Purification and partial characterization of storage proteins in <i>Lupinus angustifolius</i> seeds

Hassane Lqari; Justo Pedroche; Julio Girón-Calle; Javier Vioque; Francisco Millán

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

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

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 2023Dec.2];55(4):364-9. Available from: https://grasasyaceites.revistas.csic.es/index.php/grasasyaceites/article/view/202

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Issue

Vol. 55 No. 4 (2004)

Section

Research

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