Abstract
Rice consumption is rising in western countries with the adoption of new nutritional styles, which require the avoidance of gluten. Nevertheless, there are reports of rice allergic reactions. Rice grains contain a low amount of proteins most of which are storage proteins represented by glutelins, prolamins, albumins, and globulins. Some of these proteins are seed allergenic proteins as α‐amylase/trypsin inhibitor, globulins, β‐glyoxylase, and several glutelins. Italy is the major rice producer in Europe, and for this, seed reserve proteins of four Italian rice cultivars were characterized by 2D‐GE analysis. Some differentially abundant proteins were identified and classified as allergenic proteins, prompting a further characterization of the genes encoding some of these proteins. In particular, a deletion in the promoter region of the 19 KDa globulin gene has been identified, which may be responsible for the different abundance of the protein in the Karnak cultivar. This polymorphism can be applied for cultivar identification in commercial samples. Seed proteome was characterized by a variable combination of several proteins, which may determine a different allergenic potential. Proteomic and genomic allowed to identify the protein profile of four commercial cultivars and to develop a molecular marker useful for the analysis of commercial products.
Highlights
Oryza sativa L. is one of the main food commodity, and nearly half of the world population depend on this culture for daily nutrition
Rice grains contain a low amount of proteins (7%–10%) most of which are storage proteins represented by glutelins, prolamins, and a lower amount of albumins and globulins
At variance with other cereals, rice seed proteome is made mainly of glutelins (60% to 80%) that are encoded by 34 genes, while only 5% is represented by prolamins that are encoded by 34 genes (Kawakatsu, Hirose, Yasuda, and Takaiwa 2010)
Summary
Oryza sativa L. is one of the main food commodity, and nearly half of the world population depend on this culture for daily nutrition. The rice seed proteins responsible for allergy are α-amylase/trypsin inhibitor (14–16 kDa) classified as albumins, α-globulins, β-glyoxylase, and several glutelins (Adachi et al, 1993; Birla et al, 2017; Usui et al, 2001). At variance with other cereals, rice seed proteome is made mainly of glutelins (60% to 80%) that are encoded by 34 genes, while only 5% is represented by prolamins that are encoded by 34 genes (Kawakatsu, Hirose, Yasuda, and Takaiwa 2010). The analysis at genomic level revealed the presence of different allelic forms; in particular, in Karnak the gene encoding the 19 kDa globulin carries a deletion in the promoter region This may explain the more abundant protein expression (twofold) observed in Karnak in comparison with Carnaroli
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