Fractionation and characterization of proteins from Gevuina avellana and Rosa rubiginosa seeds

• Published in: Journal of the American Oil Chemists' Society Vol. 82; no. 3; pp. 169 - 173
• Main Authors: Moure, A, Rua, M.L, Dominguez, H
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer-Verlag 01.03.2005; Springer; Springer Nature B.V
• Subjects: Acetic acid; Biological and medical sciences; Chromatography; Fat industries; Filtration; Food industries; Fractionation; Fundamental and applied biological sciences. Psychology; Gevuina avellana; Oils & fats; plant proteins; Proteaceae; protein characterization; protein fractionation; Proteins; Rosa rubiginosa; Seeds; Sodium chloride; Sodium hydroxide; solubility; solubilization; Characterization; Oils and fats industry; Gevuina avellana; Fractionation; Seeds; protein characterization; protein fractionation; Solubilization; Protein; Rosa rubiginosa
• DOI: 10.1007/s11746-005-5168-2
• ISSN: 0003-021X

Gevuina avellana and Rosa rubiginosa proteins were evaluated for their potential food use. The proteins were sequentially separated into five fractions according to their solubilities in deionized water, 0.5 M NaCl, 70% (vol/vol) isopropyl alcohol, 50% (vol/vol) glacial acetic acid, and 0.1 M NaOH. The five fractionated protein groups were then characterized by SDS-PAGE and gel filtration chromatography to determine their M.W. profiles. Ninety-six percent of G. avellana total protein was solubilized in three extraction stages, and 88% of R. rubiginosa total protein was solubilized in one extraction stage. Albumins were the major protein fraction in G. avellana and glutelins-1 the most abundant in R. rubiginosa. The protein solubility profile determined over the pH range 1-12 showed minimal solubilities at pH 3-5 and pH 3-7 for G. avellana and R. rubiginosa, respectively. Electrophoretic studies revealed the existence of proteins composed of two major kinds of polypeptides linked together via disulfide bonds and with molecular masses ranging from 13 to 119 kDa. Gel filtration chromatography profiles of globulins and albumins were studied for both seeds. Isoelectric focusing showed an isoelectric point in the ranges of 4.5-6 and 3-6.5 for G. avellana and R. rubiginosa proteins, respectively.