KOPRI Repository

PRODUCTION OF ICE BINDING PROTEIN WITH INCREASED THERMAL HYSTERESIS ACTIVITY FROM RECOMBINANT PICHIA PASTORIS

Metadata Downloads
Title
PRODUCTION OF ICE BINDING PROTEIN WITH INCREASED THERMAL HYSTERESIS ACTIVITY FROM RECOMBINANT PICHIA PASTORIS
Other Titles
재조합 Pichia pastoris에서 온도이력활성이 향상된 재조합 결빙방지단백질의 생산
Authors
Kim, Eun Jae
Han, Se Jong
Lee, Sung Gu
Lee, Jun Hyuck
Keywords
Ice binding protein; Pichia pastoris; Thermal hysteresis
Issue Date
2017
Citation
Kim, Eun Jae, et al. 2017. PRODUCTION OF ICE BINDING PROTEIN WITH INCREASED THERMAL HYSTERESIS ACTIVITY FROM RECOMBINANT PICHIA PASTORIS. 제23차 국제 극지과학심포지움. 인천, 극지연구소. 2017.05.17~2017.05.18.
Abstract
Ice binding proteins (IBPs) are found in polar organisms such as fish, plants, and insects. IBPs assist organism to survive in cold environments. The functions of IBPs include adhesion to ice and inhibition of ice recrystallization. The FfIBP was isolated from Antarctic bacterium Flavobacterium frigoris PS1. A codon-optimized FfIBP was cloned and produced in Pichia pastoris using fed-batch fermentation with methanol feeding. The FfIBP secreted by P. pastoris has a glycosylation site, which reduces the thermal hysteresis activity of FfIBP. The FfIBP produced by P. pastoris showed a doublet on SDS-PAGE. The results of enzymatic digestion of glycosylated protein suggested that FfIBP has complex N-linked oligosaccharides. The non-glycosylated FfIBP expressed by site-direct mutagenesis exhibited a single band on SDS-PAGE and presented as high thermal hysteresis activity as expressed in E. coli. These results indicate that the glycan attached to asparagine at 203 position of FfIBP could disturb the binding of FfIBP to ice molecules. The findings of this study could be utilized to produce IBPs having hyperactivity on a large scale. [The research was supported by a grant from KOPRI (PE17100)]
URI
http://repository.kopri.re.kr/handle/201206/7184
Conference Name
제23차 국제 극지과학심포지움
Conference Place
인천, 극지연구소
Conference Date
2017.05.17~2017.05.18
Files in 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

    qrcode

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

    Browse