SEPARATION OF RAPESEED GLOBULIN BY MICELLAR ELECTROKINETIC CHROMATOGRAPHY (MEKC) – A SHORT REPORT
 
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Pol. J. Food Nutr. Sci. 2007;57(3):353–356
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ABSTRACT
Cruciferin was separated from the rapeseed crude proteins using salting out with ammonium sulphate and Sephadex G-200 gel filtration. Then, so obtained protein fraction was separated using a micellar electrokinetic chromatography (MEKC) with SDS as a the surfactant. Nine peaks with migration times between 14.33 and 20.48 min were recorded on the chromatogram. The main cruciferin subfractions were characterised with molecular mass of 22 000 and 33 000 determined using MEKC technique. UV spectra showed that cruciferin protein appears as a complex with phenolic acids.
ISSN:1230-0322