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Updated: Sep 26, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Histidine tagged protein recovery from tobacco extract by foam fractionation
Czarena Crofcheck1, Melanie Loiselle, James Weekley
1Department of Biosystems and Agricultural Engineering, College of Pharmacy, and Kentucky Tobacco Research and Development Center, University of Kentucky, Lexington, Kentucky 40546, USA. ccrofche@bae.uky.edu
Abstract:
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.

