{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T10:05:58Z","timestamp":1784801158517,"version":"3.55.0"},"reference-count":71,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T00:00:00Z","timestamp":1782518400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Membranes"],"abstract":"<jats:p>Protein A affinity chromatography is the gold standard for antibody purification. In practice, it is mainly performed using resin-based packed bed columns. However, for porous resins, mass transport depends on slow diffusion and, consequently, low flow rates\/long residence times are required to achieve decent binding capacities (i.e., &gt;30 mg\/mL), which leads to long processing time and low productivity. Recently, Protein A membranes have emerged as a promising alternative to Protein A columns. Membrane adsorbers, which have large pores, enable convection-based mass transport and allow high dynamic binding capacity to be achieved at a relatively short residence time (on the order of seconds). Hence, Protein A membranes can be operated at high flow rates and gain significantly improved productivity. In addition to high productivity, we recently found that Protein A membranes possess a much stronger impurity-removing capability than Protein A columns. This review introduces the advantages that Protein A membrane chromatography offers, especially those that have not been well recognized before. These advantages allow high-quality products to be obtained with significantly reduced costs.<\/jats:p>","DOI":"10.3390\/membranes16070222","type":"journal-article","created":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T02:16:44Z","timestamp":1782699404000},"page":"222","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Advantages of Protein A Membrane Chromatography: High Productivity, Strong Impurity Removal Capability, and More"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-6994-9276","authenticated-orcid":false,"given":"Yifeng","family":"Li","sequence":"first","affiliation":[{"name":"Downstream Process Development (DSPD), WuXi Biologics, 31 Yiwei Road, Waigaoqiao Free Trade Zone, Shanghai 200131, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hang","family":"Zhou","sequence":"additional","affiliation":[{"name":"Bioprocess Research and Development (BRD), WuXi Biologics, 31 Yiwei Road, Waigaoqiao Free Trade Zone, Shanghai 200131, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sherry","family":"Gu","sequence":"additional","affiliation":[{"name":"Global Biologics Development and Operations (GBDO), WuXi Biologics, 31 Yiwei Road, Waigaoqiao Free Trade Zone, Shanghai 200131, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.jchromb.2006.09.026","article-title":"Downstream processing of monoclonal antibodies\u2014Application of platform approaches","volume":"848","author":"Shukla","year":"2007","journal-title":"J. Chromatogr. B Anal. Technol. Biomed. Life Sci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.jchromb.2006.09.030","article-title":"Protein A chromatography for antibody purification","volume":"848","author":"Hober","year":"2007","journal-title":"J. Chromatogr. B Anal. Technol. Biomed. Life Sci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1002\/btpr.2324","article-title":"The role of more than 40 years of improvement in protein A chromatography in the growth of the therapeutic antibody industry","volume":"32","author":"Bolton","year":"2016","journal-title":"Biotechnol. Prog."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1016\/j.chroma.2011.03.063","article-title":"Theoretical investigation of diffusion along columns packed with fully and superficially porous particles","volume":"1218","author":"Gritti","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.biotechadv.2013.01.007","article-title":"Recent advances in bioprocessing application of membrane chromatography","volume":"31","author":"Orr","year":"2013","journal-title":"Biotechnol. Adv."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"460629","DOI":"10.1016\/j.chroma.2019.460629","article-title":"A direct comparison between membrane adsorber and packed column chromatography performance","volume":"1612","author":"Boi","year":"2020","journal-title":"J. Chromatogr. A"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s00216-022-04325-8","article-title":"Recent development and application of membrane chromatography","volume":"415","author":"Chen","year":"2023","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1080\/15422119.2023.2226128","article-title":"The transition from resin chromatography to membrane adsorbers for protein separations at industrial scale","volume":"53","author":"Qu","year":"2024","journal-title":"Sep. Purif. