAMSE INSTELLING VOOR TECHNOLOGISCH ONDERZOEK N.V. · MolCoordinatorBelgium

Links

Data: CORDIS, © European Union