Fervidobacterium islandicum

Fervidobacterium islandicum is a species of extremely thermophilic anaerobic bacteria, first isolated from an Icelandic hot spring.

Fervidobacterium islandicum
Scientific classification
Domain:
Bacteria
Phylum:
Thermotogota
Class:
Thermotogae
Order:
Thermotogales
Family:
Thermotogaceae
Genus:
Fervidobacterium
Species:
F. islandicum
Binomial name
Fervidobacterium islandicum
Huber et al. 1991

Biology and biochemistry

Morphology

F. islandicum cells are Gram-negative motile rods, about 1.8 μm in length, and 0.6 μm in width occurring singly or in pairs.[1] About 50% of cells form large spheroids at one end known as a 'toga' commonly found in members of the phylum Thermotogota (formerly Thermotogae)[2]

Physiology

F. islandicum isolate H21 grows in a pH range from 6.0 to 8.0 with an optimum at around 7.2.[1] Growth is observed at a temperature range between 40 °C and 80 °C, with an optimum of 70 °C.[3] At a temperature of 65 °C, strain H21 has a doubling time of 150 minutes.[1]

Culture growth

Growth of isolate H21 requires low amounts (0.3%) of yeast extract. When this is used as a single carbon and energy source, the final cell concentration is 1x107 cells/ml.[1] Growth is strongly enhanced by the addition of 0.2% pyruvate, ribose, glucose, maltose, raffinose, starch and, less efficiently, cellulose. Final cell concentrations with these additions can range from 2 to 5x108.[1] In the presence of glucose, F. islandicum produces the following end products: L(+) lactate, acetate, ethanol, H2 and CO2.[1] Isolate H21 shows a sensitivity to common antibiotics, its growth is inhibited by addition of vancomycin, streptomycin, ampicillin, chloramphenicol and rifampicin at 10 g/ml.[1]

Genomics

F. islandicum strain AW-1 has a total genome size of 2.4 million base pairs, which is slightly larger than the genomes of other Fervidobacterium strains.[3] It has a G + C content of 40.7%.[3] It contains 2,184 protein coding genes in a total of 2,248 genes.[3]

Environment

F. islandicum was originally isolated from an Icelandic hot spring on the banks of the river Varma close to Hverageri, Iceland. The anaerobic samples were taken from hot waters and muds.[1] Here, the temperatures were between 70 °C and 102 °C, and the pH was between 1.5 and 9.[1]

Biotechnological applications

F. islandicum AW-1 is capable of complete feather degradation at 70 °C and a pH of 7.[4] Feather keratin has a very high cysteine content, which makes it very rigid and hard to digest.[5] 5 million tons of chicken feathers are generated by the poultry industry every year, making chicken feathers a serious solid waste problem.[4] Therefore, F. islandicum's ability to degrade native chicken feathers is very appealing.

References
  1. Huber, Robert; Woese, Carl R.; Langworthy, Thomas A.; Kristjansson, Jakob K.; Stetter, Karl O. (1990). "Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the ?Thermotogales?". Archives of Microbiology. 154 (2): 105–111. doi:10.1007/BF00423318. ISSN 0302-8933. S2CID 40470196.
  2. Bhandari, Vaibhav; Gupta, Radhey S. (2014), Rosenberg, Eugene; DeLong, Edward F.; Lory, Stephen; Stackebrandt, Erko (eds.), "The Phylum Thermotogae", The Prokaryotes: Other Major Lineages of Bacteria and The Archaea, Berlin, Heidelberg: Springer, pp. 989–1015, doi:10.1007/978-3-642-38954-2_118, ISBN 978-3-642-38954-2, retrieved 2021-10-11
  3. Lee, Yong-Jik; Jeong, Haeyoung; Park, Gun-Seok; Kwak, Yunyoung; Lee, Sang-Jae; Lee, Sang Jun; Park, Min-Kyu; Kim, Ji-Yeon; Kang, Hwan Ku; Shin, Jae-Ho; Lee, Dong-Woo (December 2015). "Genome sequence of a native-feather degrading extremely thermophilic Eubacterium, Fervidobacterium islandicum AW-1". Standards in Genomic Sciences. 10 (1): 71. doi:10.1186/s40793-015-0063-4. ISSN 1944-3277. PMC 4587914. PMID 26421103.
  4. Nam, Gae-Won; Lee, Dong-Woo; Lee, Han-Seoung; Lee, Nam-Ju; Kim, Byoung-Chan; Choe, Eun-Ah; Hwang, Jae-Kwan; Suhartono, Maggy; Pyun, Yu-Ryang (2002-12-01). "Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe". Archives of Microbiology. 178 (6): 538–547. doi:10.1007/s00203-002-0489-0. ISSN 0302-8933.
  5. Gregg, Keith; Rogers, George E. (1986), Bereiter-Hahn, Jürgen; Matoltsy, A. Gedeon; Richards, K. Sylvia (eds.), "Feather Keratin: Composition, Structure and Biogenesis", Biology of the Integument, Berlin, Heidelberg: Springer Berlin Heidelberg, pp. 666–694, doi:10.1007/978-3-662-00989-5_33, ISBN 978-3-662-00991-8, retrieved 2021-10-11

Further reading
  • Ravot, Gilles, et al. "L-Alanine production from glucose fermentation by hyperthermophilic members of the domains Bacteria and Archaea: a remnant of an ancestral metabolism?." Applied and Environmental Microbiology 62.7 (1996): 2657-2659.
  • Dworkin, Martin, and Stanley Falkow, eds. The Prokaryotes: Vol. 7: Proteobacteria: Delta and Epsilon Subclasses. Deeply Rooting Bacteria. Vol. 7. Springer, 2006.
  • Gödde C, Sahm K, Brouns SJ, Kluskens LD, van der Oost J, de Vos WM, et al. (2005). "Cloning and expression of islandisin, a new thermostable subtilisin from Fervidobacterium islandicum, in Escherichia coli". Appl Environ Microbiol. 71 (7): 3951–8. doi:10.1128/AEM.71.7.3951-3958.2005. PMC 1168981. PMID 16000809.
  • Nam GW, Lee DW, Lee HS, Lee NJ, Kim BC, Choe EA, et al. (2002). "Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe". Arch Microbiol. 178 (6): 538–47. doi:10.1007/s00203-002-0489-0. PMID 12420177. S2CID 39043722.
  • Jabbour, Dina; Klippel, Barbara; Antranikian, Garabed (2011). "A novel thermostable and glucose-tolerant β-glucosidase from Fervidobacterium islandicum". Applied Microbiology and Biotechnology. 93 (5): 1947–1956. doi:10.1007/s00253-011-3406-0. ISSN 0175-7598. PMID 22146852. S2CID 18254613.
  • de la Tour, Claire Bouthier; Portemer, Christiane; Forterre, Patrick; Huber, Robert; Duguet, Michel (1993). "ATP-independent DNA topoisomerase from Fervidobacterium islandicum". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1216 (2): 213–220. doi:10.1016/0167-4781(93)90147-6. ISSN 0167-4781. PMID 8241262.
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