Capillary electrophoresis of caseino-peptides: influence of applied voltage and column temperature

摘要

The peptides formed upon the action of purified cardoon rennet on the Ala189-Phe190-Leu191-Leu192- Tyr193 beta-casein fragment were separated by capillary electrophoresis in an uncoated fused silica capillary. There was a linear correlation betweenelectrophoretic mobility and Z/M2/3 (Z, net charge; M, molecular mass) under all experimental conditions tested; under the optimal conditions, 25 kV and 40deg C, the correlation coefficient was 0.994. It is concluded that the method is rapid (migration times <7 min) and can be used to study the action of aspartic proteinases on the C-terminal domain of beta-casein, and to elucidate their effect on cheese quality.