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"130147","DOI":"10.1016\/j.seppur.2024.130147","article-title":"A review on chromatographic membranes for antibody purification: Factors affecting binding capacity and guidelines for membrane design","volume":"357","author":"Dabaghian","year":"2025","journal-title":"Sep. Purif. Technol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"465733","DOI":"10.1016\/j.chroma.2025.465733","article-title":"Bioseparation using membrane chromatography: Innovations, and challenges","volume":"1744","author":"Chen","year":"2025","journal-title":"J. Chromatogr. A"},{"key":"ref_11","first-page":"40P","article-title":"Purification of monoclonal and polyclonal IgG with affinity membrane matrix coupled with proteins A and G","volume":"25","author":"Malakian","year":"1993","journal-title":"Am. Lab."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/bit.260480414","article-title":"Protein A immunoaffinity hollow fiber membranes for immunoglobulin G purification: Experimental characterization","volume":"48","author":"Charcosset","year":"1995","journal-title":"Biotechnol. Bioeng."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0378-4347(98)00470-8","article-title":"Purification of immunoglobulins G by protein A\/G affinity membrane chromatography","volume":"723","author":"Dancette","year":"1999","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S0376-7388(02)00257-0","article-title":"Comparison of affinity membranes for the purification of immunoglobulins","volume":"207","author":"Castilho","year":"2002","journal-title":"J. Membr. Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1021\/bp0704743","article-title":"Performance of a new protein A affinity membrane for the primary recovery of antibodies","volume":"24","author":"Boi","year":"2008","journal-title":"Biotechnol. Prog."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.2174\/1385272820666160610114814","article-title":"Advances in membrane chromatography for the capture step of monoclonal antibodies","volume":"21","author":"Boi","year":"2017","journal-title":"Curr. Org. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Br\u00e4mer, C., T\u00fcnnermann, L., Gonzalez Salcedo, A., Reif, O.W., Solle, D., Scheper, T., and Beutel, S. (2019). Membrane adsorber for the fast purification of a monoclonal antibody using Protein A chromatography. Membranes, 9.","DOI":"10.3390\/membranes9120159"},{"key":"ref_18","unstructured":"Busse, R.A., Gruenberg, M., Kuchemueller, K.B., Toeppner, K., Adametz, P., and Thom, V. (2026, June 23). Sartobind Rapid A: Comparable High Product Quality as Protein A Resins at High Productivity. Available online: https:\/\/www.sartorius.com.cn\/download\/1301732\/sartobind-rapid-a-comparability-to-resin-application-note-en-1--data.pdf."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Gr\u00fcnberg, M., Kuchem\u00fcller, K.B., T\u00f6ppner, K., and Busse, R.A. (2022). Scalable, robust and highly productive novel convecdiff membrane platform for mAb capture. Membranes, 12.","DOI":"10.3390\/membranes12070677"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Osuofa, J., and Husson, S.M. (2023). Comparative evaluation of commercial Protein A membranes for the rapid purification of antibodies. Membranes, 13.","DOI":"10.3390\/membranes13050511"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Yang, S., Braczkowski, R., Chen, S.H., Busse, R., Li, Y., Fabri, L., and Bekard, I.B. (2023). Scalability of Sartobind Rapid A membrane for high productivity monoclonal antibody capture. Membranes, 13.","DOI":"10.3390\/membranes13100815"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e99010050","DOI":"10.14440\/jbm.2025.0109","article-title":"Incorporating ultrafiltration into Protein A membrane chromatography as a strategy to reduce elution volume and buffer consumption","volume":"12","author":"Yuan","year":"2025","journal-title":"J. Biol. Methods"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"105847","DOI":"10.1016\/j.pep.2021.105847","article-title":"Removing a single-arm species by Fibro PrismA in purifying an asymmetric IgG-like bispecific antibody","volume":"182","author":"Zhang","year":"2021","journal-title":"Protein Expr. Purif."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"106823","DOI":"10.1016\/j.pep.2025.106823","article-title":"Effective and robust separation of half-antibody byproduct in bispecific antibody purification by Sartobind Rapid A Protein A membrane chromatography","volume":"237","author":"Yuan","year":"2026","journal-title":"Protein Expr. Purif."