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Quantitation of ten barley-specific amylase/trypsin-inhibitors in the Global EcoSeed panel

ABSTRACT: Amylase/trypsin-inhibitors (ATIs) are known allergens and triggers of non-celiac wheat sensitivity. Until now, ATIs were only quantitated in wheat species. We developed and validated a targeted stable isotope dilution analysis LC-MS/MS method to quantitate ten barley-specific ATIs, including one monomeric and one dimeric amylase-inhibitor, four chloroform/methanol-soluble types, three subtilisin/chymotrypsin-inhibitors and one amylase/subtilisin-inhibitor. After successful validation in terms of precision, recovery and limits of detection and quantitation, the method was applied to 181 barley accessions from the EcoSeed panel, comprising 113 two-row and 68 six-row barleys of different genetic backgrounds. The overall ATI content was 1.1–5.2 mg/g, corresponding to 0.7–3.6% of the total protein content with no clear distinction between two-row and six-row barleys. This study is the first to provide insights on the ATI content and composition of barley, which can be used to make low-ATI foods for special dietary needs.

ORGANISM(S): Hordeum Vulgare

SUBMITTER: Sarah Joestl

PROVIDER: PXD065710 | panorama | Wed Jul 02 00:00:00 BST 2025

REPOSITORIES: PanoramaPublic

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Project description:Wheat (Triticum aestivum ssp. aestivum) contributes to 20% of the human protein supply, delivers essential amino acids and is of fundamental importance for bread and pasta quality. Wheat proteins are also involved in adverse human reactions like celiac disease, wheat allergy and the non-celiac wheat sensitivity (NCWS). Using LC-MS-based LFQ proteomics of aqueous flour extracts we determined 756 proteins across 150 wheat varieties grown in three environments. However, only 303 proteins were stably expressed across all environments in at least one variety underlining the large influence of environmental conditions on the expression of many proteins. Moreover, only 89 proteins were comparably expressed by all 150 varieties, with high coefficients of variation for the other proteins. Heritability (h) ranged from 0-1 with 114 proteins having h² > 0.6. Therefore, the expression of the variable proteins should be amenable to targeted manipulation across the wheat supply chain by varietal choice and breeding. Our study provides a first approach towards a fast and high-throughput methodology for quantifying these proteins which is required to breed wheats with the desired properties. Amylase trypsin inhibitors (ATIs) appear as a potential trigger for NCWS inducing intestinal and extra-intestinal inflammation. Studies on the prevalence and genetic architecture of ATI proteins in wheat are lacking so far. Large differences in the content and composition of 8 ATIs in the different varieties were identified by QconCAT-assisted quantification. The ATI proteins had low coefficients of correlations with quality traits commonly analyzed in wheat breeding. However, heritability was quite low except for ATI 0.28 and ATI CM2. A genome wide association mapping revealed a complex genetic architecture built up on many small but few medium and two major quantitative trait loci (QTL). The latter were on chromosome 3B for ATI 0.19-like and 6B for ATI 0.28 explaining 70.6 and 68.7% of the genetic variance, respectively. Using the wheat reference genome sequence, seven potential candidate genes behind the medium and major QTL were described with only one showing polymorphism based on exome capture analysis. Consequently, wheat breeding could contribute to a reduction of ATI contents in wheat products if incidence of ATI on human health is further confirmed.

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Quantitation of ten barley-specific amylase/trypsin-inhibitors in the Global EcoSeed panel

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