Increased Productivity and Antifreeze Activity of Ice-binding Protein from Flavobacterium frigoris PS1 Produced using Escherichia coli as Bioreactor
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- Increased Productivity and Antifreeze Activity of Ice-binding Protein from Flavobacterium frigoris PS1 Produced using Escherichia coli as Bioreactor
- Other Titles
- 생물반응기에서 대장균의 배양을 통한 플라보박테리움 프리고리스 PS1 유래 결빙방지단백질의 생산성 및 결빙방지 활성 증대
- Kim, Eun Jae
Kim, Jung Eun
Hwang, J. S.
Lee, Sung Gu
Lee, Jun Hyuck
Han, Se Jong
- Biotechnology & Applied Microbiology; Microbiology
- Antarctica; Flavobacterium frigoris; ice-binding protein; pilot-scale fermentation; thermal hysteresis
- Issue Date
- Kim, Eun Jae, et al. 2019. "Increased Productivity and Antifreeze Activity of Ice-binding Protein from Flavobacterium frigoris PS1 Produced using Escherichia coli as Bioreactor". APPLIED BIOCHEMISTRY AND MICROBIOLOGY, 55(5): 489-494.
- Ice-binding proteins (IBPs) inhibit the growth and recrystallization of intracellular ice, enabling polar organisms to survive at subzero temperatures. IBPs are promising materials in biomedical applications such as cryopreservation and the hypothermic storage of cells, tissues, and organs. In this study, recombinant IBP from the antarctic bacterium Flavobacterium frigoris PS1 (FfIBP) was produced by Escherichia coli used as bioreactor, to examine the feasibility of scale-up. Oxygen transfer was the most important factor influencing cell growth and FfIBP production during pilot-scale fermentation. The final yield of recombinant FfIBP produced by E. coli harboring the pET28a-FfIBP vector system was 1.6 g/L, 3.8-fold higher than that from the previously published report using pCold I-FfIBP vector system, and its thermal hysteresis activity was 2.5°C at 9.7 μM. This study demonstrates the successful pilot-scale production of FfIBP.
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