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"e99010089","DOI":"10.14440\/jbm.0279","article-title":"Enhanced aggregate separation with Sartobind\u00ae Rapid A Protein A membrane in the purification of aggregation-prone antibodies","volume":"13","author":"Yuan","year":"2026","journal-title":"J. Biol. Methods"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"106890","DOI":"10.1016\/j.pep.2026.106890","article-title":"Robust aggregate separation by Sartobind Rapid A Protein A membrane","volume":"240","author":"Yuan","year":"2026","journal-title":"Protein Expr. Purif."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"106891","DOI":"10.1016\/j.pep.2026.106891","article-title":"Deciphering the inconsistent performance of Protein A membrane on host cell protein clearance","volume":"240","author":"Yang","year":"2026","journal-title":"Protein Expr. Purif."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.pep.2018.11.011","article-title":"A brief introduction of IgG-like bispecific antibody purification: Methods for removing product-related impurities","volume":"155","author":"Li","year":"2019","journal-title":"Protein Expr. Purif."},{"key":"ref_29","first-page":"73","article-title":"Current trends and challenges in the downstream purification of bispecific antibodies","volume":"4","author":"Chen","year":"2021","journal-title":"Antib. Ther."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"105635","DOI":"10.1016\/j.pep.2020.105635","article-title":"Removing half antibody byproduct by Protein A chromatography during the purification of a bispecific antibody","volume":"172","author":"Chen","year":"2020","journal-title":"Protein Expr. Purif."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"106315","DOI":"10.1016\/j.pep.2023.106315","article-title":"Antibody aggregation can lead to reduced Protein A binding capacity and low step yield","volume":"210","author":"Yuan","year":"2023","journal-title":"Protein Expr. Purif."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"106418","DOI":"10.1016\/j.pep.2023.106418","article-title":"SEC-HPLC analysis of column load and flow-through provides critical understanding of low Protein A step yield","volume":"216","author":"Liu","year":"2024","journal-title":"Protein Expr. Purif."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.chroma.2016.06.031","article-title":"Molecular perspective of antibody aggregates and their adsorption on Protein A resin","volume":"1457","author":"Yu","year":"2016","journal-title":"J. Chromatogr. A"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.pep.2019.02.017","article-title":"A method for improving protein A chromatography\u2019s aggregate removal capability","volume":"158","author":"Zhang","year":"2019","journal-title":"Protein Expr. Purif."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"421","DOI":"10.2174\/138920109788488842","article-title":"Ion exchange chromatography of proteins and clearance of aggregates","volume":"10","author":"Yigzaw","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1080\/10826068.2012.654572","article-title":"Process development for robust removal of aggregates using cation exchange chromatography in monoclonal antibody purification with implementation of quality by design","volume":"42","author":"Xu","year":"2012","journal-title":"Prep. Biochem. Biotechnol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"427","DOI":"10.2174\/138920109788488897","article-title":"Recent advancement in application of hydrophobic interaction chromatography for aggregate removal in industrial purification process","volume":"10","author":"Lu","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.chroma.2013.04.018","article-title":"Evaluating antibody monomer separation from associated aggregates using mixed-mode chromatography","volume":"1294","author":"Gao","year":"2013","journal-title":"J. Chromatogr. A"},{"key":"ref_39","first-page":"30","article-title":"Ceramic hydroxyapatite chromatography plays a critical role in bispecific antibody purification process for impurity removal","volume":"6","author":"Waller","year":"2022","journal-title":"Antib. Ther."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1186\/s40643-023-00713-9","article-title":"Harnessing ceramic hydroxyapatite as an effective polishing strategy to remove product- and process-related impurities in bispecific antibody purification","volume":"10","author":"Ingavat","year":"2023","journal-title":"Bioresour. Bioprocess."