KOPRI Repository

Effect of Glycosylation on Antifreeze Protein Activity

Cited 0 time in wos
Cited 0 time in scopus
Metadata Downloads
Effect of Glycosylation on Antifreeze Protein Activity
Other Titles
결빙방지단백질에 당화가 미치는 영향
Park, Kyoung Sun
Kim, Hak Jun
Kang, Sung-Ho
AFGP; Glycosylation
Issue Date
Park, Kyoung Sun, et al. 2009. Effect of Glycosylation on Antifreeze Protein Activity. 한국미생물학회연합 국제학술대회. 한국미생물학회연합 국제학술대회. 2009.10.23~.
Antifreeze proteins (AFPs) depress the freezing point of a solution which therefore produces a difference between the melting point and freezing point, so called thermal hysteresis (TH). AFPs have been known to be essential for organisms to survive subzero environments. So far, many AFPs have been characterized from fish, insects, plants, bacteria and microalgae. We isolated AFP from the culture supernatant of an Arctic yeast Leucosporidium sp. AY30 using ice affinity method. Native AY30 AFP was observed to be glycosylated by periodic acid Schiff staining. PNGase treatment indicated that AY30 AFP was N-glycosylated protein. We cloned and expressed recombinant AFP (rAY30 AFP) in BL21 (DE3). CD spectra data indicated that tertiary structures of native and rAFP were similar. The rAY30 AFP has shown to have lower TH activity than native AY30 AFP. The shape of ice crystal of rAFP was star shape meaning weak ice-binding activity. These results shows that glycosylation enhance the TH activity and ice-binding activity. Futher study, we plans to the X-ray crystallography for more accurate 3-D structure
Conference Name
한국미생물학회연합 국제학술대회
Conference Place
한국미생물학회연합 국제학술대회
Conference Date
Files in This Item
There are no files associated with this item.
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.