Histidine tagged protein recovery from tobacco extract by foam fractionation

Czarena Crofcheck; Melanie Loiselle; James Weekley; Indu Maiti; Sitakanta Pattanaik; Paul M Bummer; Michael Jay

doi:10.1021/bp025738u

Histidine tagged protein recovery from tobacco extract by foam fractionation

Czarena Crofcheck, Melanie Loiselle, James Weekley, Indu Maiti, Sitakanta Pattanaik, Paul M Bummer, Michael Jay

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	680-2
Number of pages	3
Journal	Biotechnology Progress
Volume	19
Issue number	2
DOIs	https://doi.org/10.1021/bp025738u
State	Published - 2003

Keywords

Chemical Fractionation/methods
Enzyme Activation
Feasibility Studies
Glucuronidase/biosynthesis
Histidine/chemistry
Plant Extracts/chemistry
Plant Leaves/chemistry
Protein Binding
Recombinant Fusion Proteins/biosynthesis
Surface-Active Agents/chemistry
Tobacco/chemistry

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10.1021/bp025738u

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title = "Histidine tagged protein recovery from tobacco extract by foam fractionation",

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.",

keywords = "Chemical Fractionation/methods, Enzyme Activation, Feasibility Studies, Glucuronidase/biosynthesis, Histidine/chemistry, Plant Extracts/chemistry, Plant Leaves/chemistry, Protein Binding, Recombinant Fusion Proteins/biosynthesis, Surface-Active Agents/chemistry, Tobacco/chemistry",

author = "Czarena Crofcheck and Melanie Loiselle and James Weekley and Indu Maiti and Sitakanta Pattanaik and Bummer, {Paul M} and Michael Jay",

year = "2003",

doi = "10.1021/bp025738u",

language = "English",

volume = "19",

pages = "680--2",

number = "2",

}

TY - JOUR

T1 - Histidine tagged protein recovery from tobacco extract by foam fractionation

AU - Crofcheck, Czarena

AU - Loiselle, Melanie

AU - Weekley, James

AU - Maiti, Indu

AU - Pattanaik, Sitakanta

AU - Bummer, Paul M

AU - Jay, Michael

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

KW - Chemical Fractionation/methods

KW - Enzyme Activation

KW - Feasibility Studies

KW - Glucuronidase/biosynthesis

KW - Histidine/chemistry

KW - Plant Extracts/chemistry

KW - Plant Leaves/chemistry

KW - Protein Binding

KW - Recombinant Fusion Proteins/biosynthesis

KW - Surface-Active Agents/chemistry

KW - Tobacco/chemistry

U2 - 10.1021/bp025738u

DO - 10.1021/bp025738u

M3 - Article

C2 - 12675618

SN - 8756-7938

VL - 19

SP - 680

EP - 682

JO - Biotechnology Progress

JF - Biotechnology Progress

IS - 2

ER -

Histidine tagged protein recovery from tobacco extract by foam fractionation

Abstract

Keywords

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