ArticleMolecules (Basel, Switzerland)2020
Relative Abundance of Alpha-Amylase/Trypsin Inhibitors in Selected Sorghum Cultivars.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Gap Analysis of Metabolic Conversions of Off-Flavors and Antinutrients in Plant-Based Substrates.Comprehensive reviews in food science and food safety · 2026Review
- Potential of Quantitative α-Amylase or Trypsin Inhibition by Refined and Whole Wheat and Einkorn Using High-Performance Thin-Layer Chromatography-NanoGIT versus Conventional Spectrophotometry.Journal of agricultural and food chemistry · 2026Article
- Discovery of Species-Specific Peptide Markers for Superseed Authentication Using Targeted LC-MS/MS Proteomics.Molecules (Basel, Switzerland) · 2025Article
- Comprehensive proteogenomic characterization of early duodenal cancer reveals the carcinogenesis tracks of different subtypes.Nature communications · 2023Article
- Structure, Function and Protein Engineering of Cereal-Type Inhibitors Acting on Amylolytic Enzymes.Frontiers in molecular biosciences · 2022Review
- Effect of Sample Preparation on the Detection and Quantification of Selected Nuts Allergenic Proteins by LC-MS/MS.Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Sorghum is of growing interest and considered as a safe food for wheat related disorders. Besides the gluten, α-amylase/trypsin-inhibitors (ATIs) have been identified as probable candidates for these disorders. Several studies focused on wheat-ATIs although there is still a lack of data referring to the relative abundance of sorghum-ATIs. The objective of this work was therefore to contribute to the characterization of sorghum ATI profiles by targeted proteomics tools. Fifteen sorghum cultivars from different regions were investigated with raw proteins ranging from 7.9 to 17.0 g/100 g. Ammonium bicarbonate buffer in combination with urea was applied for protein extraction, with concentration from 0.588 ± 0.047 to 4.140 ± 0.066 mg/mL. Corresponding electrophoresis data showed different protein profiles. UniProtKB data base research reveals two sorghum ATIs, P81367 and P81368; both reviewed and a targeted LC-MS/MS method was developed to analyze these. Quantifier peptides ELAAVPSR (P81367) and TYMVR (P81368) were identified and retained as biomarkers for relative quantification. Different reducing and alkylating agents were assessed and combination of tris (2 carboxyethyl) phosphine/iodoacetamide gave the best response. Linearity was demonstrated for the quantifier peptides with standard recovery between 92.2 and 107.6%. Nine sorghum cultivars presented up to 60 times lower ATI contents as compared to wheat samples. This data suggests that sorghum can effectively be considered as a good alternative to wheat.
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