Antifreeze protein activity in Arctic cryoconite bacteria. Issue 1 (18th December 2013)
- Record Type:
- Journal Article
- Title:
- Antifreeze protein activity in Arctic cryoconite bacteria. Issue 1 (18th December 2013)
- Main Title:
- Antifreeze protein activity in Arctic cryoconite bacteria
- Authors:
- Singh, Purnima
Hanada, Yuichi
Singh, Shiv Mohan
Tsuda, Sakae - Abstract:
- <abstract abstract-type="main" id="fml12345-abs-0001"> <title>Abstract</title> <p>Fourteen Arctic bacterial strains belonging to five genera, <italic>Cryobacterium</italic>, <italic> Leifsonia</italic>, <italic> Polaromonas</italic>, <italic> Pseudomonas</italic>, and <italic>Subtercola</italic> isolated from sediments found in cryoconite holes of Arctic glaciers, were subjected to screening for antifreeze proteins (AFPs). Eight strains showed AFP activity, and six strains of four species were further characterized. <italic>Pseudomonas ficuserectae</italic> exhibited a high thermal hysteresis (TH) activity. Ice recrystallization inhibition (IRI) activity was observed in most cultures at low protein concentration. Bacterial AFPs produced rounded shape of ice crystals that did not change their size and morphology within the TH window. Cry‐g (<italic>P. ficuserectae</italic>) failed to inhibit ice recrystallization, indicating that the IRI activity of the AFPs does not relate to the strength of TH activity. SDS‐PAGE analysis of the AFPs suggests their apparent molecular weights to be around 23 kDa. This study is significant as it screens several species of Arctic bacterial strains for AFP activity. So far, only one species of bacteria, <italic>Pseudomonas putida</italic>, was reported from the Arctic to produce AFPs. N‐terminal amino acid sequence analysis shows that the bacterial AFPs isolated belong to the AFP family IBP‐1, which is known to have an important physiological<abstract abstract-type="main" id="fml12345-abs-0001"> <title>Abstract</title> <p>Fourteen Arctic bacterial strains belonging to five genera, <italic>Cryobacterium</italic>, <italic> Leifsonia</italic>, <italic> Polaromonas</italic>, <italic> Pseudomonas</italic>, and <italic>Subtercola</italic> isolated from sediments found in cryoconite holes of Arctic glaciers, were subjected to screening for antifreeze proteins (AFPs). Eight strains showed AFP activity, and six strains of four species were further characterized. <italic>Pseudomonas ficuserectae</italic> exhibited a high thermal hysteresis (TH) activity. Ice recrystallization inhibition (IRI) activity was observed in most cultures at low protein concentration. Bacterial AFPs produced rounded shape of ice crystals that did not change their size and morphology within the TH window. Cry‐g (<italic>P. ficuserectae</italic>) failed to inhibit ice recrystallization, indicating that the IRI activity of the AFPs does not relate to the strength of TH activity. SDS‐PAGE analysis of the AFPs suggests their apparent molecular weights to be around 23 kDa. This study is significant as it screens several species of Arctic bacterial strains for AFP activity. So far, only one species of bacteria, <italic>Pseudomonas putida</italic>, was reported from the Arctic to produce AFPs. N‐terminal amino acid sequence analysis shows that the bacterial AFPs isolated belong to the AFP family IBP‐1, which is known to have an important physiological role in the cold environment. AFPs of glacier cryoconite habitat have been discussed.</p> </abstract> … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 351:Issue 1(2014:Feb.)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 351:Issue 1(2014:Feb.)
- Issue Display:
- Volume 351, Issue 1 (2014)
- Year:
- 2014
- Volume:
- 351
- Issue:
- 1
- Issue Sort Value:
- 2014-0351-0001-0000
- Page Start:
- 14
- Page End:
- 22
- Publication Date:
- 2013-12-18
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1111/1574-6968.12345 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
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- 3224.xml