Amino acid, mineral and fatty acid content of pumpkin seeds (Cucurbita spp) and Cyperus esculentus nuts in the Republic of Niger.
ABSTRACT Dried seeds and nuts are widely consumed by indigenous populations of the western Sahel, especially those who inhabit rural areas. In light of the need for quantitative information regarding the content of particular nutrients in these plant foods, we collected dried pumpkin (Cucurbita spp) seeds and nuts of Cyperus esculentus in the Republic of Niger and analyzed them for their content of essential amino acids, minerals and trace elements, and fatty acids. On a dry weight basis, pumpkin seed contained 58.8% protein and 29.8% fat. However, the lysine score of the protein was only 65% relative to the FAO/WHO protein standard. The pumpkin seed contained useful amounts of linoleic (92 microg/g dry weight) and the following elements (on a microg per g dry weight basis): potassium (5,790), magnesium (5,690), manganese (49.3), zinc (113), selenium (1.29), copper (15.4), chromium (2.84), and molybdenum (0.81), but low amounts of calcium and iron. Except for potassium (5,573 microg/g dry weight) and chromium (2.88 microg/g dry weight), the C. esculentis nuts contained much less of these same nutrients compared to pumpkin seeds. In conclusion, pumpkin seeds represent a useful source of many nutrients essential to humans. The data in this report should of practical value to public health officials in rural areas of sub-Saharan Africa.
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ABSTRACT: In the western Sahel and many other regions of sub-Saharan Africa, wild edible plants contribute significantly to human diets, not only during periods when cereal staples are scarce, but also when they are readily available. Although there have been published reports regarding the nutrient contents of these plant foods, little attention has been devoted to their content of antinutrients such as calcium chelators and inhibitors of the pancreas-derived proteases, trypsin and chymotrypsin, which are required for the efficient digestion and absorption of dietary proteins. In this study, aqueous extracts of 61 different leaves, seeds, fruits and flowers of edible plants gathered in the Republic of Niger were analyzed for their content of trypsin inhibitory substances using alpha-N-benzoyl-DL-arginine-p-nitroanilide as the substrate and bovine trypsin as the enzyme source. Twelve of these plant foods contained more antitrypsin activity than soybeans (1.34-8.18 vs. 1.32 microg trypsin inhibited/mg dry weight). Boiling for 3 min did not inactivate the antitrypsin activity in most of the plant extracts. These data confirm that more than half of the wild edible plant foods widely consumed by various populations who inhabit the western Sahel contain significant quantities of heat-stable trypsin inhibitor that could possibly compromise the bioavailability of proteins present in the diets of these populations.Materiae Vegetabiles 02/2000; 55(4):335-46. · 2.36 Impact Factor
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ABSTRACT: Advances in liquid chromatography have brought about the development of new techniques in amino acid analysis which take full advantage of precolumn derivatization procedures. Using phenylisothiocyanate as the reagent, detection limits under 1 pmol can be routinely achieved, allowing the analysis of submicrogram protein samples. Analysis times as short as 10 min for samples after hydrolysis and 1 h for physiologic samples are possible. Accurate, reproducible quantitation of amino acids can be obtained from complex matrices such as plasma, urine, feed, and food samples. This level of performance and flexibility gives the analyst the first realistic alternative to ion-exchange analysis without compromising desirable features of the traditional methodology.Analytical Biochemistry 11/1988; 174(1):1-16. · 2.58 Impact Factor
- Journal of Biological Chemistry 06/1972; 247(9):2828-34. · 4.65 Impact Factor