RESUMO- Genótipos de amendoim (TATU, BR 1 e L 7) foram estudados quanto à composição aminoacídica, com o objetivo de se indicar o de melhor composição para utilização, como suplemento, na dieta alimentar. Utilizou-se a farinha desengordurada de cada genótipo para as análise dos AAs essenciais, cujas concentrações foram comparadas às dos AAs dos padrões do ovo e da FAO-85. A maioria dos AAs essenciais na farinha do amendoim foi inferior aos do ovo, com exceção da fenilalanina + tirosina; com relação ao padrão da FAO-85, a farinha superou nos AAs isoleucína, leucina fenilalanina, treonina, valina, histidina e metionina + % cistina, sendo inferior em lisina. Os genótipos BR 1 e TATU foram Iimitantes apenas em lisina, com cômputos químicos de 83,18% e 83,64% respectivamente. Portanto, apresentaram melhor composição, podendo ser indicados para a suplementação de dieta alimentar. ABSTRACT- Peanut genotypes (TATU, BR 1 and L 7) were studied as to amino acid composition with the objective to indicate the material of best composition for food diet supplement. Fatless flour of eart cultivar was utilized for essential amino acid analysis and the genotype comparisons were made in relation to eggs and FAO-85 patterns. In majority of the peanut flour essential amino acids that of was lower than egg pattern, except to phenylalanine + tyrosine. As to FAO-85 pattern, peanut flour values was higher to isoleucine, leucine phenylalanine, threonine, valine, histidine and methionine + 1/2 cystine. BR 1 and TATU genotypes were limiting only in Iysine. With chemical composition were 83,18% of 83,64%, respectively. Therefore, these genotypes present the best composition and hence are, indicated for food diet suplement.

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    ABSTRACT: The optimum conditions for direct measurement of tryptophan in soybean meals, wheat, maize, barley, rye, sunflower, fish, and meat meals have been reported. The acid ninhydrin solution has been reacted directly with the protein matrix without any previous isolation or dissolution of the protein. Reproducibility and recovery studies showed that 10-100 μg of tryptophan-containing protein can be determined with a standard error of 2.7% or less. The decreases of tryptophan content of treated soybeans are essentially a function of the parameters applied. The remaining tryptophan contents, expressed in the percentages of the untreated one, were as follows: 81% HCl + H3PO4 (pH ∼1.8), neutralized; 79% HCl + H3PO4 (pH ∼2.0), neutralized; 67% HCl + H3PO4 (pH ∼2.0), without neutralization; 63% microwave 5 min, 100°C; 57% HCl (pH ∼2.0), without neutralization.
    Journal of Agricultural and Food Chemistry 11/1989; 38(3). DOI:10.1021/jf00093a028 · 2.91 Impact Factor
  • Peanut Science 01/1984; 11(1):1-3. DOI:10.3146/i0095-3679-11-1-1
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    ABSTRACT: Quantitative determination of amino acids is made simpler and more rapid by an instrument for automatically recording the ninhydrin color value of the effluent from ion exchange columns. The influent buffer, freed of air, is pumped at a constant rate through a column of sulfonated polystyrene resin. The effluent is met by a capillary stream of ninhydrin reagent delivered by a second pump. The color is developed by passing the mixture of reagent and effluent through a spiral of capillary Teflon tubing immersed in a boiling water bath. The absorbance of the resulting solution is measured continuously at 570 and 440 mμ as it flows through a cylindrical glass cell of 2-mm. bore. The peaks on the recorded curves can be integrated with a precision of 100 ± 3% for loads from 0.1 to 3.0 μmoles of each amino acid. A hydrolyzate of a protein or peptide may be analyzed in less than 24 hours. The more complex mixtures characteristic of blood plasma, urine, and mammalian tissues can be analyzed in 2 days. The instrument is applicable in principle to detection of ninhydrin-positive constituents in the effluent from various types of Chromatograph columns.
    Federation proceedings 01/1959; 17(4):1107-15. DOI:10.1021/ac60139a006


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