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Modification of Egg White Proteins with Oleic Acid
Author(s) -
KING A. J.,
BALL H. R.,
CATIGNANI G. L.,
SWAISGOOD H. E.
Publication year - 1984
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1984.tb14962.x
Subject(s) - egg white , lysozyme , oleic acid , ovalbumin , chemistry , reagent , chromatography , mole , biochemistry , biology , organic chemistry , immunology , immune system
Studies on the chemical modification of egg white with oleic acid (5‐50 moles/50,000g of egg white protein) revealed that the reagent partitioned equally between supernatant and precipitate. The mole ratio of oleic acid to protein in solution at the 20 mole level of treatment was 14.6:1. Oleic acid did not selectively precipitate ovalbumin, conalbumin, or lysozyme. An increase in negative charge of proteins was observed in the chromatograms of treated egg white. No difference in molecular weights of treated egg white proteins was observed. The viscosity varied with the concentration of the reagent. In cooked, frozen, and thawed egg white water retaining index was 1.5‐10X greater for treated than untreated material.