α-lactalbumin and β-lactoglobulin in whey proteins were separated by HPMC(High Performance Membrane Chromatography) and GFC(Gel Filtration Chromatography). The separation mechanism of HPMC was anion-exchange, and the stationary phases were anion CIM...
α-lactalbumin and β-lactoglobulin in whey proteins were separated by HPMC(High Performance Membrane Chromatography) and GFC(Gel Filtration Chromatography). The separation mechanism of HPMC was anion-exchange, and the stationary phases were anion CIM(Convective Interaction Media) DEAE and QA disks(16×3㎜). Two types of mobile phase were used, buffer A(20mM Tris-HCI, pH 7.3) and buffer B(buffer A+1 M NaCl). The optimum mobile phase and operating condition were buffer A/Buffer B=100/0-30/70 vol%, gradient time 1 min, 30/70-10/90 vol%, gradient time 2 min. In this experimental condition, α-lactalbumin and β-lactoglobulin were separated within 5 min at a mobile phase flow rate of 4ml/min. In GFC, characterized by size exclusion, water in isocratic mode and water with TFA in gradient mode were utilized as mobile phases. Separation of the two whey proteins was performed better by HPMC than by GFC. ββ