ArticleFoods (Basel, Switzerland)2023
Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Animal- and Plant-Derived Protein Nanocarriers for the Delivery of Natural Compounds in Breast Cancer Chemoprevention.Molecules (Basel, Switzerland) · 2026Review
- Enhanced bacterial cellulose production by Komagataeibacter xylinus using agro-derived flour nitrogen sources.Applied microbiology and biotechnology · 2026Article
- Therapeutic Efficacy of Soy-Derived Bioactives: A Systematic Review of Nutritional Potency, Bioactive Therapeutics, and Clinical Biomarker Modulation.Foods (Basel, Switzerland) · 2025Review
- Nutritional Characteristics, Health-Related Properties, and Food Application of Teff (International journal of molecular sciences · 2025Review
- From 'Farm to Fork': Exploring the Potential of Nutrient-Rich and Stress-Resilient Emergent Crops for Sustainable and Healthy Food in the Mediterranean Region in the Face of Climate Change Challenges.Plants (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
To develop teff-based food products with acceptable quality, the composition, structure, and properties of teff protein fractions should be better understood. In this study, teff proteins were extracted, and their protein composition, structure, and properties were calculated, analyzed, and compared with those of wheat gliadin and glutenin. Results showed that teff flour contained 9.07% protein, with prolamin as its main protein fraction. The isoelectric points of albumin, globulin, prolamin, and glutelin were at pH 3.6, 3.0, 4.4, and 3.4, respectively. Teff prolamin and glutelin showed a significant difference in amino acids and free energy of hydration compared to wheat gliadins and glutenins. The protein chain length of teff prolamins was smaller than that of wheat gliadins, and teff glutelins lacked high molecular weight glutelin subunits. Teff prolamin had the highest α-helices content (27.08%), whereas no random coils were determined, which is different from wheat gliadin. Teff glutelin had a lower content of β-turn than wheat glutenin, and no α-helices were determined in it. Teff prolamin and glutelin had lower disulfide bond content and surface hydrophobicity. Teff prolamin had significantly higher thermal stability than wheat gliadin, whereas the thermal stability of teff glutelin was significantly lower than that of wheat glutenin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.