Aquifex aeolicus
Aquificeae | |
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Scientific classification | |
Domain: | |
Phylum: | |
Class: | |
Order: | Aquificales |
Family: | |
Genus: | |
Species: | A. aeolicus
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Binomial name | |
"Aquifex aeolicus" |
"Aquifex aeolicus" is a
Microbiological Characteristics
Morphology
Mature "A. aeolicus" cells are typically rod-shaped bacterium with an approximate length of 2.0-6.0μm and a diameter of 0.4-0.5μm.
Metabolism
As an
Regarding its growth under microaerophilic conditions, Aquifex species have been observed to grow in oxygen concentrations as long as 7.5ppm.[6] It is hypothesized that this is possible because 1) their oxygen-respiration system was already highly developed before the advent of oxygenic photosynthesis, 2) the Aquifex lineage came to life after there was a rise in atmospheric oxygen, or 3) oxygen respiration was developed, and then transferred among different bacterial lineages, such as Aquifex.[1] In response to oxidative stress, "A. aeolicus" possesses protective enzymes such as superoxide and peroxide to counter harmful oxygen species.[3]
Habitat
"A. aeolicus" was originally isolated from underwater volcanic vents near the Aeolic Islands (north of Sicily) and has also been isolated from the hot springs in Yellowstone.[5] As a hyperthermophile, "A. aeolicus" can survive up to 95 °C with a temperature optima of 85 °C[2] with a pH optima of 8.0, ranging from 6.8 to 9.0.[2]
Genomic Properties
"Aquifex aeolicus" is the first thermophilic bacterium to have its entire genome sequenced.[2] Comparison of the "Aquifex aeolicus" genome to other organisms showed that around 16% of its genes originated from the Archaea domain. It is most closely related to the hydrogen-oxidizing bacterium, Aquifex pyrophilus, and its close relative, Hydrogenobacter thermophilus.[6]
The genome of "A. aeolicus" has been successfully mapped,
Industrial Applications
Multiple enzymes have been identified for potential future use due to their high stability and capacity to oxidize molecular hydrogen, producing byproducts of heat and water.[2][5] A key enzyme of note is Hydrogenase I which was used to study the relationship of enzymes and electrodes during the development of H2-fed, energy-generating biofuel cells.[2] Researchers have explored the use of another extremely resistant enzyme known as lumazine synthase. The cage-forming enzyme has been explored as potential drug delivery nano carrier as it was engineered to encapsulate other molecules.[2]
References
- ^ PMID 9537320.)
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: CS1 maint: multiple names: authors list (link - ^ S2CID 229351588.
- ^ S2CID 4413967.
- ^ PMID 23046953.
- ^ S2CID 254232862.
- ^ PMID 7518219.)
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: CS1 maint: multiple names: authors list (link