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Extraction, denaturation and hydrophobic Properties of Rice Flour Proteins
Author(s) -
Ju Z.Y.,
Hettiarachchy N.S.,
Rath N.
Publication year - 2001
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.1365-2621.2001.tb11322.x
Subject(s) - prolamin , glutelin , denaturation (fissile materials) , isoelectric point , chemistry , globulin , chromatography , albumin , biochemistry , storage protein , nuclear chemistry , biology , immunology , gene , enzyme
Rice proteins were extracted from defatted rice flour. Turbidity measurement of supernatants revealed isoelectric points of albumin (pH 4.1), globulin (pH 4.3 and pH 7.9), and glutelin (pH 4.8), at which they were precipitated with 82.3 to 93.2% recovery efficiency. Prolamin did not aggregate and precipitate upon pH adjustment, but was precipitated by acetone. Denaturation temperatures (73.3, 78.9, and 82.2 °C) as well as enthalpy values (2.88, 3.14, and 3.79 J/g), of albumin, globulin, and glutelin were different. Prolamin did not show any thermographic denaturation peak. Heat‐denaturation of globulin and glutelin resulted in progressive increases in their surface hydrophobicities. