Počet záznamů: 1  

Diversity in Seed Storage Protein Profile of Oilseed Crop Plukenetia volubilis from Peruvian Amazon

  1. 1.
    0504502 - FGÚ 2020 RIV PK eng J - Článek v odborném periodiku
    Čepková Hlásná, P. - Jágr, Michal - Viehmannová, I. - Dvořáček, V. - Huansi, D. C. - Mikšík, Ivan
    Diversity in Seed Storage Protein Profile of Oilseed Crop Plukenetia volubilis from Peruvian Amazon.
    International Journal of Agriculture and Biology. Roč. 21, č. 3 (2019), s. 679-688. ISSN 1560-8530
    Grant CEP: GA ČR(CZ) GA15-01948S
    Institucionální podpora: RVO:67985823
    Klíčová slova: genetic variability * oilseeds * proteomics * storage proteins
    Obor OECD: Analytical chemistry
    Impakt faktor: 0.822, rok: 2019
    Způsob publikování: Open access
    http://www.fspublishers.org/published_papers/23739_26%20doi%2015.0945%20IJAB-18-1080%20(10)%20679-688.pdf

    Sacha inchi (Plukenetia volubilis L.) is a plant native to the Peruvian Amazon and produces seeds rich in some nutraceutical compounds with a high protein content. The present work aimed to characterize P. volubilis seed proteins and compare their proteomic profile between different P. volubilis populations. Crude protein content in the seeds was detected at a mean level of 22.56% with the major proportion of albumins and globulins (16.37%), followed by glutelins (5.87%) and a very low content of prolamins (0.33%). Sodium dodecyl sulfate-polyacrylamide (SDS-PAGE) gel electrophoresis of both total seed flour and Osborne's protein fractions of different populations showed that proteins were concentrated in the 8-75 kDa range. Differences in abundance of proteins between Sacha inchi populations were detected by SD S-PAGE and two-dimensional (2-DE) gel electrophoresis. Gel protein bands and spots of interest were excised, digested with trypsin and analyzed by nano-liquid chromatography/tandem mass spectrometry (nLC-MS/MS). This is the first direct identification of these proteins in actual Sacha inchi seeds. Three proteins (Oleosin 2, Oleosin 3 and elongation factor 1-alpha) directly from P. volubilis and peptides with a sequence identical to 56 proteins from the Euphothiaceae family were detected. This characterization of seed storage protein, their variability within populations and identification of important proteins provide a basis for further investigations for the food industry and bioengineering.
    Trvalý link: http://hdl.handle.net/11104/0296121

     
     
Počet záznamů: 1  

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