Quantitative analysis of the ability of ice recrystallization inhibition of antifreeze protein
| Project/Area Number |
15K13760
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Green/Environmental chemistry
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| Research Institution | National Institute of Advanced Industrial Science and Technology |
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Principal Investigator |
Tsuda Sakae 国立研究開発法人産業技術総合研究所, 生物プロセス研究部門, 上級主任研究員 (70211381)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 不凍 / タンパク質 / 氷 / 再結晶化 / 氷結晶結合 / 分子構造 / ナノスケール / 計測 / 結晶成長 / 水 / 氷結晶 / 熱ヒステリシス / 界面前進凍結濃縮 / 不凍蛋白質 / AFP / 冷熱 |
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| Outline of Final Research Achievements |
Numerous embryo single ice crystals are generated in water when it is frozen. They are progressing crystal growth and combined together to form a multi crystalline state, whose process is called ice recrystallization. Antifreeze protein (AFP) has a strong ability of ice recrystallization inhibition (IRI) , while it has not been established an efficient method to analyze the IRI activity quantitatively. Here we developed a new method, which is different from the known splat cooling assay, to precisely evaluate IRI rate of AFP based on the equation (r3 = r3(0) + Kt) of the Ostwald Ripening. We also identified a new species of AFP (BpAFP) from righteye flounder that showed a strong IRI and thermal hysteresis activity in concentration-dependent manner.
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Report
(3 results)
Research Products
(53 results)
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[Presentation] 不凍物質の科学2017
Author(s)
津田 栄
Organizer
第3回低温科学技術交流調査会
Place of Presentation
ちよだプラットフォーム、東京都
Year and Date
2017-01-20
Related Report
Invited
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