Applied and Environmental Microbiology
Thayer School of Engineering
Department of Biological Sciences
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
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.
Dartmouth Digital Commons Citation
Barnard, Gavin C.; McCool, Jesse D.; Wood, David W.; and Gerngross, Tillman U., "Integrated Recombinant Protein Expression and Purification Platform Based on Ralstonia eutropha" (2005). Dartmouth Scholarship. 493.