Stabilization of lysozyme by introducing N-glycosylation signal sequence

Tadashi Ueda, Hiroki Iwashita, Yoshio Hashimoto, Taiji Imoto

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19 Citations (Scopus)

Abstract

We designed mutant lysozymes with N-glycosylation signal sequences (Asn48-Gly49-Thr-50 and Asn87-Ile88-Thr89) by substituting Asp to Asn at positions 48 and 87. When these mutant lysozymes were expressed by using yeast (Saccharomyces cerevisiae) in Burkholder minimum medium, N-glycosylation occurred in both lysozymes. The mutant lysozyme with the oligosaccharide at Asn87 showed a similar character to a reported polymannosyl lysozyme. As judged from the thermodynamic stabilities of the lysozymes obtained by the guanidine hydrochloride denaturation method, the oligosaccharide-bearing mutant lysozymes were more stable by 0.4-1.6 kcal/mol than the corresponding unglycosylated lysozymes. Therefore, it is suggested that the introduction of an N-glycosylation signal sequence into a protein is an effective means to increase the stability of the protein.

Original languageEnglish
Pages (from-to)157-161
Number of pages5
JournalJournal of Biochemistry
Volume119
Issue number1
DOIs
Publication statusPublished - Jan 1 1996

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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