Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/34616
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dc.contributor.authorAlmeida, Catarina A. S.pt_PT
dc.contributor.authorSilva, Luís C. V.pt_PT
dc.contributor.authorSilva, Maria Carolinapt_PT
dc.contributor.authorNeves, Márcia C.pt_PT
dc.contributor.authorFreire, Mara G.pt_PT
dc.date.accessioned2022-09-15T10:53:05Z-
dc.date.available2022-09-15T10:53:05Z-
dc.date.issued2021-
dc.identifier.urihttp://hdl.handle.net/10773/34616-
dc.description.abstractAvian immunoglobulin Y (IgY), found in egg yolk, has potential to be used as a biopharmaceutical. Contrarily to its analogous mammalian immunoglobulin G (IgG), IgY presents high immunogenicity and binding avidity, and the ability to be recovered by a non-invasive method [1-3]. The amount of IgY obtained from an egg is equal to that from 200-300 mL of mammalians blood, being possible for a chicken produce 17-35 g of total IgY [1,4]. By being a polyclonal antibody, IgY antibodies recognize several epitopes on an antigen and have various applications, such as in the treatment of several diseases [1,2]. However, by being proteins present in a complex media, the use of IgY as a biopharmaceutical is restricted by its recovery at high yields and high purity, along with their preservation [5]. This work aimed to improve the stability of IgY during storage, so that it can be used as a biopharmaceutical. IgY antibodies were isolated from the yolk of commercial chicken eggs and purified by two precipitation steps. Their stability was assessed by Circular Dichroism Spectroscopy (CD) under 1-3 weeks of storage at -20 ºC. Trehalose and xylitol at several concentrations were investigated as stabilizers agents. The IgY purity degree, concentration and the percentage of aggregates formed during storage were determined by Size Exclusion- High Performance Liquid Chromatography (SEC-HPLC), whereas the protein profile was revealed by dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Both stabilizers allowed promising results and are potential stabilizing agents for IgY. A decrease in the percentage of aggregates was verified in IgY formulations with trehalose and xylitol in all storage conditions. It was confirmed the presence of β-sheets in the IgY secondary structure, and no substantial evidence of its secondary structure degradation occurred over storage with the stabilizing agents.pt_PT
dc.language.isoengpt_PT
dc.publisherSociedade Portuguesa de Microbiologia; Sociedade Portuguesa de Biotecnologia; Universidade Nova de Lisboapt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50011%2F2020/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F50011%2F2020/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/899921/EUpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/CEEC IND 2017/CEECIND%2F00383%2F2017%2FCP1459%2FCT0031/PTpt_PT
dc.rightsopenAccesspt_PT
dc.titleBiocompatible excipients to improve the stability of immunoglobulin Y (IgY) antibodiespt_PT
dc.typeconferenceObjectpt_PT
dc.description.versionpublishedpt_PT
dc.peerreviewedyespt_PT
ua.event.date23-26 November, 2021pt_PT
degois.publication.firstPage87pt_PT
degois.publication.lastPage88pt_PT
degois.publication.locationLisboapt_PT
degois.publication.titleMicrobiotec 21- Congress of Microbiology and Biotechnology 2021: abstracts bookpt_PT
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DQ - Comunicações

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