RESUMO
Samples of Lupinus luteus, var. Aurea/Weico and Lupinus albus var. Multolupa flours were analyzed. The flour proteins were extracted and fractionated by gel filtration, and the per cent pattern for both globulins and albumins was then determined. The dehulled seeds, previously analyzed for composition, were ground, defatted and consecutively extracted with distilled water (pH 5.0) and phosphate buffer (0.05 M, pH 8.5). The extracted protein content was measured by the Lowry simplified method. Globulins (pH 8.5 fraction) from both species were filtered through Sephadex G-100; besides, Lupinus albus globulins were filtered through Sephadex G-150, and absorbance of the collected fractions was measured at 280 nm. The dehulled seed (DS) of L. luteus and L. albus revealed a good protein content (58.2 and 41.0%, respectively). The protein extracted from L. luteus was constituted by 17% albumins and 58.4% globulins. In contrast, L. albus presented a higher albumin content (55.6%) than globulins (31.5%). The elution pattern for the Sephadex G-200 gel filtration showed for both lupine species analyzed a preponderant peak I corresponding in L. luteus to 55.0% and in L. albus to 84.1% of the total globulins content. From these results, it may be concluded that the dehulled seed protein content is 42.0% higher for the L. luteus sample than for the L. albus. The applied methodology indicated a predominant content of globulins above albumins in L. luteus, while in the case of L. albus, the albumin content was the highest.
Assuntos
Fabaceae , Farinha/análise , Proteínas de Vegetais Comestíveis/análise , Plantas Medicinais , Sementes , Albuminas/análise , Cromatografia em Gel , Manipulação de Alimentos , Globulinas/análiseRESUMO
The albumins and globulins extracted from Lupinus luteus var. Aurea/Weico and Lupinus albus var. Multolupa defatted flour samples were analyzed by polyacrilamide gel electrophoresis. The purpose was to determine the percentage distribution of pattern in the electrophoretograms and the relative mobility values of protein. The L. luteus albumins densitogram showed six fractions, two of them, No. 2 and No. 4, represented 58.1% of the total. On the other hand, the globulins densitogram revealed five fractions, numbers 1, 2 and 3 representing 90.7%. The densitogram of peak I from Sephadex G-100 globulins filtration indicated two fractions similar to those number 1 and 2 of the total globulins, showing low relative mobility values (from 0.26 to 0.39). The L. albus albumins resolved in four fractions, with No. 2 being the most prevalent (54.3%). In regard to the L. albus globulins, these showed five fractions identical in distribution with those of peak I, fraction 2 appearing as the most important (48.2%). It was found that Sephadex G-100 did not perform a good separation. As to the relative mobility values of globulins, fractions 2 and 3 were the most prominent (relative mobility of 0.35 and 0.48, respectively). It may be concluded that L. luteus albumins presented more components but with lower relative mobility values than those of L. albus. As for the globulins from both lupine flour samples, the gel separated fractions were classified in two groups of components, those of high and of low relative mobility.