Novel functional properties of glycosylated lysozymes constructed by chemical and genetic modifications
1996
Kato, A. | Nakamura, S. | Takasaki, H. | Maki, S.
Maillard-type lysozyme-polysaccharide conjugates prepared in a controlled dry state revealed dramatic improvements of the functional properties of proteins, such as emulsifying properties and heat stability. In order to elucidate the molecular mechanism of the dramatic improvements of the functional properties of proteins by glycosylation, oligomannose- and polymannose-linked lysozymes were constructed by using genetic engineering. cDNA encoding hen egg white lysozyme was subjected to site-directed mutagenesis to have the signal sequence for asparagine-linked glycosylation (Asn-X-Thr/Ser) at the positions 19 and 49. The oligomannosyl and polymannosyl lysozymes were secreted in the yeast carrying mutant cDNAs. The polymannosyl lysozymes showed remarkable heat stability and excellent emulsifying properties. These functional properties of polymannosyl lysozymes were much higher than those of oligomannosyl lysozymes, suggesting the importance of the length of saccharide chains. The double polymannosyl lysozyme at both positions 19 and 49 showed better emulsifying properties than the single polymannosyl lysozymes.
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