Veerman Cecile, Baptist Harry, Sagis Leonard M C, van der Linden Erik
Food Physics Group, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 8129, The Netherlands.
J Agric Food Chem. 2003 Jun 18;51(13):3880-5. doi: 10.1021/jf0261396.
The objective of this study was to obtain beta-lactoglobulin (beta-lg) gels at very low protein concentrations using a new multistep Ca(2+)-induced cold gelation process. In the conventional cold gelation process, salt free beta-lg solutions were heated at neutral pH, cooled, and cross-linked by adding salts. In our new process, first, long linear beta-lg fibrils were formed at pH 2. Solutions of these fibrils were cooled, and subsequently, the pH was adjusted to 7 or 8. Transmission electron microscopy studies showed that the long linear fibrils formed at pH 2 were stable when the pH was adjusted to 7 or 8. In the final step, the fibrils were cross-linked using CaCl(2). Using rheological measurements, the critical percolation concentration was determined. In the new multistep cold gelation process, the critical percolation concentration was an order of magnitude lower than in the conventional cold gelation method.
本研究的目的是使用一种新的多步钙诱导冷胶凝过程,在非常低的蛋白质浓度下获得β-乳球蛋白(β-lg)凝胶。在传统的冷胶凝过程中,无盐的β-lg溶液在中性pH下加热,冷却后通过添加盐进行交联。在我们的新工艺中,首先在pH 2时形成长线性β-lg原纤维。这些原纤维的溶液冷却后,随后将pH值调节至7或8。透射电子显微镜研究表明,当pH值调节至7或8时,在pH 2时形成的长线性原纤维是稳定的。在最后一步中,使用氯化钙对原纤维进行交联。通过流变学测量确定了临界渗滤浓度。在新的多步冷胶凝过程中,临界渗滤浓度比传统冷胶凝方法低一个数量级。