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Fractionation and characterization of proteins from Gevuina avellana and Rosa rubiginosa seeds
Author(s) -
Moure Andrés,
Rúa María Luisa,
Sineiro Jorge,
Domíguez Herminia
Publication year - 2005
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/s11746-005-5168-2
Subject(s) - isoelectric point , chemistry , chromatography , fractionation , size exclusion chromatography , isoelectric focusing , molecular mass , biochemistry , enzyme
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.