Siteeraan yhden artikkelin 5 vuoden takaa.
https://www.ncbi.nlm.nih.gov/pubmed/22353344
Plant Biotechnol J. 2012 Jun;10(5):533-44. doi: 10.1111/j.1467-7652.2012.00685.x. Epub 2012 Feb 21.
Modulation of kernel storage proteins in grain sorghum (Sorghum bicolor (L.) Moench).
Kumar T1, Dweikat I, Sato S, Ge Z, Nersesian N, Chen H, Elthon T, Bean S, Ioerger BP, Tilley M, Clemente T.
Abstract
Tiivistelmä: Durran prolamiinit, nimeltään kafiriinit, luokitellaan alaryhmiin alfa, beta ja gamma. kafiiriinit kotranslationaalisesti translokoituvat endoplasmiseen verkostoon ja siellä kokoontuvat proteiineiksi, jotka ovat ruoansulatuksessa siten huonosti sulavia. Tätä proteiinin saatavuutta on bioteknisesti koetettu parantaa ja artikkeli käsittelee tätä durrajyvän varastoproteiinien moduloimisasiaa: proteiinistruktuurin muuttamista, proteiinipartikkeleiden periferian disulfidisiltojen vähentämistä sulavuuden parantamiseksi, mutta syntyy samanaikaisproteiinia tunnetuin ominaisuuksin ja se voi stabilisoida kafiriinin beetatuppea taikinan valmistuksen aikana. Tässä tutkijat esittävät lopuksi modifioimansa tuotteen: on tehty transgeenistä durraa, jossa on gamma ja alfakafiriinigeenit vaimennettuja ( jälkimmäinen vaikutti tuoteen sulavuuteen), mutta on siirretty vehnästä eräs hybridisoitu gluteliini, HMW-gluteniini.( Kommenttini .... joten tulos on gluteiinia muodostavaa durrahybridiä. Muistettava tämä mahdollisuus, jos durrasta tulee vaivoja keliakikoille).
"Sorghum
prolamins, termed kafirins, are categorized into subgroups α, β, and γ.
The kafirins are co-translationally translocated to the endoplasmic
reticulum (ER) where they are assembled into discrete protein bodies
that tend to be poorly digestible with low functionality in food and
feed applications. As a means to address the issues surrounding
functionality and digestibility in sorghum, we employed a biotechnology
approach that is designed to alter protein body structure, with the
concomitant synthesis of a co-protein in the endosperm fraction of the
grain.
Wherein perturbation of protein body architecture may provide a route to impact digestibility by reducing disulphide bonds about the periphery of the body,
while synthesis of a co-protein, with known functionality attributes, theoretically could impact structure of the protein body through direct association and/or augment end-use applications of sorghum flour by stabilizing ß-sheet formation of the kafirins in sorghum dough preparations.
This in turn may improve viscoelasticity of sorghum dough.
To this end, we report here on the molecular and phenotypic characterizations of transgenic sorghum events that are down-regulated in γ- and the 29-kDa α-kafirins
and the expression of a wheat Dy10/Dx 5 hybrid high-molecular weight glutenin protein. The results demonstrate that down-regulation of γ-kafirin alone does not alter protein body formation or impacts protein digestibility of cooked flour samples. However, reduction in accumulation of a predicted 29-kDa α-kafirin alters the morphology of protein body and enhances protein digestibility in both raw and cooked samples.
Wherein perturbation of protein body architecture may provide a route to impact digestibility by reducing disulphide bonds about the periphery of the body,
while synthesis of a co-protein, with known functionality attributes, theoretically could impact structure of the protein body through direct association and/or augment end-use applications of sorghum flour by stabilizing ß-sheet formation of the kafirins in sorghum dough preparations.
This in turn may improve viscoelasticity of sorghum dough.
To this end, we report here on the molecular and phenotypic characterizations of transgenic sorghum events that are down-regulated in γ- and the 29-kDa α-kafirins
and the expression of a wheat Dy10/Dx 5 hybrid high-molecular weight glutenin protein. The results demonstrate that down-regulation of γ-kafirin alone does not alter protein body formation or impacts protein digestibility of cooked flour samples. However, reduction in accumulation of a predicted 29-kDa α-kafirin alters the morphology of protein body and enhances protein digestibility in both raw and cooked samples.
©
2012 The Authors. Plant Biotechnology Journal © 2012 Society for
Experimental Biology, Association of Applied Biologists and Blackwell
Publishing Ltd.
- PMID:
- 22353344
- DOI:
- 10.1111/j.1467-7652.2012.00685.x"
