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Biochemical characterization of white onion landraces (Allium cepa L.) through HPLC analysis of endosperm seed proteins
Authors:Giuseppe Mennella  Vincenzo Onofaro Sanaja’  Antonietta D’Alessandro  Angelo Desiderio
Affiliation:(1) Istituto Sperimentale per l"rsquo"Orticoltura (MiPAF), Via Cavalleggeri 25, 84098 Pontecagnano (SA), Italy
Abstract:Water-, salt-, alcohol- and alkali-soluble seed storage proteins, extracted from 21 ldquocipolla bianca di Pompeirdquo landraces (Allium cepa L.), were analyzed by anionic exchange-high performance liquid chromatography (AE-HPLC). Chromatographic elution profiles (time range 0–40 min) at 280 nm of water-soluble seed proteins evidenced the presence of 21 peaks, which allowed all the landraces studied to be distinguished from each other. The differences detected were both qualitative (presence/absence of one or more peaks) and quantitative; the water-soluble proteins were useful in differentiating landraces and cultivars while the other seed protein fractions only showed a weak polymorphism. The cluster analysis, based on HPLC data, showed that the landraces clustered with a genetic similarity degree ranging between 69% and 94%. The possibility of discriminating among closely related onion landraces during the course of breeding programmes could allow the identification of biochemical markers linked to useful agronomical traits. As observed by chromatographic analysis, the globulin composition of onion water-soluble seed protein appears to be independent of environmental growth conditions. The biochemical characterization of the available typical onion germplasm may contribute to obtain a community recognition and denomination, such as Denomination of Protected Origin (D.O.P.), Indication of Protected Origin (I.G.P.) or Specificity Attestation (A.S.). The biochemical method here developed resulted of high resolution, cost-effective and time-saving for characterization and genetic purity assessment of the landraces studied.
Keywords:AE-HPLC  genetic similarity  salt-soluble proteins  water-soluble proteins
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