High throughput process development for the purification of rapeseed proteins napin and cruciferin by ion exchange chromatography

Journal Article (2021)
Author(s)

Mónica Moreno Gonzalez (TU Delft - BT/Bioprocess Engineering)

Pattra Chuekitkumchorn (Student TU Delft)

Marcelo Silva (External organisation)

Roos Groenewoud (Student TU Delft)

M Ottens (TU Delft - BT/Bioprocess Engineering)

Research Group
BT/Bioprocess Engineering
Copyright
© 2021 M. Moreno Gonzalez, Pattra Chuekitkumchorn, Marcelo Silva, Roos Groenewoud, M. Ottens
DOI related publication
https://doi.org/10.1016/j.fbp.2020.11.011
More Info
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Publication Year
2021
Language
English
Copyright
© 2021 M. Moreno Gonzalez, Pattra Chuekitkumchorn, Marcelo Silva, Roos Groenewoud, M. Ottens
Research Group
BT/Bioprocess Engineering
Volume number
125
Pages (from-to)
228-241
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Abstract

Proteins derived from plant resources such as oilseed meals, canola and sunflower, are considered a viable alternative to animal proteins for food consumption. This work presents a rational methodology, using high throughput experimentation (HTE), for the separation of cruciferin and napin, the two major proteins of canola meal, by chromatography. Eight different mixed mode and ion exchange resins were evaluated at different conditions with the aim of capturing napin and identifying adsorption/desorption behavior, ease of desorption and selectivity. POROS 50 HS resulted as the most promising resin. The obtained equilibrium adsorption data for napin and cruciferin was used in a mechanistic chromatography model and compared with experimental results showing a very good agreement. The model was used to identify column operating parameters that lead to >98% yield and purity for both proteins. Subsequently a conceptual downstream processing was proposed.