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Semipurification of Ice-crystal Controlling Protein from the Arctic Bacterium Aquaspirillum sp. KOPRI-AB30

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Title
Semipurification of Ice-crystal Controlling Protein from the Arctic Bacterium Aquaspirillum sp. KOPRI-AB30
Authors
박승일
Kim, Hak Jun
Seo, Ki-Won
Kang, Sung-Ho
Keywords
antifreeze proteins; ice recrystallization; ice-structuring proteins; thermal hysteresis
Issue Date
2007
Citation
박승일, et al. 2007. Semipurification of Ice-crystal Controlling Protein from the Arctic Bacterium Aquaspirillum sp. KOPRI-AB30. Cryobiology. Cryobiology. 2007.07.30~.
Abstract
Antifreeze proteins(AFPs) bind to the surface of ice crystals and control ice crystal structure. We islated some bacteria capable of producing antifreeze proteins as part of cold adaptation mechanism from the Arctic. Among these, the strain KOPRI-AB30 showed high antifreeze activity and was identified as Aquaspirillum sp. The psychrophilic bacterium Aquaspirillum sp.KoPRI-AB30 produced antifreeze protein extracellularly. The optimal temperature and pH for the production of AFP were 5℃ and 7.0, respectively. The AFP was partially purified from the culture supernatant with tangential flow filtration and subsequent chromatography. Molecular mass of the partially-purifed AFP was approximately 20kDa. The ice-crystal controlling activity of the AFP was observed using nanooliter osmometer. The thermal hysteresis of the protein was determined to be about 0.7℃. In addition, the AFP is relatively heat and pH stable, but not calcium dependant. The possible use of the protein as a cryoprotectant was also tested.
URI
http://repository.kopri.re.kr/handle/201206/7710
Conference Name
Cryobiology
Conference Place
Cryobiology
Conference Date
2007.07.30~
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