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Qualitas Plantarum et Materiae Vegetabiles

, Volume 19, Issue 4, pp 313–332 | Cite as

Some chemical and biological properties of a protein concentrate from nigerseed (Guizotia abyssinica Cass.)

  • Anders Eklund
  • Gunnar Ågren
Article

Abstract

A protein concentrate has been prepared from nigerseed (Guizotia abyssinica Cass.) by a method involving extraction of the protein with NaCl-solution.

The protein concentrate contains about 65% of protein (N×5.5) calculated from the dry weight, and the amino acid pattern is fairly well balanced. The chemical score is 82 calculated from the A/E values.

The nutritional value of the product has been tested on young rats. These tests revealed the presence of antinutritional factors in the protein concentrate. The PER was only 1.5.

It was also found that the rate of digestion by pancreatin was much slower for the protein concentrate than for casein, possibly due to enzyme resistent linkages.

The protein concentrate seems to be devoid of hemagglutinin activity. Antibodies against the nug extracts could not be found.

Keywords

Enzyme Protein Concentrate Plant Physiology Biological Property Pancreatin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Résumé

Une solution concentrée de protéine a été préparée de grains de ‚nug’ (Guizotia abyssinica Cass.) par une méthode contenant l'extraction de la protéine avec la solution NaCl.

La solution concentrée contient environ 65% de protéine (N X 5,5) calculée du poids sec, et le modèle des aminoacides est assez bien balancé. Le ‚chemical score’ est 82 calculé des valeurs A/E. La valeur nutritive du produit a été éprouvé à de jeunes rats. Ces épreuves ont révélé la présence d'éléments antinutritives dans la solution concentrée de protéine. La PER (‚protein efficiency ratio’) était seulement 1,5.

On a aussi trouvé que la rapidité de digestion enzymatique (avec la pancréatine) pour la solution concentrée de protéine était beaucoup plus lente que pour le casein. Ceci est peut-être du à des liaisons qui résistent aux enzymes.

Il semble que la solution concentrée de protéine manque d'activité hemagglutinine. On n'a pas pu trouver des anticorps dirigés contre les extraits de ‚nug’.

Zusammenfassung

Ein Proteinkonzentrat wurde aus ‚Nug’-Samen (Guizotia abyssinica Cass.) durch eine Methode gewonnen, die eine Extraktion des Proteins mit NaCl-Lösung einschließt.

Das Proteinkonzentrat enthalt etwa 65% Protein (N x 5,5), berechnet auf das Trockengewicht. Das Aminosäuregleichgewicht ist relativ gut balanziert. Die ‚chemical score’ nach den A/E Werten berechnet, beträgt 82.

Der Nährwert des Produktes ist an jungen Ratten getestet worden. Diese Tests zeigten das Vorhandensein von Antinähr-Faktoren im Proteinkonzentrat. Die PER (‚protein efficiency ratio’) betrug nur 1,5.

Es wurde außerdem festgestellt, daß die Geschwindigkeit der enzymatischen Verdauung (mit Pankreatin) für das Proteinkonzentrat viel langsamer abläuft als für Casein. Dieses ist vielleicht bedingt durch Enzymresistente Bindungen.

Das Proteinkonzentrat scheint von Hämagglutininaktivität frei zu sein. Es wurden keine Antikörper gegen ‚Nug’-Extrakte gefunden.

