Fractionation and characterization of proteins from <Emphasis Type="Italic">Gevuina avellana</Emphasis> and <Emphasis Type="Italic">Rosa rubiginosa</Emphasis> seeds |
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Authors: | Andrés?Moure Email author" target="_blank">María?Luisa?RúaEmail author Jorge?Sineiro Herminia?Domíguez |
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Affiliation: | 1.Departamentos de Enxe?eria Química, Xenética e Inmunoloxia,Universidad de Vigo (Campus Ourense),Ourense,Spain;2.Departamento do Chemical Engineering,Universidad de Santiago de Compostela,Santiago de Compostela,Spain;3.Dep. Bioquímica, Xenética e Inmunoloxía,University of Vigo (Campus Ourense),Ourense,Spain |
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Abstract: | 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. |
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Keywords: | Gevuina avellana protein characterization protein fractionation Rosa rubiginosa solubilization |
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