Adsorbed protein secondary and tertiary structures by circular dichroism and infrared spectroscopy with refractive index matched emulsions

被引：98

作者：

Husband, FA ^{[1
]}

Garrood, MJ ^{[1
]}

Mackie, AR ^{[1
]}

Burnett, GR ^{[1
]}

Wilde, PJ ^{[1
]}

机构：

[1] Inst Food Res, Norwich NR4 7UA, Norfolk, England

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2001年 / 49卷 / 02期

关键词：

emulsion; secondary structure; beta-lactoglobulin; BSA; CD; refractive index matched emulsion;

D O I：

10.1021/jf000688z

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

The secondary structure of protein adsorbed at the emulsion interface has been studied in refractive index matched emulsions using the techniques of circular dichroism (CD) and Fourier transform infrared spectroscopy. Bovine serum albumin (BSA) and bovine beta -lactoglobulin (beta lg) stabilized emulsions were studied, and the refractive index was altered by the addition of glycerol or polyethylene glycol. The effect df additive on the solution and adsorbed protein structure in addition to the effect of adsorption time was considered. Both adsorption and glycerol addition alter protein secondary structure; however, the majority of secondary structure remains. Small changes are observed in the secondary structure of adsorbed protein with time. Near-ultraviolet CD studies showed the effect of glycerol and adsorption on the aromatic groups. BSA showed small changes both upon the addition of glycerol to protein in solution and upon adsorption. beta lg showed slightly larger changes upon the addition of glycerol to protein in solution and a larger change-upon adsorption.

引用

页码：859 / 866

页数：8

共 27 条

[1] Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study [J].