A DIFFERENTIAL MICROCALORIMETRIC STUDY OF WHEY PROTEINS AND THEIR BEHAVIOR IN OIL-IN-WATER EMULSIONS

被引：52

作者：

CORREDIG, M ^{[1
]}

DALGLEISH, DG ^{[1
]}

机构：

[1] UNIV GUELPH,DEPT FOOD SCI,GUELPH,ON N1G 2W1,CANADA

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 1995年 / 4卷 / 06期

关键词：

DIFFERENTIAL MICROCALORIMETRIC STUDY; OIL-IN-WATER EMULSIONS; WHEY PROTEINS;

D O I：

10.1016/0927-7765(95)01186-M

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Oil-in-water emulsions (20% soya oil, 1% protein) have been prepared containing lysozyme or isolates of alpha-lactalbumin and beta-lactoglobulin from whey protein. The structural characteristics of these proteins adsorbed at an oil/water interface were determined by following their thermal transitions using differential scanning microcalorimetry. Thermograms of the proteins in the adsorbed state differed markedly from the corresponding transitions seen for the proteins in solution. This suggests that the proteins underwent substantial changes in secondary and tertiary structure upon adsorption. In general, for all the proteins studied, a net decrease in the total energy absorbed during denaturation was found when the proteins were in an adsorbed state. Both lysozyme and alpha-lactalbumin were in part ''surface denatured'', and they showed a certain degree of reversibility between solution and the adsorbed state. beta-Lactoglobulin showed the highest degree of denaturation upon adsorption and the conformational change was irreversible.

引用

页码：411 / 422

页数：12

共 33 条

[1] ADSORPTION BEHAVIOR OF MILK-PROTEINS ON POLYSTYRENE LATEX - A STUDY BASED ON SEDIMENTATION FIELD-FLOW FRACTIONATION AND DYNAMIC LIGHT-SCATTERING [J].