| Project/Area Number |
17580107
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Food science
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
HATTORI Makoto Tokyo University of Agriculture and Technology, Institute of Symbiotic Science and Technology, Associate Professor, 大学院共生科学技術研究院, 助教授 (40221501)
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Tadashi Tokyo University of Agriculture and Technology, Institute of Symbiotic Science and Technology, Research Associate, 大学院共生科学技術研究院, 助手 (20302911)
TOTSUKA Mamoru The University of Tokyo, Department of Applied Biological Chemistry, Associate Professor, 大学院農学生命科学研究科, 助教授 (70227601)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2006: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2005: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | β-lactoglobulin / reduction of allergenisity / bioconjugate / Pichia pastris / protein engineering / β-ラクトグロブリン / Pichia pastroris |
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| Research Abstract |
Purpose of this study was to create novel biocojugates of β-lactoglobulin (BLG), major whey protein, by using protein engineering technique with reduced allergenoicity and improved emulsifying ability, while maintaining native protein structure and ligand binding activity.
Glycosylated bioconjugates of BLG (P153A, D28N, D137N/A139S) were produced in the methylotrophic yeast Pichia pastoris. Molecular weight of each biocojugate was determined to be 24 kDa, which indicates saccharide chain of 6 kDa was attached to BLG in each bioconjugate.
As for the functional changes in BLG by preparing novel bioconjugates, emulsifying ability and immunogenicity were evaluated. D28N showed improved emulsifying activity, while emulsion stability of the emulsion prepared with D28 was similar to emulsion stability of the emulsion prepared with native protein. Immunogenicity of BLG was reduced in P153A, while glycosilation of C-terminal residue (D137N/A139S) showed the tendency of reduced immunogenicity.
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