Gluten proteome comparison among durum wheat genotypes with different release date |
| |
| Affiliation: | 1. Department of Plant Sciences, Norwegian University of Life Sciences, P.O. Box 5003, NO-1432 Ås, Norway;2. Graminor AS, Bjørke Research Station, Hommelstadvegen 60, NO-2322 Ridabu, Norway;3. Nofima AS, P.O.Box 210, NO-1431 Ås, Norway;4. Bioforsk, the Norwegian Institute for Agricultural and Environmental Research, Arable Crops Division, Nylinna 226, N-2849 Kapp, Norway;5. Dept. of Agronomy & Plant Genetics, University of Minnesota, 411 Borlaug Hall, 1991 Buford Circle, St. Paul, MN 55180, USA;1. Nofima, Osloveien 1, NO-1430 Ås, Norway;2. Department of Plant Sciences, Norwegian University of Life Sciences, P.O. Box 5003, NO-1432 Ås, Norway;3. Deutsche Forschungsanstalt für Lebensmittelchemie, Leibniz Institut, Lise-Meitner-Straße 34, 85354 Freising, Germany |
| |
| Abstract: | In order to deepen insight into durum wheat prolamin composition in relation to both end use quality and gluten related disorders, a phenotyping of four genotypes of different release date and technological performance was carried out. A proteomic approach integrated with the evaluation of protein aggregation level, amino acid composition and reactivity to G12 monoclonal antibody, was adopted. The degree of polymerization, estimated as unextractable polymeric proteins (UPP), was positively influenced by Cys-rich proteins (Glu-B3 LMW-GS), with Saragolla showing up to 40% higher values than other genotypes. The proteomic assessment allowed to identify proteins involved in gluten related disorders. In particular, ω5-gliadin involved in wheat allergy (WA), resulted markedly over-expressed in the old landrace Dauno III, up to four-fold than in modern Saragolla. A marked influence of genotype on the expression level of gliadins containing toxic epitopes (TECP) was observed with the more recent genotypes showing lower values (−53%). Also, reactivity to G12 moAb resulted higher in the two old genotypes consistently to their higher celiac disease (CD) toxicity evaluated by the proteomic approach. In conclusion a better gluten composition for processing seems to be associated to a lower expression level of CD toxic peptides and Tri a 19. |
| |
| Keywords: | Durum wheat Gluten Proteomics CD toxicity 2DE" },{" #name" :" keyword" ," $" :{" id" :" kwrd0035" }," $$" :[{" #name" :" text" ," _" :" two-dimensional polyacrylamide gel electrophoresis ACN" },{" #name" :" keyword" ," $" :{" id" :" kwrd0045" }," $$" :[{" #name" :" text" ," _" :" acetonitrile AG" },{" #name" :" keyword" ," $" :{" id" :" kwrd0055" }," $$" :[{" #name" :" text" ," _" :" albumin and globulin proteins ω-α-γ-" },{" #name" :" keyword" ," $" :{" id" :" kwrd0065" }," $$" :[{" #name" :" text" ," _" :" ratio between ω-gliadins and α-γ-gliadins CD" },{" #name" :" keyword" ," $" :{" id" :" kwrd0075" }," $$" :[{" #name" :" text" ," _" :" celiac disease EAA" },{" #name" :" keyword" ," $" :{" id" :" kwrd0085" }," $$" :[{" #name" :" text" ," _" :" essential amino acids ELISA" },{" #name" :" keyword" ," $" :{" id" :" kwrd0095" }," $$" :[{" #name" :" text" ," _" :" enzyme-linked immunosorbent assay H/L" },{" #name" :" keyword" ," $" :{" id" :" kwrd0105" }," $$" :[{" #name" :" text" ," _" :" ratio between HMW-GS and LMW-GS H Bx/By" },{" #name" :" keyword" ," $" :{" id" :" kwrd0115" }," $$" :[{" #name" :" text" ," _" :" ratio between HMW-GS Bx and By IECP" },{" #name" :" keyword" ," $" :{" id" :" kwrd0125" }," $$" :[{" #name" :" text" ," _" :" immunogenic epitope-containing proteins L B/C" },{" #name" :" keyword" ," $" :{" id" :" kwrd0135" }," $$" :[{" #name" :" text" ," _" :" ratio between B-type and C-type LMW-GS TECP" },{" #name" :" keyword" ," $" :{" id" :" kwrd0145" }," $$" :[{" #name" :" text" ," _" :" toxic epitope-containing proteins WA" },{" #name" :" keyword" ," $" :{" id" :" kwrd0155" }," $$" :[{" #name" :" text" ," _" :" wheat allergy |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
