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Protein–protein interactions: Their importance in the foaming of heterogeneous protein systems
Author(s) -
Poole Stephen,
West Stuart I.,
Walters Clifford L.
Publication year - 1984
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740350618
Subject(s) - lysozyme , isoelectric point , ovalbumin , chemistry , chromatography , sucrose , isoelectric focusing , egg albumen , electrophoresis , egg white , biochemistry , enzyme , food science , biology , immune system , immunology
Analysis of egg albumen foams by electrophoresis showed that the basic protein lysozyme (pI 10.7) was strongly retained. Addition of low concentrations (0.01–0.10% w/v) of the basic proteins clupeine (pI 12) and lysozyme to solutions (0.50% w/v) of several acidic proteins (pI 4.7–6.0) greatly improved their foaming properties at pH values between the isoelectric points. Sucrose strongly enhanced the action of the basic proteins, while not significantly affecting the foaming of the acidic proteins alone. Basic proteins did not enhance the foaming of ovalbumin and egg albumen in the absence of sucrose. Clupeine enhanced foaming more effectively than lysozyme under all conditions studied. Lysozyme was least effective near the isoelectric point of the acidic protein, where electrostatic interactions were weakest. Sodium chloride (0.1 M ) had a detrimental effect on the action of lysozyme.