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Membranes
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Membrane Chromatography for Biomolecules Purification
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Membrane Chromatography for Biomolecules Purification

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Membrane Applications".

Deadline for manuscript submissions: closed (31 July 2019) | Viewed by 27264

Special Issue Editor

Dr. Cristiana Boi

E-Mail Website
Guest Editor
Department of Civil, Chemical, Environmental and Materials Engineering, Alma Mater Studiorum-Università di Bologna, Via Terracini 34, 40128 Bologna, Italy
Interests: membrane separation processes; membrane chromatography; mixed matrix membranes; protein purification; bioseparations; ultrafiltration; membrane bioreactors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Adsorptive membranes play an important role in the purification of proteins and biomolecules such as viruses, viral vectors, plasmid DNA, extracellular vesicles, and many others. The concept of membrane chromatography was developed in the 1980s to solve the diffusion limitations of packed-bed chromatography columns. However, because of the limited binding capacity of the membrane support materials, the industrial application of membrane chromatography was not successful. Nowadays, the need to recover valuable biomolecules combined with the discovery of novel and improved membrane materials has fostered an important research effort in this area. Indeed, membrane chromatography is gaining an increasing popularity in the bioprocess industry, especially in polishing step applications for the removal of contaminants, where disposable membrane adsorbers play an important role.

This themed issue aims to collect key contributions to the field and give an overview of novel adsorptive membranes with improved properties and functionalities, new applications, and more efficient module design and mathematical modelling, addressing both fundamental aspects and applied research.

Prof. Cristiana Boi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Membranes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Membrane chromatography
  • Membrane adsorbers
  • Affinity
  • Ion exchange
  • Hydrophobic interactions
  • Biomolecules
  • Proteins
  • Antibodies
  • Surface modification
  • Mathematical modelling

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Published Papers (5 papers)

