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Updated: Jul 20, 2026
Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli
Published on: June 30, 2023
Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin
Jane A Brockelbank1, Verena Peters, Bernd H A Rehm
1Institute of Molecular Biosciences, Massey University, Private Bag 11222, Palmerston North, New Zealand.
Abstract:
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 enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient purification of IgG from human serum.
