Husband F A, Garrood M J, Mackie A R, Burnett G R, Wilde P J
Institute of Food Research, Norwich Research Park, Colney Lane, Norwich NR4 7UA, United Kingdom.
J Agric Food Chem. 2001 Feb;49(2):859-66. doi: 10.1021/jf000688z.
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 (betalg) stabilized emulsions were studied, and the refractive index was altered by the addition of glycerol or polyethylene glycol. The effect of 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. betalg showed slightly larger changes upon the addition of glycerol to protein in solution and a larger change upon adsorption.
利用圆二色性（CD）和傅里叶变换红外光谱技术，在折射率匹配的乳液中研究了吸附在乳液界面的蛋白质的二级结构。研究了牛血清白蛋白（BSA）和牛β-乳球蛋白（βlg）稳定的乳液，并通过添加甘油或聚乙二醇来改变折射率。除了吸附时间的影响外，还考虑了添加剂对溶液和吸附蛋白质结构的影响。吸附和添加甘油都会改变蛋白质的二级结构；然而，大部分二级结构仍然保留。随着时间的推移，吸附蛋白质的二级结构出现了微小变化。近紫外CD研究表明了甘油和吸附对芳香基团的影响。在溶液中向蛋白质添加甘油以及吸附时，BSA都出现了微小变化。在溶液中向蛋白质添加甘油时，βlg的变化略大，而吸附时变化更大。
