Document Type

Article

Publication Date

5-13-2005

Publication Title

Applied and Environmental Microbiology

Department

Thayer School of Engineering

Additional Department

Department of Biological Sciences

Abstract

Protein purification of recombinant proteins constitutes a significant cost of biomanufacturing and various efforts have been directed at developing more efficient purification methods. We describe a protein purification scheme wherein Ralstonia eutropha is used to produce its own “affinity matrix,” thereby eliminating the need for external chromatographic purification steps. This approach is based on the specific interaction of phasin proteins with granules of the intracellular polymer poly

DOI

10.1128/AEM.71.10.5735-5742.2005

Original Citation

Barnard GC, McCool JD, Wood DW, Gerngross TU. Integrated recombinant protein expression and purification platform based on Ralstonia eutropha. Appl Environ Microbiol. 2005 Oct;71(10):5735-42. doi: 10.1128/AEM.71.10.5735-5742.2005. PMID: 16204482; PMCID: PMC1265954.

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