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Rup\u010d\u00edkov\u00e1, V., Moln\u00e1r, T., Kur\u00e1k, T., and Polakovi\u010d, M. (2025). Antibody aggregate removal by multimodal chromatography. Molecules, 30.","DOI":"10.3390\/molecules30112363"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"467126","DOI":"10.1016\/j.chroma.2026.467126","article-title":"Exploiting ligand-driven salt selectivity for aggregate retention: Enhancing monomer resolution on a high elution pH Protein A membrane","volume":"1783","author":"Guth","year":"2026","journal-title":"J. Chromatogr. A"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"464523","DOI":"10.1016\/j.chroma.2023.464523","article-title":"Evaluation of mild pH elution protein A resins for antibodies and Fc-fusion proteins","volume":"1713","author":"Wang","year":"2024","journal-title":"J. Chromatogr. A"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"106677","DOI":"10.1016\/j.pep.2025.106677","article-title":"Praesto Jetted A50 HipH, a mild pH elution protein A resin, exhibits improved aggregate separation capability and protein elution from it shows unique response to mobile phase additive sodium chloride","volume":"229","author":"Lu","year":"2025","journal-title":"Protein Expr. Purif."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1002\/bit.22304","article-title":"Host cell proteins in biologics development: Identification, quantitation and risk assessment","volume":"103","author":"Wang","year":"2009","journal-title":"Biotechnol. Bioeng."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1002\/bit.22494","article-title":"Degradation of an Fc-fusion recombinant protein by host cell proteases: Identification of a CHO cathepsin D protease","volume":"104","author":"Robert","year":"2009","journal-title":"Biotechnol. Bioeng."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1002\/bit.22982","article-title":"Fragmentation of a highly purified monoclonal antibody attributed to residual CHO cell protease activity","volume":"108","author":"Gao","year":"2011","journal-title":"Biotechnol. Bioeng."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1002\/jps.23931","article-title":"Impact of residual impurities and contaminants on protein stability","volume":"103","author":"Wang","year":"2014","journal-title":"J. Pharm. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1016\/j.xphs.2016.02.029","article-title":"Residual host cell protein promotes polysorbate 20 degradation in a sulfatase drug product leading to free fatty acid particles","volume":"105","author":"Dixit","year":"2016","journal-title":"J. Pharm. Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.chroma.2018.03.060","article-title":"Evaluation of recent Protein A stationary phase innovations for capture of biotherapeutics","volume":"1554","author":"Pabst","year":"2018","journal-title":"J. Chromatogr. A"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"123989","DOI":"10.1016\/j.jchromb.2023.123989","article-title":"Rapid purification of mAb using protein a membranes yielding high HCP clearance","volume":"1232","author":"Gehrmann","year":"2024","journal-title":"J. Chromatogr. B Anal. Technol. Biomed. Life Sci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e3508","DOI":"10.1002\/btpr.3508","article-title":"Assessment of membrane-based downstream purification processes as a replacement to traditional resin bead for monoclonal antibody purification","volume":"41","author":"Pasquier","year":"2025","journal-title":"Biotechnol. Prog."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.pep.2017.04.006","article-title":"Effective strategies for host cell protein clearance in downstream processing of monoclonal antibodies and Fc-fusion proteins","volume":"134","author":"Li","year":"2017","journal-title":"Protein Expr. Purif."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"106113","DOI":"10.1016\/j.pep.2022.106113","article-title":"Two major mechanisms contributing to copurification of CHO host cell proteins and strategies to minimize their negative impact","volume":"197","author":"Li","year":"2022","journal-title":"Protein Expr. Purif."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.chroma.2013.03.028","article-title":"Characterization and removal of aggregates formed by nonspecific interaction of IgM monoclonal antibodies with chromatin catabolites during cell culture production","volume":"1291","author":"Gan","year":"2013","journal-title":"J. Chromatogr. A"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.chroma.2014.03.010","article-title":"Nonspecific interactions of chromatin with immunoglobulin G and protein A, and their impact on purification performance","volume":"1340","author":"Gagnon","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.chroma.2014.11.052","article-title":"Chromatin-mediated depression of fractionation performance on electronegative multimodal chromatography media, its prevention, and ramifications for purification of immunoglobulin G","volume":"1374","author":"Gagnon","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_58","unstructured":"Hicks, M., Summers, B., Jackson, R., and Johansson, H. (2026, June 23). Praesto\u2122 Jetted A50 HipH. A Novel Protein A Resin Designed Specifically for Elution of Fc-Containing Molecules at Higher pH Levels. Available online: https:\/\/www.purolite.com\/dam\/jcr:a0b47168-3194-457a-98bd-db5cfabfd489\/Praesto-Jetted-A50-HipH-Poster.pdf."