Composition and functional properties of Lupinus campestris protein isolates

S. L. Rodríguez-Ambriz, A. L. Martínez-Ayala, F. Millán, G. Dávila-Ortíz

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Protein isolates from L. campestris and soybean seeds were prepared using isoelectric precipitation (PI) and micellization (MI) procedures. The amount of protein recovered was considerably higher with the isoelectric precipitation than with the micellization procedure (60% and 30%, respectively). Protein contents were higher than 90% in protein isolates. Antinutritional factors content (alkaloids, lectins, and tannins) were reduced to innocuous levels after protein isolate preparation. Minimum protein solubility for the precipitated lupin protein isolate (LPI) was at pH 4.0, and between pH 4 and 6 for the micellized lupin protein isolate (LMI), increasing at both extremes of the pH scale. Water absorption for the LMI was 1.3 ml/g of protein and its oil absorption 2.2 ml/g of protein. The LPI had 1.7 ml/g of protein in both water and oil absorption. Foaming capacity and stability was pH-dependent. Foaming capacity was higher at pH 2 and lower near the protein isoelectric points. Minimum protein concentration for gelation in LMI was 8% w/v at pH 4, while for LPI was 6% at pH 4 and 6. Amino acid composition in L. campestris flour and protein isolates was high in lysine and low in methionine. Most of the essential amino acids in lupin protein isolates were at acceptable levels compared to a reference pattern for infants and adults. The electrophoretic pattern of both protein isolates showed three bands with different mobilities, suggesting that the protein fractions belong to α-conglutin (11S-like protein), β-conglutin (7S-like protein) and γ-conglutin. It is proven that some of the functional properties of L. campestris protein isolates are similar to those soybean protein isolates recovered under equal conditions. ©2005 Springer Science+Business Media, Inc.
Original languageAmerican English
Pages (from-to)99-107
Number of pages88
JournalPlant Foods for Human Nutrition
DOIs
StatePublished - 1 Sep 2005

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Lupinus
protein isolates
functional properties
Chemical analysis
Proteins
proteins
foaming capacity
Micellization
oils
antinutritional factors
protein solubility
isoelectric point
gelation
soy protein
essential amino acids
amino acid composition
lectins
water uptake
tannins
Oils

Cite this

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title = "Composition and functional properties of Lupinus campestris protein isolates",
abstract = "Protein isolates from L. campestris and soybean seeds were prepared using isoelectric precipitation (PI) and micellization (MI) procedures. The amount of protein recovered was considerably higher with the isoelectric precipitation than with the micellization procedure (60{\%} and 30{\%}, respectively). Protein contents were higher than 90{\%} in protein isolates. Antinutritional factors content (alkaloids, lectins, and tannins) were reduced to innocuous levels after protein isolate preparation. Minimum protein solubility for the precipitated lupin protein isolate (LPI) was at pH 4.0, and between pH 4 and 6 for the micellized lupin protein isolate (LMI), increasing at both extremes of the pH scale. Water absorption for the LMI was 1.3 ml/g of protein and its oil absorption 2.2 ml/g of protein. The LPI had 1.7 ml/g of protein in both water and oil absorption. Foaming capacity and stability was pH-dependent. Foaming capacity was higher at pH 2 and lower near the protein isoelectric points. Minimum protein concentration for gelation in LMI was 8{\%} w/v at pH 4, while for LPI was 6{\%} at pH 4 and 6. Amino acid composition in L. campestris flour and protein isolates was high in lysine and low in methionine. Most of the essential amino acids in lupin protein isolates were at acceptable levels compared to a reference pattern for infants and adults. The electrophoretic pattern of both protein isolates showed three bands with different mobilities, suggesting that the protein fractions belong to α-conglutin (11S-like protein), β-conglutin (7S-like protein) and γ-conglutin. It is proven that some of the functional properties of L. campestris protein isolates are similar to those soybean protein isolates recovered under equal conditions. {\circledC}2005 Springer Science+Business Media, Inc.",
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Composition and functional properties of Lupinus campestris protein isolates. / Rodríguez-Ambriz, S. L.; Martínez-Ayala, A. L.; Millán, F.; Dávila-Ortíz, G.

In: Plant Foods for Human Nutrition, 01.09.2005, p. 99-107.

Research output: Contribution to journalArticle

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AU - Rodríguez-Ambriz, S. L.

AU - Martínez-Ayala, A. L.

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