Posttranslational Modifications of Lysozyme
| Project/Area Number |
10460058
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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 |
食品科学・栄養科学
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| Research Institution | Yamaguchi University |
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Principal Investigator |
KATO Akio Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (00035114)
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| Co-Investigator(Kenkyū-buntansha) |
AZAKAMI Hiroyuki Faculty of Agriculture, Yamaguchi University, Assistant Professor, 農学部, 助手 (40263850)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1999: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | lysozyme / glycosylation of lysozyme / lipophilization of lysozyne / post-translational modification of proteins / transgenic tobacco / 酵母発現 / 抗菌性 / 耐熱性 / 多糖修飾 |
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| Research Abstract |
Effects of post-translational modification such as glycosylation and lipophilization on the functional properties of hen egg white lysozyme were investigated in yeast expression system using genetic modification. The N-linked glycosylation signal (Asn-X-Thr/Ser) was constructed in the position 19 and 49 by site-directed mutagenesis. The polymannosy lysozyme thus obtained was very effective to enhance the thermal stability and the emulsifying property and to decrease the allergenicity. Although the lipophization of lysozyme was examined by the attachment of N-myristylation signal sequence into N-terminal, the folding of lysozyme failed to produce the unfolded form. Instesd of lipophilization, the hydrophobic peptide having the same length as myristic acid was attached to C-terminal of lysozyme. The hydrophobic attached lysozyme (H5) revealed a strong antimicrobial activity agianst Gram-negative bacteria. These modified lysozymes were inserted into tobacco to improve the bactericial action. The transgenic tobacco showed a strong resistance to gray mold.
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Report
(3 results)
Research Products
(11 results)