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Research

17 pages, 2388 KiB  
Article
A Summary of Practical Considerations for the Application of the Steric Exclusion Chromatography for the Purification of the Orf Viral Vector
by Friederike Eilts, Keven Lothert, Sabri Orbay, Felix Pagallies, Ralf Amann and Michael W. Wolff
Membranes 2022, 12(11), 1070; https://doi.org/10.3390/membranes12111070 - 29 Oct 2022
Cited by 6 | Viewed by 3308
Abstract
Steric exclusion chromatography (SXC) is a promising purification method for biological macromolecules such as the Orf virus (ORFV) vector. The method’s principle is closely related to conventional polyethylene glycol (PEG) precipitation, repeatedly implementing membranes as porous chromatographic media. In the past decade, several [...] Read more.
Steric exclusion chromatography (SXC) is a promising purification method for biological macromolecules such as the Orf virus (ORFV) vector. The method’s principle is closely related to conventional polyethylene glycol (PEG) precipitation, repeatedly implementing membranes as porous chromatographic media. In the past decade, several purification tasks with SXC showed exceptionally high yields and a high impurity removal. However, the effect of varying process parameters, on the precipitation success and its limitations to SXC, is not yet well understood. For this reason, the precipitation behavior and SXC adaptation for ORFV were investigated for the PEG/ORFV contact time, the membranes pore size, and the type and concentration of ions. All three parameters influenced the ORFV recoveries significantly. A small pore size and a long contact time induced filtration effects and inhibited a full virus recovery. The application of salts had complex concentration-dependent effects on precipitation and SXC yields, and ranged from a complete prevention of precipitation in the presence of kosmotropic substances to increased efficiencies with Mg2+ ions. The latter finding might be useful to reduce PEG concentrations while maintaining high yields. With this knowledge, we hope to clarify several limitations of SXC operations and improve the tool-set for a successful process adaptation. Full article
(This article belongs to the Special Issue Membrane Chromatography for Biomolecules Purification)
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15 pages, 3136 KiB  
Article
Electrospun Weak Anion-Exchange Fibrous Membranes for Protein Purification
by Shu-Ting Chen, S. Ranil Wickramasinghe and Xianghong Qian
Membranes 2020, 10(3), 39; https://doi.org/10.3390/membranes10030039 - 1 Mar 2020
Cited by 16 | Viewed by 4324
Abstract
Membrane based ion-exchange (IEX) and hydrophobic interaction chromatography (HIC) for protein purification is often used to remove impurities and aggregates operated under the flow-through mode. IEX and HIC are also limited by capacity and recovery when operated under bind-and-elute mode for the fractionation [...] Read more.
Membrane based ion-exchange (IEX) and hydrophobic interaction chromatography (HIC) for protein purification is often used to remove impurities and aggregates operated under the flow-through mode. IEX and HIC are also limited by capacity and recovery when operated under bind-and-elute mode for the fractionation of proteins. Electrospun nanofibrous membrane is characterized by its high surface area to volume ratio and high permeability. Here tertiary amine ligands are grafted onto the electrospun polysulfone (PSf) and polyacrylonitrile (PAN) membrane substrates using UV-initiated polymerization. Static and dynamic binding capacities for model protein bovine serum albumin (BSA) were determined under appropriate bind and elute buffer conditions. Static and dynamic binding capacities in the order of ~100 mg/mL were obtained for the functionalized electrospun PAN membranes whereas these values reached ~200 mg/mL for the functionalized electrospun PSf membranes. Protein recovery of over 96% was obtained for PAN-based membranes. However, it is only 56% for PSf-based membranes. Our work indicates that surface modification of electrospun membranes by grafting polymeric ligands can enhance protein adsorption due to increased surface area-to-volume ratio. Full article
(This article belongs to the Special Issue Membrane Chromatography for Biomolecules Purification)
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12 pages, 1448 KiB  
Article
Affinity Membranes and Monoliths for Protein Purification
by Eleonora Lalli, Jouciane S. Silva, Cristiana Boi and Giulio C. Sarti
Membranes 2020, 10(1), 1; https://doi.org/10.3390/membranes10010001 - 24 Dec 2019
Cited by 31 | Viewed by 6821
Abstract
Affinity capture represents an important step in downstream processing of proteins and it is conventionally performed through a chromatographic process. The performance of this step highly depends on the type of matrix employed. In particular, resin beads and convective materials, such as membranes [...] Read more.
Affinity capture represents an important step in downstream processing of proteins and it is conventionally performed through a chromatographic process. The performance of this step highly depends on the type of matrix employed. In particular, resin beads and convective materials, such as membranes and monoliths, are the commonly available supports. The present work deals with non-competitive binding of bovine serum albumin (BSA) on different chromatographic media functionalized with Cibacron Blue F3GA (CB). The aim is to set up the development of the purification process starting from the lab-scale characterization of a commercially available CB resin, regenerated cellulose membranes and polymeric monoliths, functionalized with CB to identify the best option. The performance of the three different chromatographic media is evaluated in terms of BSA binding capacity and productivity. The experimental investigation shows promising results for regenerated cellulose membranes and monoliths, whose performance are comparable with those of the packed column tested. It was demonstrated that the capacity of convective stationary phases does not depend on flow rate, in the range investigated, and that the productivity that can be achieved with membranes is 10 to 20 times higher depending on the initial BSA concentration value, and with monoliths it is approximately twice that of beads, at the same superficial velocity. Full article
(This article belongs to the Special Issue Membrane Chromatography for Biomolecules Purification)
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15 pages, 3371 KiB  
Article
Membrane Adsorber for the Fast Purification of a Monoclonal Antibody Using Protein A Chromatography
by Chantal Brämer, Lisa Tünnermann, Alina Gonzalez Salcedo, Oscar-Werner Reif, Dörte Solle, Thomas Scheper and Sascha Beutel
Membranes 2019, 9(12), 159; https://doi.org/10.3390/membranes9120159 - 27 Nov 2019
Cited by 21 | Viewed by 7367
Abstract
Monoclonal antibodies are conquering the biopharmaceutical market because they can be used to treat a variety of diseases. Therefore, it is very important to establish robust and optimized processes for their production. In this article, the first step of chromatography (Protein A chromatography) [...] Read more.
Monoclonal antibodies are conquering the biopharmaceutical market because they can be used to treat a variety of diseases. Therefore, it is very important to establish robust and optimized processes for their production. In this article, the first step of chromatography (Protein A chromatography) in monoclonal antibody purification was optimized with a focus on the critical elution step. Therefore, different buffers (citrate, glycine, acetate) were tested for chromatographic performance and product quality. Membrane chromatography was evaluated because it promises high throughputs and short cycle times. The membrane adsorber Sartobind® Protein A 2 mL was used to accelerate the purification procedure and was further used to perform a continuous chromatographic run with a four-membrane adsorber-periodic counter-current chromatography (4MA-PCCC) system. It was found that citrate buffer at pH 3.5 and 0.15 M NaCl enabled the highest recovery of >95% and lowest total aggregate content of 0.26%. In the continuous process, the capacity utilization of the membrane adsorber was increased by 20%. Full article
(This article belongs to the Special Issue Membrane Chromatography for Biomolecules Purification)
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12 pages, 2206 KiB  
Article
Performance Comparison of a Laterally-Fed Membrane Chromatography (LFMC) Device with a Commercial Resin Packed Column
by Pedram Madadkar, Rahul Sadavarte and Raja Ghosh
Membranes 2019, 9(11), 138; https://doi.org/10.3390/membranes9110138 - 29 Oct 2019
Cited by 12 | Viewed by 4175
Abstract
The use of conventional membrane adsorbers such as radial flow devices is largely restricted to flow-through applications, such as virus and endotoxin removal, as they fail to give acceptable resolution in bind-and-elute separations. Laterally-fed membrane chromatography or LFMC devices have been specifically developed [...] Read more.
The use of conventional membrane adsorbers such as radial flow devices is largely restricted to flow-through applications, such as virus and endotoxin removal, as they fail to give acceptable resolution in bind-and-elute separations. Laterally-fed membrane chromatography or LFMC devices have been specifically developed to combine high-speed with high-resolution. In this study, an LFMC device containing a stack of strong cation exchange membranes was compared with an equivalent resin packed column. Preliminary characterization experiments showed that the LFMC device had a significantly greater number of theoretical plates per metre than the column. These devices were used to separate a ternary model protein mixture consisting of ovalbumin, conalbumin and lysozyme. The resolution obtained with the LFMC device was better than that obtained with the column. For instance, the LFMC device could resolve lysozyme dimer from lysozyme monomer, which was not possible using the column. In addition, the LFMC device could be operated at lower pressure and at significantly higher flow rates. The devices were then compared based on an application case study, i.e., preparative separation of monoclonal antibody charge variants. The LFMC device gave significantly better separation of these variants than the column. Full article
(This article belongs to the Special Issue Membrane Chromatography for Biomolecules Purification)
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