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 a water-soluble fraction (albumin) from a salt-soluble fraction (globulin) before freeze-drying. Ethanol extracts and neutralized sodium hydroxide extracts (glutelin) were dialyzed against water and freeze-dried. Globulin accounted for the highest amount of protein nitrogen, followed by glutelin and albumin. SDS-PAGE 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. Nonprotein nitrogen of defatted meal was 23% of total nitrogen, higher than defatted soybean, sunflower, and rapeseed meals. Albumin had the highest proportion of lysine and sulfur amino acids per 16 g nitrogen among all the fractions analyzed.
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Victor Wu, Y., Sessa, D.J. Protein fractionation and properties of salicornia meal. J Amer Oil Chem Soc 81, 173–176 (2004). https://doi.org/10.1007/s11746-004-0877-8
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DOI: https://doi.org/10.1007/s11746-004-0877-8