<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11(100)</volume><submitter>Dhadge VL</submitter><pubmed_abstract>FucoPol, a fucose-containing extracellular polysaccharide (EPS) produced by bacterium Enterobacter A47 using glycerol as the carbon source, was employed as a coating material for magnetic particles (MPs), which were subsequently functionalized with an artificial ligand for the capture of antibodies. The performance of the modified MPs (MP-EPS-22/8) for antibody purification was investigated using direct magnetic separation alone or combined with an aqueous two-phase system (ATPS) composed of polyethylene glycol (PEG) and dextran. In direct magnetic capturing, and using pure protein solutions of human immunoglobulin G (hIgG) and bovine serum albumin (BSA), MP-EPS-22/8 bound 120 mg hIgG g(-1) MPs, whereas with BSA only 10 ± 2 mg BSA g(-1) MPs was achieved. The hybrid process combining both the ATPS and magnetic capturing leads to a good performance for partitioning of hIgG in the desired phase as well as recovery by the magnetic separator. The MPs were able to bind 145 mg of hIgG g(-1) of particles which is quite high when compared with direct magnetic separation. The theoretical maximum capacity was calculated to be 410 ± 15 mg hIgG adsorbed g(-1) MPs with a binding affinity constant of 4.3 × 10(4) M(-1). In multiple extraction steps, the MPs bound 92% of loaded hIgG with a final purity level of 98.5%. The MPs could easily be regenerated, recycled and re-used for five cycles with only minor loss of capacity. FucoPol coating allowed both electrostatic and hydrophobic interactions with the antibody contributing to enhance the specificity for the targeted products.</pubmed_abstract><journal>Journal of the Royal Society, Interface</journal><pagination>20140743</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4191107</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>An extracellular polymer at the interface of magnetic bioseparations.</pubmed_title><pmcid>PMC4191107</pmcid><pubmed_authors>Morgado PI</pubmed_authors><pubmed_authors>Dhadge VL</pubmed_authors><pubmed_authors>Freitas F</pubmed_authors><pubmed_authors>Reis MA</pubmed_authors><pubmed_authors>Azevedo A</pubmed_authors><pubmed_authors>Roque AC</pubmed_authors><pubmed_authors>Aires-Barros R</pubmed_authors></additional><is_claimable>false</is_claimable><name>An extracellular polymer at the interface of magnetic bioseparations.</name><description>FucoPol, a fucose-containing extracellular polysaccharide (EPS) produced by bacterium Enterobacter A47 using glycerol as the carbon source, was employed as a coating material for magnetic particles (MPs), which were subsequently functionalized with an artificial ligand for the capture of antibodies. The performance of the modified MPs (MP-EPS-22/8) for antibody purification was investigated using direct magnetic separation alone or combined with an aqueous two-phase system (ATPS) composed of polyethylene glycol (PEG) and dextran. In direct magnetic capturing, and using pure protein solutions of human immunoglobulin G (hIgG) and bovine serum albumin (BSA), MP-EPS-22/8 bound 120 mg hIgG g(-1) MPs, whereas with BSA only 10 ± 2 mg BSA g(-1) MPs was achieved. The hybrid process combining both the ATPS and magnetic capturing leads to a good performance for partitioning of hIgG in the desired phase as well as recovery by the magnetic separator. The MPs were able to bind 145 mg of hIgG g(-1) of particles which is quite high when compared with direct magnetic separation. The theoretical maximum capacity was calculated to be 410 ± 15 mg hIgG adsorbed g(-1) MPs with a binding affinity constant of 4.3 × 10(4) M(-1). In multiple extraction steps, the MPs bound 92% of loaded hIgG with a final purity level of 98.5%. The MPs could easily be regenerated, recycled and re-used for five cycles with only minor loss of capacity. FucoPol coating allowed both electrostatic and hydrophobic interactions with the antibody contributing to enhance the specificity for the targeted products.</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Nov</publication><modification>2025-05-29T22:30:27.77Z</modification><creation>2025-05-29T22:30:27.77Z</creation></dates><accession>S-EPMC4191107</accession><cross_references><pubmed>25185582</pubmed><doi>10.1098/rsif.2014.0743</doi></cross_references></HashMap>