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Histidine Tagged Protein Recovery from Tobacco Extract by Foam Fractionation
Author(s) -
Crofcheck Czarena,
Loiselle Melanie,
Weekley James,
Maiti Indu,
Pattanaik Sitakanta,
Bummer Paul M.,
Jay Michael
Publication year - 2003
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp025738u
Subject(s) - foam fractionation , histidine , fractionation , pulmonary surfactant , chemistry , chelation , chromatography , cobalt , biochemistry , enzyme , organic chemistry
Tobacco plants have the potential to be used for the production of proteins for pharmaceutical applications. This work describes a novel protein recovery strategy where the protein of interest is “tagged” with a histidine sequence, which forms a complex with cobalt ions and surfactant possessing a chelating functionality, such that the protein is recovered in the foamate of a foam fractionation step. His‐gus, a histidine‐tagged enzyme, was chosen as a model protein to study the feasibility of this strategy. The His‐gus is recovered from spiked prefoamed tobacco extract by foam fractionation in the presence of surfactant and cobalt ions with an enrichment of 1.29 and a recovery of 21.5% in terms of an adjusted activity.