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ARS Home » Research » Publications at this Location » Publication #142605
Title: PROTEIN FRACTIONATION AND PROPERTIES OF SALICORNIA MEAL

Author
item Wu, Ying Victor
item Sessa, David

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: 5/7/2002
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Salicornia bigelovii Torr. is an annual salt-marsh oilseed plant. Hexane-defatted salicornia meal was extracted sequentially with 0.5 M sodium chloride (2x), water, 70% ethanol, and 0.1 N sodium hydroxide (2x). Each sodium chloride extract was dialyzed against deionized water and centrifuged to separate water-soluble fraction (albumin) from salt-soluble fraction (globulin) before freeze drying. Ethanol extract and neutralized sodium hydroxide extracts (glutelin) were dialyzed against water and freeze-dried. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of reduced albumin, globulin and glutelin showed a number of protein bands. Nitrogen solubility of defatted salicornia meal from pH 2 to 11 indicated a minimum solubility of 22% around pH 4.5. Non-protein nitrogen of defatted meal was 23% of total nitrogen. Albumin had highest lysine and sulfur amino acids per 16 g nitrogen among all the fractions analyzed.