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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Plant Polymer Research » Research » Publications at this Location » Publication #191890

Title: FUNCTIONAL PROPERTIES OF PROTEINS IN LESQUERELLA SEED AND PRESS CAKE FROM OIL PROCESSING

Author
item Hojilla-Evangelista, Milagros - Mila
item Evangelista, Roque

Submitted to: American Oil Chemists' Society Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 1/30/2006
Publication Date: 4/30/2006
Citation: Hojillaevangelist, M.P., Evangelista, R.L. 2006. Functional properties of proteins in lesquerella seed and press cake from oil processing [abstract]. American Oil Chemists' Society Meeting. p.108.

Interpretive Summary:

Technical Abstract: Lesquerella seed oil has generated great interest because its hydroxy FAs are similar to the main FA found in castor oil and could be used in lubricants, coatings, paint, and cosmetics. Processing Lesquerella seed for oil is expected to produce protein-rich meals (30% crude protein) for which uses and markets will have to be developed. We recently completed a study that determined the soluble classes, amino acid composition, and MW of major fractions of Lesquerella seed proteins. The present investigation determined the functional properties of protein in Lesquerella seed and press cake from oil processing. Unprocessed Lesquerella seed protein showed the greatest solubility (greater than 60%) at pH 2 and 10, was least soluble (25%) at pH 5.5-7, had high surface hydrophobicity index (S0) and had excellent foaming capacity and stability, emulsifying properties, and water-holding capacity (WHC). Protein solubility profile of the press cake showed up to 50% reduction in soluble proteins at nearly all pH levels, indicating heat denaturation during cooking and screw-pressing. Foaming capacity of the press cake protein decreased slightly, but foam stability was completely lost. Press cake protein also had markedly reduced values fo S0, emulsifying properties and WHC, further confirming Lesquerella protein's sensitivity to heat treatment.