Surface modification of monolithic pore for solid phaseprotein PEGylation based on its mass transfer
| Project/Area Number |
16K18301
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Yamaguchi University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
YAMAMOTO Shuichi 山口大学, 大学院創成科学研究科, 教授 (80144921)
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| Research Collaborator |
PODGORNIK Ales リュブリャナ大学, 教授
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | モノリス / クロマトグラフィー / PEG化タンパク質 / 固相反応 / monolith / PEGylation / chromatography / バイオリアクター |
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| Outline of Final Research Achievements |
Site-specific PEGylation of proteins was examined by applying a monolithic ion exchange chromatography with low diffusional resistance. The mass transfer property within pores and the binding of proteins to solid phase were focused as the factors dominating the yield and selectivity of the reaction. The effects of pore size and density of ligands of monolithic supports on the above factors were clarified. Negligible mass transfer resistance was observed with respect to any monolithic supports used. The number of binding sites was unaffected by pore size and the density of ligands. Furthermore, the reaction yield was improved from 5% to about 20% by increasing reaction temperature while the site-specificity of reaction was maintained.
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Report
(3 results)
Research Products
(7 results)
