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• W1971101436 abstract "The protein fractions in three different teff types were studied in comparison to sorghum to explain teff’s superior bread making quality. The proportion of aqueous alcohol-soluble teff protein was approx 40% and it was rich in glutamine and leucine. Hence, contrary to previous reports, prolamin is the major teff grain storage protein. With SDS-PAGE under non-reducing and reducing conditions, teff prolamins showed broad bands at approx. 20.3 and 22.8 kDa. Other bands were at approx. 36.1, 50.2, 66.2 and 90.0 kDa, respectively under non-reducing conditions, but were absent under reducing conditions, indicating that these polypeptides are disulphide bonded. The presence of broad monomeric prolamin bands in teff under non-reducing conditions indicates that teff prolamin is less polymerized than sorghum prolamin. Estimated free energy of hydration of teff prolamins was −161.3 kcal/mol compared to −139.8 kcal/mol for sorghum prolamin. By 2-D electrophoresis, teff protein contained more polypeptides than maize or sorghum. Teff contained a higher proportion of basic polypeptides than maize. With differential scanning calorimetry, teff prolamin exhibited a single endothermic peak at 69.85 °C, while no peak was detected for sorghum prolamin. The lower polymerization, hydrophobicity and denaturation temperature of teff prolamins probably make them somewhat functional in bread making." @default.
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• W1971101436 date "2011-11-01" @default.
• W1971101436 modified "2023-10-17" @default.
• W1971101436 title "Fractionation and characterization of teff proteins" @default.
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• W1971101436 doi "https://doi.org/10.1016/j.jcs.2011.08.002" @default.
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