Chromatography and intrinsic fluorescence studies of possible structural evolution of globular proteins during ultrafiltration.
Résumé
Ultrafiltration (UF) is a sepn. process widely used for filtration of proteins. For applications with high added value we should ensure that they are not denatured, which could lead to a loss of functional properties. We propose a study methodol. based on model expts. able to voluntary denature proteins in a mech./thermal way and the comparison of final states with those obtained in UF retentate after long time filtration. The approach is validated by two complementary anal. techniques: intrinsic fluorescence and reverse phase HPLC (RP-HPLC). [on SciFinder(R)]