TY - JOUR
T1 - Biological conversion of methane to methanol
AU - Park, Donghyun
AU - Lee, Jeewon
N1 - Funding Information:
This study was supported by the 2012 NLRL (National Leading Research Lab.) Project (grant no. 2012R1A2A1A01008085) (the main project that supported this work) and the Basic Science Research Program (ERC program, grant no. 2010-0029409) of the National Research Foundation of Korea (NRF).
PY - 2013/5
Y1 - 2013/5
N2 - The conversion of methane to methanol is important to economic utilization of natural/shale gas. Methanol is a valuable liquid fuel and raw material for various synthetic hydrocarbon products. Its industrial production is currently based on a two-step process that is energy-intensive and environmentally unfriendly, requiring high pressure and temperature. The biological oxidation of methane to methanol, based on methane monooxygenase activity of methanotrophic bacteria, is desirable because the oxidation is highly selective under mild conditions, but conversion rate and yield and stability of catalytic activity should be improved up to an industrially viable level. Since methanotrophic bacteria produce methanol as only a precursor of formaldehyde that is then used to synthesize various essential metabolites, the direct use of bacteria seems unsuitable for selective production of a large amount of methanol. There are two types of methane monooxygenase: soluble (sMMO) and particulate (pMMO) enzyme. sMMO consisting of three components (reductase, hydroxylase, and regulatory protein) features an (αβγ)2 dimer architecture with a di-iron active site in hydroxlase. pMMO, a trimer (pmoA, pmoB, and pmoC) in an α3β3γ3 polypeptide arrangement is a copper enzyme with a di-copper active site located in the soluble domain of pmoB subunit. Since the membrane transports electrons well and delivers effectively methane with increased solubility in the lipid bilayer, pMMO seems more rationally designed enzyme in nature than sMMO. The engineering/evolution/modification of MMO enzymes using various biological and chemical techniques could lead to an optimal way to reach the ultimate goal of technically and economically feasible and environmentally friendly oxidation of methane. For this, multidisciplinary efforts from chemical engineering, protein engineering, and bioprocess research sectors should be systematically combined.
AB - The conversion of methane to methanol is important to economic utilization of natural/shale gas. Methanol is a valuable liquid fuel and raw material for various synthetic hydrocarbon products. Its industrial production is currently based on a two-step process that is energy-intensive and environmentally unfriendly, requiring high pressure and temperature. The biological oxidation of methane to methanol, based on methane monooxygenase activity of methanotrophic bacteria, is desirable because the oxidation is highly selective under mild conditions, but conversion rate and yield and stability of catalytic activity should be improved up to an industrially viable level. Since methanotrophic bacteria produce methanol as only a precursor of formaldehyde that is then used to synthesize various essential metabolites, the direct use of bacteria seems unsuitable for selective production of a large amount of methanol. There are two types of methane monooxygenase: soluble (sMMO) and particulate (pMMO) enzyme. sMMO consisting of three components (reductase, hydroxylase, and regulatory protein) features an (αβγ)2 dimer architecture with a di-iron active site in hydroxlase. pMMO, a trimer (pmoA, pmoB, and pmoC) in an α3β3γ3 polypeptide arrangement is a copper enzyme with a di-copper active site located in the soluble domain of pmoB subunit. Since the membrane transports electrons well and delivers effectively methane with increased solubility in the lipid bilayer, pMMO seems more rationally designed enzyme in nature than sMMO. The engineering/evolution/modification of MMO enzymes using various biological and chemical techniques could lead to an optimal way to reach the ultimate goal of technically and economically feasible and environmentally friendly oxidation of methane. For this, multidisciplinary efforts from chemical engineering, protein engineering, and bioprocess research sectors should be systematically combined.
KW - Biological Oxidation
KW - Methane
KW - Methane Monooxygenase
KW - Methanol
KW - Natural/Shale Gas
UR - http://www.scopus.com/inward/record.url?scp=84876896467&partnerID=8YFLogxK
U2 - 10.1007/s11814-013-0060-5
DO - 10.1007/s11814-013-0060-5
M3 - Article
AN - SCOPUS:84876896467
SN - 0256-1115
VL - 30
SP - 977
EP - 987
JO - Korean Journal of Chemical Engineering
JF - Korean Journal of Chemical Engineering
IS - 5
ER -