Molecular mechanism of the excellent emulsifying properties of phosvitin-galactomannan conjugate

被引：15

作者：

Khan, MAS ^{[1
]}

Babiker, EFE ^{[1
]}

Azakami, H ^{[1
]}

Kato, A ^{[1
]}

机构：

[1] Yamaguchi Univ, Dept Biol Chem, Yamaguchi 753, Japan

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1999年 / 47卷 / 06期

关键词：

chymotrypsin; emulsifying properties; galactomannan; pepsin; phosvitin; trypsin;

D O I：

10.1021/jf9806659

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

The emulsifying properties of native and N- and C-terminal-deleted phosvitin (protease digests) were compared after conjugation with galactomannan. The emulsifying properties of Maillard-type phosvitin-galactomannan conjugates were greatly improved, whereas those of the protease-digested phosvitin-galactomannan conjugates were not so dramatically improved. Phosvitin was highly glycosylated with galactomannan; whereas the protease-digested phosvitin conjugate consisting of a highly phosphorylated core peptide fragment was not. The results suggest that both N and C termini of the peptide moiety, digested by protease, were essential for the improvement of emulsifying properties of phosvitin-galactomannan conjugates. In addition, the role of N and C termini as anchors in oil droplets was supported from the comparative studies of native phosvitin, phosvitin-galactomannan conjugates, and protease-digested phosvitin-galactomannan conjugates.

引用

页码：2262 / 2266

页数：5

共 13 条

[1]

BURLEY RW, 1989, AVIAN EGG CHEM BIOL, P201

[2] Oligophosphopeptides of varied structural complexity derived from the egg phosphoprotein, phosvitin [J].