Purification and partial characterization of storage proteins in Lupinus angustifolius seeds

Authors

  • Hassane Lqari Instituto de la Grasa
  • Justo Pedroche Instituto de la Grasa
  • Julio Girón-Calle Instituto de la Grasa
  • Javier Vioque Instituto de la Grasa
  • Francisco Millán Instituto de la Grasa

DOI:

https://doi.org/10.3989/gya.2004.v55.i4.202

Keywords:

Albumins, α, β and δ conglutins, Globulins, Lupinus angustifolius, Seed proteins

Abstract


Lupinus angustifolius seed proteins have been purified by sequential dialysis and ion exchange chromatography, and their amino acid composition has been studied in order to determine their nutritional value as sources of essential amino acids. Albumins include a great variety of proteins. Globulins were resolved in α, β and δ conglutins. Conglutin α is the main protein in the seeds of L. angustifolius, representing 76.6% of the total. While lysine was found to be the limiting amino acid in L. Angustifolius seed proteins as a whole, tyrosine was the limiting amino acid in albumins, and methione and lysine were limiting in globulins. Lysine, methionine and histidine were limiting amino acids in  α conglutin.

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Published

2004-12-30

How to Cite

1.
Lqari H, Pedroche J, Girón-Calle J, Vioque J, Millán F. Purification and partial characterization of storage proteins in Lupinus angustifolius seeds. grasasaceites [Internet]. 2004Dec.30 [cited 2022Dec.7];55(4):364-9. Available from: https://grasasyaceites.revistas.csic.es/index.php/grasasyaceites/article/view/202

Issue

Section

Research

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