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Some Functional Properties under Heating of the Globin Prepared by Carboxymethyl Cellulose Procedure
Author(s) -
HAYAKAWA S.,
OGAWA T.,
SATO Y.
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.tb04951.x
Subject(s) - isoelectric point , carboxymethyl cellulose , ovalbumin , globin , chemistry , bovine serum albumin , chromatography , albumin , hemoglobin , biochemistry , organic chemistry , biology , immunology , immune system , enzyme , sodium
Conditions for gel formation of heated globin and inhibition of thermocoagulation of ovalbumin and bovine serum albumin by globin were investigated. Globin was highly soluble even when heated at 100°C at pH below 5. Globin also considerably inhibited thermocoagulation of ovalbumin and serum albumin near their isoelectric point. A great increase of viscosity was observed when 1% globin solution was heated at above 80°C in the narrow pH range between pH 5.2 and 5.4. Heated globin formed a transparent gel at concentration above 3% under well controlled heat conditions.