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Biological conversion of methane to methanol

Authors
Park, DonghynnLee, Jeewon
Issue Date
5월-2013
Publisher
KOREAN INSTITUTE CHEMICAL ENGINEERS
Keywords
Natural/Shale Gas; Methane; Methanol; Biological Oxidation; Methane Monooxygenase
Citation
KOREAN JOURNAL OF CHEMICAL ENGINEERING, v.30, no.5, pp.977 - 987
Indexed
SCIE
SCOPUS
KCI
Journal Title
KOREAN JOURNAL OF CHEMICAL ENGINEERING
Volume
30
Number
5
Start Page
977
End Page
987
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103279
DOI
10.1007/s11814-013-0060-5
ISSN
0256-1115
Abstract
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 (alpha beta gamma)(2) dimer architecture with a di-iron active site in hydroxlase. pMMO, a timer (pmoA, pmoB, and pmoC) in an alpha(3)beta(3)gamma(3) 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.
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공과대학 (화공생명공학과)
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