Grasas y Aceites, Vol 55, No 4 (2004)

Purification and partial characterization of storage proteins in Lupinus angustifolius seeds

Hassane Lqari
Instituto de la Grasa, Spain

Justo Pedroche
Instituto de la Grasa, Spain

Julio Girón-Calle
Instituto de la Grasa, Spain

Javier Vioque
Instituto de la Grasa, Spain

Francisco Millán
Instituto de la Grasa, Spain


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.


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

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