Retention of modified BSA by ultrafiltration membranes

摘要: BACKGROUND The efficiency of protein purification depends on membrane pore size and electrostatic repulsion between a surface. The current study investigates how deliberate modification affects the repulsion, degree separation transmembrane flux. RESULTS The experiments were performed with bovine serum albumin (BSA) modified by guanidation, succinylation citraconation. latter is reversible can be used to improve separation. Modified native proteins filtrated through polyethersulphone PES-20 in dead-end cross-flow filtration modes at pH 5–10. Guanidation diminished electronegativity protein. In mode, relative flux BSA decreased 0.45–0.7 pure water over 27.5 min. case unmodified BSA, average drop was 0.3–0.5. guanidated increased 11% acidic conditions. Succinylation citraconation electronegativity. remained close declining 0.2–0.4, greater than 95% alkaline conditions both operational modes. CONCLUSION Suggested modifications do not require changes chemistry bulk suspensions membranes, but increase rejection keeping high flux. suggested approach novel holds promise achieving purity level therapeutic required drug authorities. Under investigated best results observed for mode © 2014 Society Chemical Industry