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© Research
Publication : Journal of chromatography. B, Analytical technologies in the biomedical and life sciences

Large scale purification of rapeseed proteins (Brassica napus L.)

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of chromatography. B, Analytical technologies in the biomedical and life sciences - 15 Apr 2005

Bérot S, Compoint JP, Larré C, Malabat C, Guéguen J

Link to Pubmed [PMID] – 15722042

J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2005 Apr;818(1):35-42

Rapeseed (Brassica napus L.) cruciferin (12S globulin), napin (2S albumin) and lipid transfer proteins (LTP) were purified at a multi-g scale. The procedure developed was simple, rather fast and resolutive; it permitted the recovery of these proteins with a good yield, such as 40% for cruciferin and 18% for napin. Nanofiltration eliminated the major phenolic compounds. The remaining protein fraction was fractionated by cation exchange chromatography (CEC) on a streamline SP-XL column in alkaline conditions. The unbound neutral cruciferin was polished by size exclusion chromatography. The alkaline napin isoforms and LTP, adsorbed on the beads, were eluted as a whole fraction and further separated by an other CEC step at acidic pH. Napins were polished by hydrophobic interaction chromatography (HIC). The fractions were characterized by reverse phase HPLC, electrophoresis, N-terminal sequencing and mass spectrometry. All the fractions contained less than 5% of impurities.

http://www.ncbi.nlm.nih.gov/pubmed/15722042