Functional Properties of Glycosylated Lysozyme Secreted in Pichia pastoris

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  • SAITO Akira
    <i>Department of Biological Chemistry, Yamaguchi University</i>
  • SAKO Yukikazu
    <i>Department of Biological Chemistry, Yamaguchi University</i>
  • USUI Masakatsu
    <i>Department of Biological Chemistry, Yamaguchi University</i>
  • AZAKAMI Hiroyuki
    <i>Department of Biological Chemistry, Yamaguchi University</i>
  • KATO Akio
    <i>Department of Biological Chemistry, Yamaguchi University</i>

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  • Functional Properties of Glycosylated Lysozyme Secreted in<i>Pichia pastoris</i>

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  Various mutant lysozymes having the N-glycosylation signal sequence, R21T (Asn19-Tyr20-Thr21), G49N (Asn49- Ser50-Thr51), R21T/G49N (Asn19-Tyr20-Thr21/Asn49-Ser50-Thr51), were secreted in the Pichia pastoris expression system. The secreted amounts of these mutant glycosylated lysozymes were almost the same as those of wild-type lysozyme (about 30 mg/liter). Glycosylation of the mutant lysozymes was confirmed by SDS-PAGE patterns, Endo-H treatment, TOF-MS analysis and chemical analysis. The composition of the carbohydrate chain attached to the single glycosylated lysozymes, R21T and G49N, was GlcNAc2Man9-11, while that of the double glycosylated lysozyme, R21T/G49N, was GlcNAc4Man27-32. The results of a CD analysis and lytic activity suggested that the conformation of the single glycosylated lysozymes had been conserved, while that of the double glycosylated lysozyme was less stable. The emulsifying properties of the lysozyme when glycosylated were greatly improved, being especially noteworthy in the double glycosylated lysozyme.<br>

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