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- Methane monooxygenase, or MMO, is an
enzyme capable of oxidizing the C-H bond in methane as well as other
alkanes. Methane monooxygenase belongs to the class of oxidoreductase
Methane monooxygenase comes in two varieties: soluble and
membrane bound. The soluble MMO is very nonspecific and is present
primarily in Type II methanotrophs, where it is induced by low copper
conditions enzyme. The membrane bound or particulate MMO (pMMO) is
constitutive, but limited by the availability of copper. It is more
specific for methane and oxidizes fewer xenobiotics
- The particulate methane monooxygenase
and related ammonia monooxygenase are integral membrane proteins,
occurring in methanotrophs and ammonia oxidisers, respectively
- Methane monooxygenases are found in
methanotrophic bacteria, a class of bacteria that exist at the interface
of aerobic and anaerobic environments.
monooxygenases are found in methanotrophic bacteria, a class of bacteria
that exist at the interface of aerobic and anaerobic environments.
- MMOs are found in
methanotrophs, which are bacteria that appear to be ubiquitous in the
environment and can grow with methane as the sole source of carbon and
- The soluble
methane monooxygenase from the pseudothermophile Methylococcus
(Bath) is a three-component enzyme system that catalyzes
the selective oxidation of methane to methanol.
- In order to
obtain particulate methane monooxygenase (pMMO)-enriched membranes from
capsulatus (Bath) with high activity and in high yields, a method is
devised to process cell growth in a fermentor adapted with a
hollow-fiber bioreactor that allows easy control and quantitative
adjustment of the
copper ion concentration in NMS medium over the time course of cell
The use of enzymes known as methane monooxygenases to
catalyse the oxidation of methane to methanol is a defining characteristic
enzyme also has potential applications for converting waste methane into
methanol, synthesizing homochiral epoxides, and probing the biochemical
fundamentals of the methane oxidation reaction.
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