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"106859","DOI":"10.1016\/j.pep.2025.106859","article-title":"The advantage of high pH eluting Protein A resins over their regular counterparts in aggregate and host cell protein clearance","volume":"239","author":"Li","year":"2026","journal-title":"Protein Expr. Purif."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1002\/btpr.50","article-title":"Host cell protein clearance during protein A chromatography: Development of an improved column wash step","volume":"24","author":"Shukla","year":"2008","journal-title":"Biotechnol. Prog."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1002\/biot.201100479","article-title":"Studying host cell protein interactions with monoclonal antibodies using high throughput protein A chromatography","volume":"7","author":"Sisodiya","year":"2012","journal-title":"Biotechnol. J."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1002\/btpr.1514","article-title":"Select host cell proteins coelute with monoclonal antibodies in protein A chromatography","volume":"28","author":"Nogal","year":"2012","journal-title":"Biotechnol. Prog."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1002\/bit.25158","article-title":"Identification and characterization of host cell protein product-associated impurities in monoclonal antibody bioprocessing","volume":"111","author":"Levy","year":"2014","journal-title":"Biotechnol. Bioeng."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1002\/btpr.2272","article-title":"Characterization of the co-elution of host cell proteins with monoclonal antibodies during protein A purification","volume":"32","author":"Zhang","year":"2016","journal-title":"Biotechnol. Prog."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"e99010087","DOI":"10.14440\/jbm.0213","article-title":"Cation exchange membrane chromatography: An efficient alternative to multi-column for avoiding the impact of loading density variation on performance","volume":"13","author":"Yuan","year":"2026","journal-title":"J. Biol. Methods"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.chroma.2011.12.106","article-title":"Improving affinity chromatography resin efficiency using semi-continuous chromatography","volume":"1227","author":"Mahajan","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1002\/biot.201200068","article-title":"Periodic counter-current chromatography\u2014Design and operational considerations for integrated and continuous purification of proteins","volume":"7","author":"Godawat","year":"2012","journal-title":"Biotechnol. J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"3018","DOI":"10.1002\/bit.24584","article-title":"Integrated continuous production of recombinant therapeutic proteins","volume":"109","author":"Warikoo","year":"2012","journal-title":"Biotechnol. Bioeng."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/bit.28695","article-title":"Continuous multi-column capture of monoclonal antibodies with convective diffusive membrane adsorbers","volume":"121","author":"Schmitz","year":"2024","journal-title":"Biotechnol. Bioeng."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"465201","DOI":"10.1016\/j.chroma.2024.465201","article-title":"Comparison of batch and continuous multi-column capture of monoclonal antibodies with convective diffusive membrane adsorbers","volume":"1732","author":"Schmitz","year":"2024","journal-title":"J. Chromatogr. A"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1002\/bit.28884","article-title":"Streamlined clarification and capture process for monoclonal antibodies using fluidized bed centrifugation and multi-column chromatography with membrane adsorbers","volume":"122","author":"Schmitz","year":"2025","journal-title":"Biotechnol. Bioeng."}],"container-title":["Membranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2077-0375\/16\/7\/222\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T09:44:26Z","timestamp":1784799866000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2077-0375\/16\/7\/222"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,27]]},"references-count":71,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["membranes16070222"],"URL":"https:\/\/doi.org\/10.3390\/membranes16070222","relation":{},"ISSN":["2077-0375"],"issn-type":[{"value":"2077-0375","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,27]]}}}