Separation of rapeseed globulin by micellar electrokinetic chromatography [MEKC] - a short report

• Autorzy: Rybarczyk A. , Chavan U.D. , Amarowicz R.

Warianty tytułu

PL

Rozdzial globuliny rzepaku metoda micelarnej elektrokinetycznej chromatografii [MEKC] - krotki komunikat

• Języki publikacji: EN

Abstrakty

EN

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.

PL

Krucyferyna została oczyszczona z ekstraktu białek rzepaku stosując wysalanie siarczanem amonu i filtrację żelową na żelu Sephadex G-200. Tak otrzymane białko rozdzielono metodą micelarnej elektrokinetycznej chromatografii (MEKC) z SDS jako związkiem powierzchniowo czynnym. Na chromatogramie zarejestrowano dziewięć pików o czasach retencji między 14,33 i 20,48 min. Główne subfrakcje krucyferyny charakteryzowały się masą cząsteczkową 22 000 i 33 000. Widmo UV wskazuje, że krucyferyna występuje w nasionach rzepaku jako kompleks z fenolokwasami.

Słowa kluczowe

EN

rapeseed; globulin; separation; capillary electrophoresis; micellar electrokinetic chromatography; MEKC technique zob.micellar electrokinetic chromatography

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2007
• Tom: 57
• Numer: 3
• Opis fizyczny: p.353-356,fig.,ref.

Twórcy

autor

Rybarczyk A.

• Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland

autor

Chavan U.D.

autor

Amarowicz R.

Bibliografia

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