The role of polysaccharide-chain attachment to lysozyme in the excellent emulsifying properties of polymannosyl lysozyme

Y. Shu, Soichiro Nakamura, A. Kato
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引用次数: 3

Abstract

Polymannosyl lysozyme (G49N), which is polymannosylated at the position 49 by genetic modification, exhibited excellent emulsifying properties at low concentrations compared with a commercial emulsifier, Sunsoft SE-16. The polymannosyl chain was removed from G49N by the treatment with hydrazine anhydrous without any degradation of the chain. The removal of polymannosyl chain resulted in a dramatic decrease in the emulsifying properties, while the mixture of lysozyme and the polymannosyl chain did not exhibited good emulsifying properties. This suggests that the polysaccharide-chain attachment to lysozyme is critical for the excellent emulsifying properties of polymannosyl lysozyme.
多糖链与溶菌酶的结合在聚甘露糖基溶菌酶优良乳化性能中的作用
聚甘露糖基溶菌酶(G49N)通过基因修饰在49位进行了聚甘露糖基化,与商用乳化剂Sunsoft SE-16相比,G49N在低浓度下具有优异的乳化性能。用无水联氨法去除G49N中的聚甘露糖基链,无任何降解。聚甘露糖基链的去除导致其乳化性能急剧下降,而溶菌酶与聚甘露糖基链的混合物则没有表现出良好的乳化性能。这表明多糖链与溶菌酶的结合是聚甘露糖基溶菌酶具有优异乳化性能的关键。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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