Abstract
Enzymatic CO2 conversion offers a promising strategy for alleviating global warming and promoting renewable energy exploitation, while the high cost of cofactors is a bottleneck for large-scale applications. To address the challenge, cofactor regeneration is usually coupled with the enzymatic reaction. Meanwhile, artificial cofactors have been developed to further improve conversion efficiency and decrease cost. In this review, the methods, such as enzymatic, chemical, electrochemical, and photochemical catalysis, developed for cofactor regeneration, together with those developed artificial cofactors, were summarized and compared to offer a solution for large-scale enzymatic CO2 conversion in a sustainable way.
Highlights
Due to the rapid increase in energy demand and the excessive combustion of fossil fuels, the concentration of carbon dioxide (CO2) in the atmosphere has been increasing at an alarming rate, which causes global warming, climate change, and severe environmental issues [1]
Ji et al [12] immobilized three enzymes, i.e., formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), and alcohol dehydrogenase (ADH), in polyelectrolytedoped hollow nanofibers for methanol production from CO2, which was coupled with enzymes glutamate dehydrogenase and substrate glutamic acid for the reduction of NAD+ to NADH
The stability of immobilized enzymes was proved, and the yield of methanol was maintained after 6 cycles, demonstrating the successful combination of enzymatic CO2 conversion and NADH regeneration powered by Glucose dehydrogenase (GCDH) and further revealing a facile enzyme immobilization method
Summary
Due to the rapid increase in energy demand and the excessive combustion of fossil fuels, the concentration of carbon dioxide (CO2) in the atmosphere has been increasing at an alarming rate, which causes global warming, climate change, and severe environmental issues [1]. Ji et al [12] immobilized three enzymes, i.e., FDH, FaldDH, and ADH, in polyelectrolytedoped hollow nanofibers for methanol production from CO2, which was coupled with enzymes glutamate dehydrogenase and substrate glutamic acid for the reduction of NAD+ to NADH. Over 80% of their original productivity was retained after 11 reusing cycles, with a cumulative methanol yield up to 127%, which was promising to the practical application All these works demonstrated that GDH is an excellent candidate in the reduction of NAD+ to NADH for sustainable enzymatic CO2 conversion. The stability of immobilized enzymes was proved, and the yield of methanol was maintained after 6 cycles, demonstrating the successful combination of enzymatic CO2 conversion and NADH regeneration powered by GCDH and further revealing a facile enzyme immobilization method. TohferNefAorDe,+GtoCDNHADcoHul.dFpirostv,iditepernoovuigdhesNaAnDeHnavmirounnmt efonrtaelnlzyyfmriaetnicdcloynsvoelrusitoionn. for NAD+ re ducTtihoene, naznydmitateixchmibeitthsohdigfohr sNeAleDctHivriteygeannedraetfiofinciheanscyp.roFsuarnthdecromnosrien, tthheereendzuycmtioantic reduc otfioNnAoDf+ NtoANDA+ DisHc. oFmirspt,atitibplerovwiditehs tahneenevnizryonmmaetinctaclolynvfreiernsidolny soofluCtiOon, faocrhNieAvDin+g in sit rrsreeeaNditdddnuuAuuudcNcccDtatttiAiiioHooocnDnnnorH,omoeoafgffrpneNeNNdlgneAAeAxeintrDDDseaey+r++txaisphiotptsiirenorbecemniossftoeesfmoonnrhrfpttcsisacpgootshrsinnoboottmsldmiieennuelueuwecdcootditutiuisshivsseasiamdpttmhydvaeevaretaahnaetnhtnantdianazotgayoneneglmfo.sfipel,Aacsrsptio,nieurcdsnycouucchhdyocco.tuhaniwsocvFatne,iuisn.rotrshsIintinnthoea.snecbIetornianmolnibzftctoiyryoClarimneotsOy,ttfa,2rtet,atohhinsafecetzce,myehentnnmiheezzzvteeyyyh,immmneohngdaaeizgtt,iiiiyhncchsmiagahptirccoomrse ciossitn, gansdolautcioomnpfloerxcsoyfsatcetmororfepgreondeurcattsioepnairnatteiognr.atAinngyheonwz,ytmheateinczCymO2atriecdmuectthioond.is a promising solution for cofactor regeneration integrating enzymatic CO2 reduction
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