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Effects of limited proteolysis on functional properties of ovalbumin
Author(s) -
Doi Etsushiro,
Koseki Taihei,
Kitabatake Naofumi
Publication year - 1987
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02542506
Subject(s) - ovalbumin , proteolysis , pepsin , chemistry , hydrolysis , peptide , chromatography , biochemistry , enzyme , antigen , immunology , biology
Abstract We examined the limited proteolysis of ovalbumin by pepsin and its effect on the functional properties of the ovalbumin. Pepsin hydrolyzed only the single peptide bond of ovalbumin between His‐22 and Ala‐23. This provided a large intermediate (MW 42,500), P‐ovalbumin. A P‐ovalbumin solution gave a transparent gel when heated. Under the same conditions, an ovalbumin solution gave a turbid gel. We studied the physicochemical properties of P‐ovalbumin and the formation of the transparent gel.