2000 Fiscal Year Final Research Report Summary
Studies on the development of functional biopolymers and the removal of pathogenic viruses in the water environment
| Project/Area Number |
10450194
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Civil and environmental engineering
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| Research Institution | Tohoku University |
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Principal Investigator |
OMURA Tatsuo Tohoku University, Graduate School of Engineering, Professor, 大学院・工学研究科, 教授 (30111248)
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| Project Period (FY) |
1998 – 2000
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| Keywords | Virus-binding proteins / Poliovirus 1 / Capsid proteins / Affinity chromatography / SDS-PAGE / ELISA method / Activated sludge / Interaction between proteins |
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| Research Abstract |
Most of pathogenic viruses in the sewage sludge is removed through the activated sludge process. This removal of pathogenic viruses is mainly due to the adsorption to the sludge flocs. It is said that this adsorption is based on the interaction between capsid proteins of viruses and proteins included in the sludge flocs. There is high possibility that the proteins in the sewage sludge can be utilized for the removal of pathogenic viruses from the water environment.
The objectives of this research were to survey the virus-binding protein (VBP) from the activeted sludge and to resolve the binding mechanism between the VBP and pathogenic viruses.
Following conclusions were obtained in this research :
-VBPs were isolated from the activated sludge culture by the affinity chromatography technique.
-VBPs were classified into two groups by the molecular weight (estimated by SDS-PAGE). They had the molecular weights around 110,000 Da and over 170,000 Da, respectively.
-It became obvious by ELISA method that VBPs could bind poliovirus 1 two times as efficinently as the crude proteins extracted from activated sludge culture.
-Isolation points of VBPs were pH 7.0 and 7.7. This result indicated that the binding of pathogenic viruses by VBPs was based on the interaction between proteins such as hydrophobic bond and hydrogen bond.
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Research Products
(12 results)
