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Applied and Environmental Microbiology, November 2006, p. 7394-7397, Vol. 72, No. 11
0099-2240/06/$08.00+0     doi:10.1128/AEM.01014-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Recombinant Escherichia coli Strain Produces a ZZ Domain Displaying Biopolyester Granules Suitable for Immunoglobulin G Purification{triangledown}

Jane A. Brockelbank, Verena Peters, and Bernd H. A. Rehm*

Institute of Molecular Biosciences, Massey University, Private Bag 11222, Palmerston North, New Zealand

Received 1 May 2006/ Accepted 14 August 2006

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.

* Corresponding author. Mailing address: Institute of Molecular Biosciences, Massey University, Private Bag 11222, Palmerston North, New Zealand. Phone: 64 6 350 5515, ext. 7890. Fax: 64 6 350 5688. E-mail: B.Rehm{at}massey.ac.nz.

{triangledown} Published ahead of print on 25 August 2006.

Applied and Environmental Microbiology, November 2006, p. 7394-7397, Vol. 72, No. 11
0099-2240/06/$08.00+0     doi:10.1128/AEM.01014-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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