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Posttranslational Modifications of Lysozyme

Posttranslational Modifications of Lysozyme
溶菌酶的翻译后修饰
批准号:
10460058
负责人:
KATO Akio
金额:
$1.47万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (B)
财政年份:
1998
资助国家:
日本
项目状态:
已结题
起止时间:
1998 至 1999

项目摘要

项目成果

KATO Akio的其他基金

相关文献

中文摘要
翻译
在酵母基因修饰表达系统中,研究了糖基化和脂质化等翻译后修饰对蛋清溶菌酶功能特性的影响。n链糖基化信号(Asn-X-Thr/Ser)通过定点诱变在第19位和第49位构建。所制得的多甘露溶菌酶在提高热稳定性、乳化性和降低致敏性方面效果显著。虽然通过n -肉豆荚化信号序列附着在n端来检测溶菌酶的脂化,但溶菌酶的折叠不能产生展开形式。与肉豆蔻酸长度相同的疏水肽不是亲脂作用,而是附着在溶菌酶的c端。疏水附着溶菌酶(H5)对革兰氏阴性菌具有较强的抑菌活性。将这些改性的溶菌酶插入烟草中,以提高其抑菌作用。转基因烟草对灰霉病表现出较强的抗性。
英文摘要
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.
期刊论文(11)
专著(0)
科研奖励(0)
会议论文
KATO, A, NAKAMURA, S, H. Ibrahim, MATSUMI, T, TSUMIYAMA, C and KATO, M: "Production of genetically of modified lysozymes having extreme heat stability and antimicrobial activity against Gram negative bacteria in yeast and in plant"Nahrung. 42. 128-130 (19
KATO, A、NAKAMURA, S、H. Ibrahim、MATSUMI, T、TSUMIYAMA, C 和 KATO, M:“通过遗传方式生产具有极端热稳定性和针对酵母和植物中革兰氏阴性菌的抗菌活性的修饰溶菌酶”Nahrung。
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通讯作者:
Y.Shu,S.Nakamura,A.Kato: "The role of polysaccharide-chain atiiachment to lysozyme in the excellent emlistying properties of polymernosye lysoyme"Nohrung. 42. 67-69 (1998)
Y.Shu,S.Nakamura,A.Kato:“多糖链与溶菌酶的结合在聚合物溶菌酶优异的乳化特性中的作用”Nohrung。
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通讯作者:
Y.Shu,M.Maki,S.Nakamura,A.Kato: "Double-glaycosylatect lyszyme at positions 19 and 49 constructed by genetic modification and its surface fanction properties"J.Agric.Food Chem. 46. 2433-2438 (1998)
Y.Shu,M.Maki,S.Nakamura,A.Kato:“通过基因修饰构建的第 19 和 49 位双糖基乳酸溶酶及其表面功能特性”J.Agric.Food Chem。
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通讯作者:
A.KATO,S.Makamura,H.Ibrahim,T.Matsumi: "Production of genetically modified lysozymes habing extrome heat styability and antimirobiol activity in yeaat and in plant"Nahrung. 42. 128-130 (1998)
A.KATO、S.Makamura、H.Ibrahim、T.Matsumi:“在酵母和植物中生产具有极高热稳定性和抗微生物活性的转基因溶菌酶”Nahrung。
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11
    Molecular Designs for Functional Food Proteins by Genetic Modification
    • 批准号:
      14360077
    • 项目类别:
      Grant-in-Aid for Scientific Research (B)
    • 资助金额:
      $8.32万
    • 财政年份:
      2002
    • 负责人:
      KATO Akio
    • 依托单位:
    Reduction of antigenicity of allergen proteins by the attachment of polysaccjarides and induction of immune tolerance
    • 批准号:
      13556019
    • 项目类别:
      Grant-in-Aid for Scientific Research (B)
    • 资助金额:
      $6.02万
    • 财政年份:
      2001
    • 负责人:
      KATO Akio
    • 依托单位:
    Molecular design of lysozyme for switching the antimicrobial action
    • 批准号:
      12660115
    • 项目类别:
      Grant-in-Aid for Scientific Research (C)
    • 资助金额:
      $2.3万
    • 财政年份:
      2000
    • 负责人:
      KATO Akio
    • 依托单位:
    Function-structure of protein-polysaccharide cpmplex constructed by protein engineering.
    • 批准号:
      08660160
    • 项目类别:
      Grant-in-Aid for Scientific Research (C)
    • 资助金额:
      $1.73万
    • 财政年份:
      1996
    • 负责人:
      KATO Akio
    • 依托单位: