Laboratory of Food Chemistry, Wageningen University, Bomenweg 2, 6703 HD Wageningen, The Netherlands.
J Agric Food Chem. 2011 Dec 14;59(23):12460-6. doi: 10.1021/jf2032022. Epub 2011 Nov 3.
α-Lactalbumin was glycated via the Maillard reaction in the dry state using various mono- and oligosaccharides. The reaction resulted not only in coupling of the saccharides to α-lactalbumin but also in cross-linked proteins. The glycation rate and the extent of cross-link formation were highly dependent on the saccharide used. Glycation by arabinose and xylose led to a very fast protein cross-link formation, whereas glucose showed a relatively low protein cross-linking ability. The stability of foams, created using the various glycated protein samples, depended on the type of saccharide used, the extent of glycation, and possibly the amount of cross-linked protein. Compared to nonmodified α-lactalbumin, glycation with rhamnose and fucose improved foam stability, whereas application of glucose, galacturonic acid, and their oligosaccharides did not exert a clear effect. Mass spectrometric analysis revealed that dehydration of the Amadori products is an indicator of the formation of protein cross-links.
α-乳白蛋白在干燥状态下通过美拉德反应与各种单糖和寡糖发生糖化。该反应不仅导致糖与α-乳白蛋白结合，还导致蛋白质交联。糖化率和交联程度高度依赖于所用的糖。阿拉伯糖和木糖的糖化导致蛋白质快速交联，而葡萄糖的蛋白质交联能力相对较低。使用各种糖化蛋白样品形成的泡沫的稳定性取决于所用糖的类型、糖化程度以及可能的交联蛋白量。与未修饰的α-乳白蛋白相比，用鼠李糖和岩藻糖糖化可提高泡沫稳定性，而葡萄糖、半乳糖醛酸及其寡糖的应用则没有明显效果。质谱分析表明，阿马多里产物的脱水是蛋白质交联形成的一个指标。
