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Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris

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Title
Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris
Other Titles
호냉성 박테리아 (Flavobacterium frigoris)종이 분비하는 결빙방지단백질의 구조적 기초조사 및 특징
Authors
Do, Hackwon
Lee, Sung Gu
Kim, Hak Jun
Lee, Jun Hyuck
Issue Date
2012
Citation
Do, Hackwon, et al. 2012. Characterization and preliminary X-ray crystallographic analysis of an Ice-binding protein (FfIBP) from phychrophilic bacteria, Flavobacterium frigoris. 한국생물공학회. 한국생물공학회. 2012.04.11~.
Abstract
The Ice binding protein (IBP) is a prerequisite material for organism to be allowed to live in a subzero environment. Ice growth in a cold environment is fatal for organism which is not just physically destruction of inner cell organelle but also chemical damage such an osmotic shock. IBP has been characterized property of which ability inhibit the ice growth by binding to specific ice plane. Flavobacterium frigoris isolated from Antarctic area produce an ice-binding protein (FfIBP) to survive and reduce damage from ice growth. The FfIBP has been cloned and over-expressed in Escherichia coli. To diagnose ice-binding mechanism, we measured thermal hysteresis (TH) activity which is numerical value of a gap between freezing and melting point as well as ice re-crystallization inhibition activity. Thermal hysteresis activity of the FfIBP was approximately 2.5℃ at 50uM that is 10 times higher than moderately active LeIBP. Furthermore, the Ice Re-crystallization inhibition activity represent the FfIBP has ability to inhibit ice growing at low concentration 2.5uM limit. Consequently the FfIBP was classified as a hyper-active Ice binding protein. Also, preliminary X-ray crystallography was performed to reveal the ice-binding site of FfIBP at the molecular level.e but also chemical damage such an osmotic shock. IBP has been characterized property of which ability inhibit the ice growth by binding to specific ice plane. Flavobacterium frigoris isolated from Antarctic area produce an ice-binding protein (FfIBP) to survive and reduce damage from ice growth. The FfIBP has been cloned and over-expressed in Escherichia coli. To diagnose ice-binding mechanism, we measured thermal hysteresis (TH) activity which is numerical value of a gap between freezing and melting point as well as ice re-crystallization inhibition activity. Thermal hysteresis activity of the FfIBP was approximately 2.5℃ at 50uM that is 10 times higher than moderately a
URI
https://repository.kopri.re.kr/handle/201206/8442
Conference Name
한국생물공학회
Conference Place
한국생물공학회
Conference Date
2012.04.11~
Type
Proceeding
Indexed
세미나-학술발표
Appears in Collections  
2011-2012, Developing cryoprotectant materials derived from antifreeze proteins for the cryopreservation of valuable bioresources (11-12) / Kim, Hak Jun (PE11100, PG11010, PG12010, PE12210)
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