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A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors

Multi-enzyme cascade catalysis involved three types of dehydrogenase enzymes, namely, formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), alcohol dehydrogenase (ADH), and an equimolar electron donor, nicotinamide adenine dinucleotide (NADH), assisting the reaction is an interesting pat...

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Autores principales: Ahmad Rizal Lim, Fatin Nasreen, Marpani, Fauziah, Anak Dilol, Victoria Eliz, Mohamad Pauzi, Syazana, Othman, Nur Hidayati, Alias, Nur Hashimah, Nik Him, Nik Raikhan, Luo, Jianquan, Abd Rahman, Norazah
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778536/
https://www.ncbi.nlm.nih.gov/pubmed/35054554
http://dx.doi.org/10.3390/membranes12010028
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author Ahmad Rizal Lim, Fatin Nasreen
Marpani, Fauziah
Anak Dilol, Victoria Eliz
Mohamad Pauzi, Syazana
Othman, Nur Hidayati
Alias, Nur Hashimah
Nik Him, Nik Raikhan
Luo, Jianquan
Abd Rahman, Norazah
author_facet Ahmad Rizal Lim, Fatin Nasreen
Marpani, Fauziah
Anak Dilol, Victoria Eliz
Mohamad Pauzi, Syazana
Othman, Nur Hidayati
Alias, Nur Hashimah
Nik Him, Nik Raikhan
Luo, Jianquan
Abd Rahman, Norazah
author_sort Ahmad Rizal Lim, Fatin Nasreen
collection PubMed
description Multi-enzyme cascade catalysis involved three types of dehydrogenase enzymes, namely, formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), alcohol dehydrogenase (ADH), and an equimolar electron donor, nicotinamide adenine dinucleotide (NADH), assisting the reaction is an interesting pathway to reduce thermodynamically stable molecules of CO(2) from the atmosphere. The biocatalytic sequence is interesting because it operates under mild reaction conditions (low temperature and pressure) and all the enzymes are highly selective, which allows the reaction to produce three basic chemicals (formic acid, formaldehyde, and methanol) in just one pot. There are various challenges, however, in applying the enzymatic conversion of CO(2), namely, to obtain high productivity, increase reusability of the enzymes and cofactors, and to design a simple, facile, and efficient reactor setup that will sustain the multi-enzymatic cascade catalysis. This review reports on enzyme-aided reactor systems that support the reduction of CO(2) to methanol. Such systems include enzyme membrane reactors, electrochemical cells, and photocatalytic reactor systems. Existing reactor setups are described, product yields and biocatalytic productivities are evaluated, and effective enzyme immobilization methods are discussed.
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spelling pubmed-87785362022-01-22 A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors Ahmad Rizal Lim, Fatin Nasreen Marpani, Fauziah Anak Dilol, Victoria Eliz Mohamad Pauzi, Syazana Othman, Nur Hidayati Alias, Nur Hashimah Nik Him, Nik Raikhan Luo, Jianquan Abd Rahman, Norazah Membranes (Basel) Review Multi-enzyme cascade catalysis involved three types of dehydrogenase enzymes, namely, formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), alcohol dehydrogenase (ADH), and an equimolar electron donor, nicotinamide adenine dinucleotide (NADH), assisting the reaction is an interesting pathway to reduce thermodynamically stable molecules of CO(2) from the atmosphere. The biocatalytic sequence is interesting because it operates under mild reaction conditions (low temperature and pressure) and all the enzymes are highly selective, which allows the reaction to produce three basic chemicals (formic acid, formaldehyde, and methanol) in just one pot. There are various challenges, however, in applying the enzymatic conversion of CO(2), namely, to obtain high productivity, increase reusability of the enzymes and cofactors, and to design a simple, facile, and efficient reactor setup that will sustain the multi-enzymatic cascade catalysis. This review reports on enzyme-aided reactor systems that support the reduction of CO(2) to methanol. Such systems include enzyme membrane reactors, electrochemical cells, and photocatalytic reactor systems. Existing reactor setups are described, product yields and biocatalytic productivities are evaluated, and effective enzyme immobilization methods are discussed. MDPI 2021-12-27 /pmc/articles/PMC8778536/ /pubmed/35054554 http://dx.doi.org/10.3390/membranes12010028 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ahmad Rizal Lim, Fatin Nasreen
Marpani, Fauziah
Anak Dilol, Victoria Eliz
Mohamad Pauzi, Syazana
Othman, Nur Hidayati
Alias, Nur Hashimah
Nik Him, Nik Raikhan
Luo, Jianquan
Abd Rahman, Norazah
A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title_full A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title_fullStr A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title_full_unstemmed A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title_short A Review on the Design and Performance of Enzyme-Aided Catalysis of Carbon Dioxide in Membrane, Electrochemical Cell and Photocatalytic Reactors
title_sort review on the design and performance of enzyme-aided catalysis of carbon dioxide in membrane, electrochemical cell and photocatalytic reactors
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778536/
https://www.ncbi.nlm.nih.gov/pubmed/35054554
http://dx.doi.org/10.3390/membranes12010028
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