Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling

The classic application of ultrafiltration (UF) is for the complete retention of proteins, and in that situation, the transport behavior is well established. More open membranes with fractional retention are used when separating different proteins. However, protein transport has not been well docume...

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Main Authors: Eric Suryawirawan, Anja E. M. Janssen, Remko M. Boom, Albert van der Padt
Format: Article
Language:English
Published: MDPI AG 2024-01-01
Series:Membranes
Subjects:
Online Access:https://www.mdpi.com/2077-0375/14/1/26
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author Eric Suryawirawan
Anja E. M. Janssen
Remko M. Boom
Albert van der Padt
author_facet Eric Suryawirawan
Anja E. M. Janssen
Remko M. Boom
Albert van der Padt
author_sort Eric Suryawirawan
collection DOAJ
description The classic application of ultrafiltration (UF) is for the complete retention of proteins, and in that situation, the transport behavior is well established. More open membranes with fractional retention are used when separating different proteins. However, protein transport has not been well documented yet in the literature. The bovine serum albumin (∼69 kDa) observed rejection ranges from 0.65 to 1 using a 300 kDa molecular weight cut-off membrane at different pH, ionic strength, and pressure. We demonstrated that, especially with open UF, the transport of proteins through the membrane is dominated by advection, with insignificant diffusion effects (<i>p</i> value > 0.05). We showed that with open UF, retention is not only caused by size exclusion but also to a large extent by electrostatic interactions and oligomerization of the proteins. Mass transfer in the polarization layer was relatively independent of the pH and ionic strength. It was underestimated by common Sherwood relations due to a relatively large contribution of the reduction in the flow turbulence near the membrane by the removal of fluid through the membrane. We propose a model that allows relatively quick characterization of the rejection of proteins without prior knowledge of the pore sizes and charges based on just a limited set of experiments. Therefore, protein rejection with the open UF system can be targeted by tuning the processing conditions, which might be useful for designing protein fractionation processes.
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spelling doaj.art-0ceda9e99c0048b7801b9ca7b8d235522024-01-26T17:36:43ZengMDPI AGMembranes2077-03752024-01-011412610.3390/membranes14010026Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and ModelingEric Suryawirawan0Anja E. M. Janssen1Remko M. Boom2Albert van der Padt3Food Process Engineering Group, Wageningen University, P.O. Box 17, 6700 AA Wageningen, The NetherlandsFood Process Engineering Group, Wageningen University, P.O. Box 17, 6700 AA Wageningen, The NetherlandsFood Process Engineering Group, Wageningen University, P.O. Box 17, 6700 AA Wageningen, The NetherlandsFood Process Engineering Group, Wageningen University, P.O. Box 17, 6700 AA Wageningen, The NetherlandsThe classic application of ultrafiltration (UF) is for the complete retention of proteins, and in that situation, the transport behavior is well established. More open membranes with fractional retention are used when separating different proteins. However, protein transport has not been well documented yet in the literature. The bovine serum albumin (∼69 kDa) observed rejection ranges from 0.65 to 1 using a 300 kDa molecular weight cut-off membrane at different pH, ionic strength, and pressure. We demonstrated that, especially with open UF, the transport of proteins through the membrane is dominated by advection, with insignificant diffusion effects (<i>p</i> value > 0.05). We showed that with open UF, retention is not only caused by size exclusion but also to a large extent by electrostatic interactions and oligomerization of the proteins. Mass transfer in the polarization layer was relatively independent of the pH and ionic strength. It was underestimated by common Sherwood relations due to a relatively large contribution of the reduction in the flow turbulence near the membrane by the removal of fluid through the membrane. We propose a model that allows relatively quick characterization of the rejection of proteins without prior knowledge of the pore sizes and charges based on just a limited set of experiments. Therefore, protein rejection with the open UF system can be targeted by tuning the processing conditions, which might be useful for designing protein fractionation processes.https://www.mdpi.com/2077-0375/14/1/26protein transportultrafiltrationsolution–friction modelgeneral rejection equation
spellingShingle Eric Suryawirawan
Anja E. M. Janssen
Remko M. Boom
Albert van der Padt
Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
Membranes
protein transport
ultrafiltration
solution–friction model
general rejection equation
title Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
title_full Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
title_fullStr Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
title_full_unstemmed Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
title_short Bovine Serum Albumin Rejection by an Open Ultrafiltration Membrane: Characterization and Modeling
title_sort bovine serum albumin rejection by an open ultrafiltration membrane characterization and modeling
topic protein transport
ultrafiltration
solution–friction model
general rejection equation
url https://www.mdpi.com/2077-0375/14/1/26
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AT anjaemjanssen bovineserumalbuminrejectionbyanopenultrafiltrationmembranecharacterizationandmodeling
AT remkomboom bovineserumalbuminrejectionbyanopenultrafiltrationmembranecharacterizationandmodeling
AT albertvanderpadt bovineserumalbuminrejectionbyanopenultrafiltrationmembranecharacterizationandmodeling