Real flue gas CO2 hydrogenation to formate by an enzymatic reactor using O2- and CO-tolerant hydrogenase and formate dehydrogenase

被引:4
作者
Cha, Jaehyun [1 ]
Lee, Jinhee [2 ]
Jeon, Byoung Wook [2 ]
Kim, Yong Hwan [2 ]
Kwon, Inchan [1 ,3 ]
机构
[1] Gwangju Inst Sci & Technol GIST, Sch Mat Sci & Engn, Gwangju, South Korea
[2] Ulsan Natl Inst Sci & Technol UNIST, Sch Energy & Chem Engn, Ulsan, South Korea
[3] Gwangju Inst Sci & Technol GIST, Res Ctr Innovat Energy & Carbon Optimized Synth Ch, Gwangju, South Korea
基金
新加坡国家研究基金会;
关键词
carbon dioxide; hydrogen; formate; flue gas; hydrogenase; formate dehydrogenase; OXYGEN-TOLERANT; REDUCTION; METHANOL;
D O I
10.3389/fbioe.2023.1265272
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
It is challenging to capture carbon dioxide (CO2), a major greenhouse gas in the atmosphere, due to its high chemical stability. One potential practical solution to eliminate CO2 is to convert CO2 into formate using hydrogen (H-2) (CO2 hydrogenation), which can be accomplished with inexpensive hydrogen from sustainable sources. While industrial flue gas could provide an adequate source of hydrogen, a suitable catalyst is needed that can tolerate other gas components, such as carbon monoxide (CO) and oxygen (O-2), potential inhibitors. Our proposed CO2 hydrogenation system uses the hydrogenase derived from Ralstonia eutropha H16 (ReSH) and formate dehydrogenase derived from Methylobacterium extorquens AM1 (MeFDH1). Both enzymes are tolerant to CO and O-2, which are typical inhibitors of metalloenzymes found in flue gas. We have successfully demonstrated that combining ReSH- and MeFDH1-immobilized resins can convert H-2 and CO2 in real flue gas to formate via a nicotinamide adenine dinucleotide-dependent cascade reaction. We anticipated that this enzyme system would enable the utilization of diverse H-2 and CO2 sources, including waste gases, biomass, and gasified plastics.
引用
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页数:8
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共 47 条
[1]   Global warming: review on driving forces and mitigation [J].
Al-Ghussain, Loiy .
ENVIRONMENTAL PROGRESS & SUSTAINABLE ENERGY, 2019, 38 (01) :13-21
[2]   Clostridium carboxidivorans Strain P7T Recombinant Formate Dehydrogenase Catalyzes Reduction of CO2 to Formate [J].
Alissandratos, Apostolos ;
Kim, Hye-Kyung ;
Matthews, Hayden ;
Hennessy, James E. ;
Philbrook, Amy ;
Easton, Christopher J. .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2013, 79 (02) :741-744
[3]   Formate dehydrogenase for CO2 utilization and its application [J].
Amao, Yutaka .
JOURNAL OF CO2 UTILIZATION, 2018, 26 :623-641
[4]   Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation [J].
Appel, Aaron M. ;
Bercaw, John E. ;
Bocarsly, Andrew B. ;
Dobbek, Holger ;
DuBois, Daniel L. ;
Dupuis, Michel ;
Ferry, James G. ;
Fujita, Etsuko ;
Hille, Russ ;
Kenis, Paul J. A. ;
Kerfeld, Cheal A. ;
Morris, Robert H. ;
Peden, Charles H. F. ;
Portis, Archie R. ;
Ragsdale, Stephen W. ;
Rauchfuss, Thomas B. ;
Reek, Joost N. H. ;
Seefeldt, Lance C. ;
Thauer, Rudolf K. ;
Waldrop, Grover L. .
CHEMICAL REVIEWS, 2013, 113 (08) :6621-6658
[5]   The Legacy of Fossil Fuels [J].
Armaroli, Nicola ;
Balzani, Vincenzo .
CHEMISTRY-AN ASIAN JOURNAL, 2011, 6 (03) :768-784
[6]   Production of formate from CO2gas under ambient conditions: towards flow-through enzyme reactors [J].
Baccour, Mohamed ;
Lamotte, Alexandra ;
Sakai, Kento ;
Dubreucq, Eric ;
Mehdi, Ahmad ;
Kano, Kenji ;
Galarneau, Anne ;
Drone, Jullien ;
Brun, Nicolas .
GREEN CHEMISTRY, 2020, 22 (12) :3727-3733
[7]   INFRARED STUDIES ON THE INTERACTION OF CARBON-MONOXIDE WITH DIVALENT NICKEL IN HYDROGENASE FROM CHROMATIUM-VINOSUM [J].
BAGLEY, KA ;
VANGARDEREN, CJ ;
CHEN, M ;
DUIN, EC ;
ALBRACHT, SPJ ;
WOODRUFF, WH .
BIOCHEMISTRY, 1994, 33 (31) :9229-9236
[8]   Recombinant Peptide Production Platform Coupled with Site-Specific Albumin Conjugation Enables a Convenient Production of Long-Acting Therapeutic Peptide [J].
Bak, Mijeong ;
Park, Junyong ;
Min, Kiyoon ;
Cho, Jinhwan ;
Seong, Jihyoun ;
Hahn, Young S. ;
Tae, Giyoong ;
Kwon, Inchan .
PHARMACEUTICS, 2020, 12 (04)
[9]   The soluble NAD+-reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH [J].
Burgdorf, T ;
van der Linden, E ;
Bernhard, M ;
Yin, QY ;
Back, JW ;
Hartog, AF ;
Muijsers, AO ;
de Koster, CG ;
Albracht, SPJ ;
Friedrich, B .
JOURNAL OF BACTERIOLOGY, 2005, 187 (09) :3122-3132
[10]   Engineered formate dehydrogenase from Chaetomium thermophilum, a promising enzymatic solution for biotechnical CO2 fixation [J].
Cakar, Mehmet M. ;
Ruupunen, Jouni ;
Mangas-Sanchez, Juan ;
Birmingham, William R. ;
Yildirim, Deniz ;
Turunen, Ossi ;
Turner, Nicholas J. ;
Valjakka, Jarkko ;
Binay, Baris .
BIOTECHNOLOGY LETTERS, 2020, 42 (11) :2251-2262