naa a22 4500 510821235 CHVBK 20180411083533.0 cr unu---uuuuu 180411e20130501xx s 000 0 eng 10.1007/s11814-013-0060-5 doi (NATIONALLICENCE)springer-10.1007/s11814-013-0060-5 Biological conversion of methane to methanol [Elektronische Daten] [Donghyun Park, Jeewon Lee] 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 α 3 β 3 γ 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. Korean Institute of Chemical Engineers, Seoul, Korea, 2013 Natural/Shale Gas nationallicence Methane nationallicence Methanol nationallicence Biological Oxidation nationallicence Methane Monooxygenase nationallicence Park Donghyun Department of Chemical and Biological Engineering, Korea University, Anam-dong, 5-1, Sungbuk-gu, 136-713, Seoul, Korea aut Lee Jeewon Department of Chemical and Biological Engineering, Korea University, Anam-dong, 5-1, Sungbuk-gu, 136-713, Seoul, Korea aut Korean Journal of Chemical Engineering Springer US; http://www.springer-ny.com 30/5(2013-05-01), 977-987 0256-1115 30:5<977 2013 30 11814 https://doi.org/10.1007/s11814-013-0060-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11814-013-0060-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Park Donghyun Department of Chemical and Biological Engineering, Korea University, Anam-dong, 5-1, Sungbuk-gu, 136-713, Seoul, Korea aut NATIONALLICENCE 700 1- Lee Jeewon Department of Chemical and Biological Engineering, Korea University, Anam-dong, 5-1, Sungbuk-gu, 136-713, Seoul, Korea aut NATIONALLICENCE 773 0- Korean Journal of Chemical Engineering Springer US; http://www.springer-ny.com 30/5(2013-05-01), 977-987 0256-1115 30:5<977 2013 30 11814 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer