1988Journal of the Science of Food and AgricultureRequires access

Japanese barnyard millet (Echinochloa frumentacea): Protein content, quality and SDS–PAGE of protein fractions

P. Vincent Monteiro, L. Sudharshana, Geeta Ramachandra

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Abstract

Abstract Total protein from five varieties of Japanese barnyard millet (Echinochloa frumentacea,) was separated into albumin/globulin, prolamin and glutelin fractions. The protein fractions were examined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Total protein of the varieties ranged from 110·5 to 139·3 mg g−1 of which 11·3–17·2% was albumin/globulins, 6·8–9·3% prolamins, 7·5–11·6% prolamin–like, 5·9–9·1% glutelin‐like and 39·3–54·4% true glutelins. Amino acid analyses of the total protein showed that the varieties had essentially the same ammo acid composition. With the exception of lysine the amino acid levels adequately matched the provisional FAO scoring pattern. The amino acid composition of the protein fractions was also very similar. Electrophoretic analysis showed that the albumin/globulin fraction contained three or four components; the prolamin and glutelin fractions each had five components. The glutelin fraction had higher molecular weight components than the other two fractions.

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Abstract Total protein from five varieties of Japanese barnyard millet (Echinochloa frumentacea,) was separated into albumin/globulin, prolamin and glutelin fractions. The protein fractions were examined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Total protein of the varieties ranged from 110·5 to 139·3 mg g−1 of which 11·3–17·2% was albumin/globulins, 6·8–9·3% prolamins, 7·5–11·6% prolamin–like, 5·9–9·1% glutelin‐like and 39·3–54·4% true glutelins. Amino acid analyses of the total protein showed that the varieties had essentially the same ammo acid composition. With the exception of lysine the amino acid levels adequately matched the provisional FAO scoring pattern. The amino acid composition of the protein fractions was also very similar. Electrophoretic analysis showed that the albumin/globulin fraction contained three or four components; the prolamin and glutelin fractions each had five components. The glutelin fraction had higher molecular weight components than the other two fractions.

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Available abstract

Abstract Total protein from five varieties of Japanese barnyard millet (Echinochloa frumentacea,) was separated into albumin/globulin, prolamin and glutelin fractions. The protein fractions were examined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Total protein of the varieties ranged from 110·5 to 139·3 mg g−1 of which 11·3–17·2% was albumin/globulins, 6·8–9·3% prolamins, 7·5–11·6% prolamin–like, 5·9–9·1% glutelin‐like and 39·3–54·4% true glutelins. Amino acid analyses of the total protein showed that the varieties had essentially the same ammo acid composition. With the exception of lysine the amino acid levels adequately matched the provisional FAO scoring pattern. The amino acid composition of the protein fractions was also very similar. Electrophoretic analysis showed that the albumin/globulin fraction contained three or four components; the prolamin and glutelin fractions each had five components. The glutelin fraction had higher molecular weight components than the other two fractions.

Key concepts: Glutelin, Prolamin, Globulin, Albumin, Polyacrylamide gel electrophoresis, Chemistry, Storage protein, Composition (language)

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