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J Chromatogr A ; 1438: 143-9, 2016 Mar 18.
Article in English | MEDLINE | ID: mdl-26898148

ABSTRACT

The application of membrane adsorbers instead of classical packed bed columns for protein fractionation is still a growing field. In the case of egg white protein fractionation, the application of classical chromatography is additionally limited due to its high viscosity that impairs filtration. By using tangential flow membrane adsorbers as stationary phase this limiting factor can be left out, as they can be loaded with particle containing substrates. The flow conditions existing in tangential flow membrane adsorbers are not fully understood yet. Thus, the aim of the present study was to gain a deeper understanding of the transport mechanisms in tangential flow membrane adsorbers. It was found that loading in recirculation mode instead of single pass mode increased the binding capacity (0.39 vs. 0.52 mg cm(-2)). Further, it was shown that either higher flow rates (0.39 mg cm(-2) vs. 0.57 mg cm(-2) at 1 CV min(-1) or 20 CV min(-1), respectively) or higher amounts of the target protein in the feed (0.24 mg cm(-2) vs. 0.85 mg cm(-2) for 2.5 or 39.0 g lysozyme, respectively) led to more protein binding. These results show that, in contrast to radial flow or flat sheet membrane adsorbers, the transport in tangential flow membrane adsorbers is not purely based on convection, but on a mix of convection and diffusion. Additionally, investigations concerning the influence of fouling formation were performed that can lead to transport limitations. It was found that this impact is neglectable. It can be concluded that the usage of tangential flow membrane adsorbers is very recommendable for egg white protein fractionations, although the transport is partly diffusion-limited.


Subject(s)
Chemical Fractionation/methods , Egg Proteins/isolation & purification , Muramidase/isolation & purification , Adsorption , Chemical Fractionation/instrumentation , Chromatography , Diffusion , Egg Proteins/chemistry , Filtration , Membranes, Artificial , Muramidase/metabolism , Protein Binding
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