Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification.
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ABSTRACT:
SUBMITTER: Brockelbank JA
PROVIDER: S-EPMC1636211 | biostudies-literature | 2006 Nov
REPOSITORIES: biostudies-literature
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Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification.
Brockelbank Jane A JA Peters Verena V Rehm Bernd H A BH
Applied and environmental microbiology 20060825 11
The 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 ...[more]
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