Improving thermal hysteresis activity of antifreeze protein from recombinant Pichia pastoris by removal of N-glycosylation
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- Improving thermal hysteresis activity of antifreeze protein from recombinant Pichia pastoris by removal of N-glycosylation
- Other Titles
- N-glycosylation 제거를 통한 재조합 Pichia pastoris로부터 결빙방지단백질의 온도이력 활성 증대
- Kim, Eun Jae
Han, Se Jong
Lee, Sung Gu
Lee, Jun Hyuck
- Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology
- Antifreeze protein; Flavobacterium frigoris; Glycosylation; Ice-binding protein; Pichia pastoris
- Issue Date
- Kim, Eun Jae, et al. 2017. "Improving thermal hysteresis activity of antifreeze protein from recombinant Pichia pastoris by removal of N-glycosylation". PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, 47(3): 299-304.
- To survive in a sub-zero environment, polar organisms produce ice-binding proteins (IBPs). These IBPs prevent the formation of large intracellular ice crystals, which may be fatal to the organism. Recently, a recombinant FfIBP (an IBP from Flavobacterium frigoris PS1) was cloned and produced in Pichia pastoris using fed-batch fermentation with methanol feeding. In this study, we demonstrate that FfIBP produced by P. pastoris has a glycosylation site, which diminishes the TH activity of FfIBP. The FfIBP expressed by P. pastoris exhibited a doublet on SDS-PAGE. The results of a glycosidase reaction and PAS staining suggested that FfIBP possesses complex N-linked oligosaccharides. 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 antifreeze proteins on a large scale.
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