Molecular design of lysozyme for switching the antimicrobial action
| Project/Area Number |
12660115
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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 |
食品科学・栄養科学
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| Research Institution | Yamaguchi University |
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Principal Investigator |
KATO Akio Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (00035114)
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| Co-Investigator(Kenkyū-buntansha) |
AZAKAMI Hiroyuki Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Assistant Professor, 農学部, 助手 (40263850)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2000: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Lysozyme / Bactericidal lysozyme / Lipophilized lysozyme / Hyrdophobic peptide-fused lysozyme / ソポフィル化リゾチ-ム / 疎水ペプチド結合リゾチ-ム / 抗菌性スイッチング / Pichia pastoris |
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| Research Abstract |
In order to expand the antimicrobial action to Gram-negative and Gram-positive, the molecular design of hen egg white lysozyme was attempted by genetic modification. The penta hydrophobic peptide (Phe-Phe-Val-Ala-Pro) was fused to the C terminus of lysozyme. The resulting petapeptide fused lysozyme (H5-Lz) showed strong bactericidal action against Gram-negative and -positive bacteria. The secretion amount of H5-Lz greatly increased in Pichia pastoris expression system, although it was very poor in Saccharomyces . cerevisiae. The conformation of H5-Lz was kept in a folded form, but the stability was lightly decreased, reflecting the fusion of hydrophobic peptide. The H5-Lz can be useful for industrial applications. As a typical example, the H5-Lz was introduce into tobacco leaf through agrobacterium infection. The transgenic tobacco showed strong resistance to gray mold and powdery mildew infection.
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Report
(3 results)
Research Products
(13 results)
