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Proteins of Italian millet: amino acid composition, solubility fractionation and electrophoresis of protein fractions.

Monteiro, P. V. and Virupaksha, T. K. and Rajagopal Rao, D. (1982) Proteins of Italian millet: amino acid composition, solubility fractionation and electrophoresis of protein fractions. Journal of the Science of Food and Agriculture, 33 (11). 1072-1079, 21 ref.. (In Press)

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Abstract

Determination of the protein contents of 14 var. of Italian millet revealed considerable varietal differences. The total protein of the 14 var. was fractionated into albumin-globulin, prolamin and glutelin fractions. The prolamin fraction constitutes the major storage protein of the grain. There is a positive correlation between protein content and the prolamin levels of the seeds and the increase in protein contents is largely due to an increase in the prolamin content. The amino acid composition of each of 14 var. of the millet and the individual protein fractions from 3 var. were determined. The limiting amino acids are lysine followed by tryptophan and the S-containing amino acids, methionine and cystine. The lysine content of the grain decreases with increase in protein content. The total protein has a rather high content of leucine. SDS-polyacrylamide gel electrophoresis of the protein fractions indicated similarities in the prolamin fraction and differences in the albumin-globulin and glutelin fractions of the different var.

Item Type: Article
Uncontrolled Keywords: BREED-; millets, var. & proteins in; PROTEINS-CEREAL; AMINO-ACIDS; millets, var. & amino acids in; MILLETS-; var. & proteins in millets
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 21 Cereals > 05 Ragi (Finger Millet)
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 25 May 2016 07:09
Last Modified: 30 Dec 2016 08:32
URI: http://ir.cftri.res.in/id/eprint/6760

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