Abstract
Abstract To compare actual and effective porous structure in operative conditions of ultrafiltration membranes, flux, retention, and the amount of adsorbed protein have been measured for 0.1% w/w aqueous solutions of several proteins [lysozyme, pepsin, bovine serum albumin (BSA), lipase, and γ-globulin] with molecular weights from 14.6 to 150 kD tangentially filtered through two asymmetric polysulfone membranes, E-100 and E-500. From retention and flux experiments, the dependency of mass transfer coefficients on molecular volume has been analyzed. Results imply that protein molecules behave as being slightly uncoiled, especially when filtered through the smallest pore size membrane. By using a simple sieving model, retention data allow pore size distributions to be obtained. The data are modified by taking into account adsorption and volume hindrance effects in operational conditions.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
