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Protein fractionation and properties of salicornia meal
Author(s) -
Victor Wu Y.,
Sessa David J.
Publication year - 2004
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-004-0877-8
Subject(s) - glutelin , chemistry , globulin , sodium , chromatography , fractionation , solubility , sodium hydroxide , albumin , nitrogen , food science , biochemistry , storage protein , biology , organic chemistry , immunology , gene
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.