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Effect of Chemical Modifications on Some Physicochemical Properties and Heat Coagulation of Egg Albumen
Author(s) -
MA CHINGYUNG,
HOLME JOHN
Publication year - 1982
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.1365-2621.1982.tb04959.x
Subject(s) - carbodiimide , chemistry , succinic anhydride , monomer , coagulation , egg white , egg albumen , polymer chemistry , chromatography , chemical engineering , organic chemistry , polymer , food science , psychology , psychiatry , engineering
Egg albumen was modified with succinic anhydride and a water‐soluble carbodiimide, 1‐ethyl‐3(3‐dimethylaminopropyl) carbodiimide. The chemically modified proteins exhibited only minor conformational changes, but were altered in their responses to heat treatment. Heat‐induced coagulation was retarded by both modifications suggesting that thermocoagulation requires a balanced electrostatic attraction between protein molecules. Hydrophobicity measurements and pH‐titration data suggest the involvement of hydrophobic and ionic interactions in heat aggregation and gelation of egg white proteins. The soluble fraction of the heat‐coagulated proteins contained mainly monomers, while under conditions where a gel or coagulum was not formed, the heat‐treated egg albumen solutions contained high M.W. soluble aggregates. A scheme for the thermal coagulation of egg albumen is proposed.