RecombinantEscherichia coliStrain Produces a ZZ Domain Displaying Biopolyester Granules Suitable for Immunoglobulin G Purification
- 1 November 2006
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 72 (11), 7394-7397
- https://doi.org/10.1128/aem.01014-06
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.Keywords
This publication has 10 references indexed in Scilit:
- In Vivo Enzyme Immobilization by Use of Engineered Polyhydroxyalkanoate SynthaseApplied and Environmental Microbiology, 2006
- Genetics and Biochemistry of Polyhydroxyalkanoate Granule Self-assembly: The Key Role of Polyester SynthasesBiotechnology Letters, 2006
- Integrated Recombinant Protein Expression and Purification Platform Based on Ralstonia eutrophaApplied and Environmental Microbiology, 2005
- In vivo monitoring of PHA granule formation using GFP-labeled PHA synthasesFEMS Microbiology Letters, 2005
- Novel and economical purification of recombinant proteins: Intein‐mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix associationProtein Science, 2005
- Polyester synthases: natural catalysts for plasticsBiochemical Journal, 2003
- Biochemical Characterization of the Pseudomonas putida 3-Hydroxyacyl ACP:CoA Transacylase, Which Diverts Intermediates of Fatty Acid de Novo BiosynthesisOnline Journal of Public Health Informatics, 2002
- Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: molecular characterization of the polyhydroxybutyrate synthaseMicrobiology, 2001
- Class I and III Polyhydroxyalkanoate Synthases from Ralstonia eutropha and Allochromatium vinosum: Characterization and Substrate Specificity StudiesArchives of Biochemistry and Biophysics, 2001
- A gene fusion system for generating antibodies against short peptidesGene, 1987