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References

  1. 1.
    Altschul, A.M. (1966) World Protein Resources, Advan. Chem. Ser.57.Google Scholar
  2. 2.
    United States Department of Agriculture (1965) Proceedings of a Conference on Cottonseed Protein Concentrates, New Orleans Louisiana 1964, ARS 72–38.Google Scholar
  3. 3.
    United States Department of Agriculture (1967) Proceedings of International Conference of Soybean Protein Foods, Peoria Illinois 1966, ARS 71–35.Google Scholar
  4. 4.
    Ågren, G. & Liedén, S.Å. (1968) Some Chemical and Biological Properties of a Protein Concentrate from Sunflower Seeds,Acta Chem. Scand. 22 1981–1988.Google Scholar
  5. 5.
    Imperial Ethiopian Government (1964) Ethiopia Statistical Abstracts, Central Statistical Office, Addis Ababa.Google Scholar
  6. 6.
    Huffnagel, H.P. (1961) Agriculture in Ethiopia, FAO publication, Rome.Google Scholar
  7. 7.
    Ågren, G. & Gibson, R. (1969) Food Composition Table for Use in Ethiopia, Almqvist & Wiksell, Uppsala, Sweden.Google Scholar
  8. 8.
    Ågren, G. (1966) Unpublished results.Google Scholar
  9. 9.
    Hofvander, Y. (1967) Testing of Supplementary Mixtures and Weaning Foods at the Children's Home September 1965-October 1966, Report from Children Nutrition Unit, Addis Ababa.Google Scholar
  10. 10.
    Kungliga Lantbruksstyrelsens Kungorelse M.M. (1950) No. 6, p. 29–34, Sweden.Google Scholar
  11. 11.
    Spackman, D.H., Stein, W.H. & Moore, S. (1958) Automatic Recording Apparatus for Use in the Chromatography of Amino Acids.Anal. Chem. 30 1190–1206.Google Scholar
  12. 12.
    Moore, S. (1963) On the Determination of Cystine as Cysteic Acid,J. Biol. Chem. 238 235–237.Google Scholar
  13. 13.
    Lunven, P. (1963) Considérations sur le dosage de tryptophane dans les aliments végétaux,Qual. Plant. Mater. Veg. 10 276–291.Google Scholar
  14. 14.
    Rao, S.R., Carter, F.L. & Frampton, V.L. (1963) Determination of Available Lysine in Oilseed Meal Proteins,Anal. Chem. 35 1927–1930.Google Scholar
  15. 15.
    Blom, L., Hendricks, P. & Caris, J. (1967) Determination of Available Lysine in Foods,Anal. Biochem. 21 382–400.Google Scholar
  16. 16.
    Kolthoff, I.M. & Sandell, E.B. (1952) Textbook of Quantitative Inorganic Analysis, ed. 3, p. 351, Macmillan Co., New York.Google Scholar
  17. 17.
    Müller, R. (1964) Vorschrift zur Proteinbewertung in Versuchen am wachsenden Ratten,Z. Tierphysiol. Tierernähr. Futtermittelk. 19 305–308.Google Scholar
  18. 18.
    National Academy of Sciences-National Research Council (1963) Evaluation of Protein Quality, p. 31–32, Publication 1100, Washington D.C.Google Scholar
  19. 19.
    Hawk, P.B., Oser, B.L. & Summerson, W.H. (1947) Practical Physiological Chemistry, ed. 12, p. 837, Blakiston Comp. Philadelphia, Toronto.Google Scholar
  20. 20.
    Kabat, E.A. & Mayer, M.M. (1961) Experimental Immunochemistry, ed. 2, p. 149, Thomas Books, Springfield, Illinois.Google Scholar
  21. 21.
    Liener, I.E. (1955) The Photometric Determination of the Hemagglutinating Activity of Soyin and Crude Soybean Extracts,Arch. Biochem. Biophys. 54 223–231.Google Scholar
  22. 22.
    Eklund, A. (1969) Unpublished results.Google Scholar
  23. 23.
    Ouchterlony, Ö, 1967 Handbook of Experimental Immunology, ed. by Weir, p. 675, Blackwell Scientific Publications, Oxford.Google Scholar
  24. 24.
    Feinberg, J.G. (1957) Identification, Discrimination and Quantification in Ouchterlony Gel Plates,Int. Arch. Allergy Appl. Immunol. 11 129–152.Google Scholar
  25. 25.
    Joint FAO/WHO Expert Group (1965) Protein Requirements,WHO Tech. Rep. Ser. 301 35–38.Google Scholar
  26. 26.
    Meldolesi, J. (1967) On the Significance of the Hypertrophy of the Smooth Endoplasmic Reticulum in Liver Cells after Administration of Drugs,Biochem. Pharmacol. 16 125–129.Google Scholar
  27. 27.
    Rackis, J.J. & Anderson, R.L. (1964) Isolation of four Soybean Trypsin Inhibitors by DEAE—cellulose Chromatography,Biochem. Biophys. Res. Commun. 15 230–235.Google Scholar
  28. 28.
    Bird, G.W. (1959) Hemagglutinins in Seeds,Brit. Med. Bull. 15 165–168.Google Scholar
  29. 29.
    Krüpe, M. (1954) Inkomplete Hemagglutinine in Pflanzenextrakten,Z. Immunitätsforsch. 111 22–31.Google Scholar
  30. 30.
    Honovar, P.M., Shih, C-V. & Liener, I.E. (1962) Inhibition of the Growth of Rats by Purified Hemagglutinin Fractions Isolated from Phaseolus vulgaris,J. Nutr. 77 109–114.Google Scholar
  31. 31.
    Jaffé, W.G. (1969) Toxische und Wachstumshemmende Faktoren in Bohnen,Qual. Plant. Mater. Veg. 17 113–130.Google Scholar

Copyright information

© Dr. W. Junk N. V. - Publishers 1970

Authors and Affiliations

  • Anders Eklund
    • 1
  • Gunnar Ågren
    • 1
  1. 1.Institute of Medical ChemistryUniversity of UppsalaUppsalaSweden

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