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dc.contributor.authorBrockelbank, Jane A
dc.contributor.authorPeters, Verena
dc.contributor.authorRehm, Bernd HA
dc.date.accessioned2018-03-13T03:14:53Z
dc.date.available2018-03-13T03:14:53Z
dc.date.issued2006
dc.identifier.issn0099-2240
dc.identifier.doi10.1128/AEM.01014-06
dc.identifier.urihttp://hdl.handle.net/10072/371084
dc.description.abstractThe immunoglobulin G (IgG) binding ZZ domain of protein A from Staphylococcus aureus was fused to the N terminus of the polyhydroxyalkanoate (PHA) synthase from Cupriavidus necator. The fusion protein was confirmed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and mediated formation of ZZ domain-displaying PHA granules in recombinant Escherichia coli. The IgG binding capacity of isolated granules was assessed using enzyme-linked immunosorbent assay and could be enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient purification of IgG from human serum.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Society for Microbiology
dc.relation.ispartofpagefrom7394
dc.relation.ispartofpageto7397
dc.relation.ispartofissue11
dc.relation.ispartofjournalApplied and Environmental Microbiology
dc.relation.ispartofvolume72
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchcode310199
dc.titleRecombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2006 American Society for Microbiology. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.hasfulltextFull Text
gro.griffith.authorRehm, Bernd


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