China 
Africa 
Explore chapters and articles related to this topic
1-Proteins Prospect for Production of Industrial Proteins and Protein-Based Materials from Methane
Published in Shashi Kant Bhatia, Sanjeet Mehariya, Obulisamy Parthiba Karthikeyan, Algal Biorefineries and the Circular Bioeconomy, 2022
Hamilton Richard, Nizovtseva Irina, Chernuskin Dmitri, Marina G. Kalyuzhnaya
Methane monooxygenase (MMO) as a platform for epoxidation, bioremediation, and cell-free methane conversion. The use of methane monooxygenase as an enzyme for epoxidation or bioremediation is one of the most sought-after areas of methanotrophic protein implementation (Smith et al., 2002; Jiang et al., 2010; Lawton & Rosenzweig, 2016; Chan & Yu, 2019; Khider et al., 2021). The heterologous expression of methane monooxygenase in non-methanotrophic hosts has been challenging; however, the methanotrophs themselves represent an attractive production system. It is estimated that MMOs comprise up to 80% of their cellular proteome (Yu et al., 2003). Significant progress has been made in engineering methanotrophic MMO for degradation of aromatic compounds, expanding the potential of the enzyme for environmental cleanup (Smith et al., 2002; Lock et al., 2017). Use of pure enzymes as a cell-free system for converting methane to methanol is another area of active studies (Blanchette et al., 2016; Chan & Yu, 2019; Park & Kim, 2019; Xin et al., 2019). Considering the explosion in cell-free biotechnology, the demand for robust methane-converting enzymes is expected to grow.
3D Printed Immobilized Biocatalysts for Conversion of Methane
Published in Jianli Hu, Dushyant Shekhawat, Direct Natural Gas Conversion to Value-Added Chemicals, 2020
The oxidoreductase methane monooxygenase (MMO), found in methanotroph bacteria, catalyzes the partial oxidation of methane to methanol at ambient conditions with the highest known selectivity of any catalyst of this reaction, biological or chemical (Hammond et al. 2012). Methanotrophic bacteria and isolated MMOs are interesting biocatalysts for methane conversion because they operate at low temperature and pressures and can withstand the presence of some contaminants such as hydrogen sulfide (Mühlemeier, Speight, and Strong 2018), unlike most inorganic or chemical catalysts. Additionally, methanotrophs have been genetically engineered to convert methane into various valuable products besides methanol, such as bioprotein (Bothe et al. 2002; Harrison and Hamer 1971), polyhydroxybutyrate (Khosravi-Darani et al. 2013), and lactate (Henard et al. 2016). Catalysis of methane gas-to-liquid products is important because U.S. emissions of methane, a greenhouse gas 70 times more potent than CO2 over a 20 year period (Stocker et al. 2013), are expected to rise 20% from natural gas production over the next 15 years (U.S. Department of State 2014) and sources such as farming and arctic melt (Stolaroff et al. 2012) will also increase. It is essential to mitigate small and remote methane streams < 1000 ppm to control these emissions (Stolaroff et al. 2012), which are currently released or flared due to the impracticality and expense of traditional chemical processing at these remote sites with low concentrations of methane.
Bioconversion of Waste Biomass to Biomethanol
Published in Prakash Kumar Sarangi, Sonil Nanda, Bioprocessing of Biofuels, 2020
Prakash Kumar Sarangi, Sonil Nanda
Soluble cytoplasmic form (sMMO) as well as particulate membrane-bound form (pMMO) are the two forms of methane monooxygenase. There are other possible routes for the conversion of methanol into CO2 via formaldehyde and formic acid and three different types of enzymes, i.e. methanol dehydrogenase (MDH), formaldehyde dehydrogenase (FADH) and formate dehydrogenase (FDH) (Hanson and Hanson 1996; Xin et al. 2009). The selection of the methanotrophic bacteria and the standardization of its growth conditions can affect the final recovery of biomethanol. More exploration of potential microbial communities and understanding their biocatalytic activities could aid in the large-scale production of biomethanol from waste biomass sources.
A mathematical model of aerobic methane oxidation coupled to denitrification
Published in Environmental Technology, 2018
The focus of this study, however, is on methane oxidation coupled to denitrification under aerobic conditions. Aerobic methanotrophs are ubiquitous and fast-growing bacteria that use methane as their sole source of carbon and energy. They oxidize methane to carbon dioxide via methanol, formaldehyde, and formate. The initial oxidation of methane to methanol is catalyzed by methane monooxygenase, which requires molecular oxygen and two reducing equivalents. The following oxidation of methanol to carbon dioxide generates the reducing equivalents needed for maintenance and growth of the bacteria [4,5]. Phylogenetically, aerobic methanotrophs are located in the Gamma-proteobacteria, Alpha-proteobacteria, and Verrucomicrobia phyla [6,7]. Several nitrogen conversions can be catalyzed by aerobic methanotrophs, including N2-fixation [8], assimilatory nitrate reduction to ammonia [9], and cometabolic ammonium oxidation by the methane monooxygenase enzyme [10]. Some aerobic methanotrophs also possess denitrifying pathways [11]. Recently, Dam et al. [12] showed that Methylcystis sp. strain SC2 could denitrify using methanol or possibly intracellularly stored polyhydroxybutyrate as electron donor. Kits et al. [13] showed that Methylomonas denitrificans sp. nov strain FJG1 could reduce nitrate to nitrous oxide using methane as the electron donor, although molecular oxygen appeared to be needed for the initial oxidation of methane.
Harnessing biodegradation potential of rapid sand filtration for organic micropollutant removal from drinking water: A review
Published in Critical Reviews in Environmental Science and Technology, 2021
Jinsong Wang, David de Ridder, Albert van der Wal, Nora B. Sutton
Removal of methane from treated groundwater in RSF is performed by methane oxidizing bacteria (MOB) (Benner et al., 2013; Hedegaard et al., 2018). Similar to the ammonia monooxygenase enzyme, methane monooxygenase enzymes also can oxidize many different OMPs (Benner et al., 2013; Brusseau et al., 1990; Colby et al., 1977; Sullivan et al., 1998).