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Improvement of thermal hysteresis activity of ice binding protein from recombinant Pichia pastoris by removing of N-glycosylation

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Title
Improvement of thermal hysteresis activity of ice binding protein from recombinant Pichia pastoris by removing of N-glycosylation
Other Titles
재조합 Pichia pastoris에서 발현한 결빙방지단백질의 활성향상을 위한 N-glycosylation의 제거
Authors
Lee, Jun Hyuck
Han, Se Jong
Lee, Sung Gu
Kim, Eun Jae
Keywords
FfIBP; Ice binding protein; Pichia pastoris
Issue Date
2017
Citation
Lee, Jun Hyuck, et al. 2017. Improvement of thermal hysteresis activity of ice binding protein from recombinant Pichia pastoris by removing of N-glycosylation. 2017 한국생물공학회 춘계학술발표대회 및 국제심포지엄. 경주, 화백컨벤션센터. 2017.04.05~2017.04.07.
Abstract
Polar organisms produce ice-binding proteins (IBPs) to survive in a sub-zero environment. These IBPs prevent the formation of large intracellular ice crystals, which may be fatal to the organism. The FfIBP having a hyper-thermal hysteresis activity was isolated from Antarctic bacterium Flavobacterium frigoris PS1. Recombinant FfIBP was cloned and produced in Pichia pastoris using fed-batch fermentation with methanol feeding. The FfIBP produced by P. pastoris has a glycosylation site, which reduces the thermal hysteresis activity of FfIBP. The FfIBP expressed by P. pastoris exhibited a doublet on SDS-PAGE. The results of a glycosidase reaction suggested that FfIBP possesses complex N-linked oligosaccharides. The non-glycosylated FfIBP produced by site-direct mutagenesis exhibited a single band on SDS-PAGE and showed as high thermal hysteresis activity as expressed in E. coli. These results indicate that the residues of the glycosylated site could disturb the binding of FfIBP to ice molecules. The findings of this study could be utilized to produce highly active ice binding proteins on a large scale. [The research was supported by a grant from KOPRI (PE17100)]
URI
http://repository.kopri.re.kr/handle/201206/7183
Conference Name
2017 한국생물공학회 춘계학술발표대회 및 국제심포지엄
Conference Place
경주, 화백컨벤션센터
Conference Date
2017.04.05~2017.04.07
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