Functional improvement of alginic acid by conjugating with beta-lactoglobulin

被引：29

作者：

Hattori, M

Aiba, Y

Nagasawa, K

Takahashi, K

机构：

[1] Dept. of Applied Biological Science, Faculty of Agriculture, Tokyo Univ. of Agric. and Technology, Fuchu City, Tokyo 183

来源：

JOURNAL OF FOOD SCIENCE | 1996年 / 61卷 / 06期

关键词：

alginic acid; beta-lactoglobulin; neoglycoconjugate; protein conjugation; lipocalin;

D O I：

10.1111/j.1365-2621.1996.tb10954.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Two bovine beta-lactoglobulin-alginic acid (beta-LG-ALG) conjugates were prepared to improve the function of ALG by using water-soluble carbodiimide and the Maillard reaction. Fluorescence studies suggested that the conformation around Trp had been changed in each conjugate and that the surface of each conjugate was covered with polysaccharide chain. Structural analyses with monoclonal antibodies indicated that the conformation around 15Val-29IIe (beta-sheet) in each conjugate had changed, while the native structure was maintained around 125Thr-135Lys (alpha-helix). After conjugating with beta-LG, ALG showed retinol-binding and high emulsifying ability. The aggregating property of ALG in acid and in the presence of Ca2+ was improved in each conjugate.

引用

页码：1171 / 1176

页数：6

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