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Functional properties of acetylated and succinylated sunflower protein isolate
Author(s) -
KABIRULLAH M.,
WILLS R. B. H.
Publication year - 1982
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1982.tb00179.x
Subject(s) - succinylation , isoelectric point , succinic anhydride , acetic anhydride , lysine , acetylation , chemistry , sunflower , chlorogenic acid , solubility , aqueous solution , acylation , organic chemistry , biochemistry , chromatography , amino acid , biology , agronomy , gene , enzyme , catalysis
Summary Sunflower protein isolate was acylated with acetic and succinic anhydride. Succinylation changed the electrophoretic mobility, decreased the lysine and chlorogenic acid content and bulk density, increased the aqueous solubility, shifted the isoelectric point and increased the absorption, emulsification and foaming properties. Acetylation improved the functional properties of the protein to a much lesser extent. Implication of these changes is discussed with reference to food applications.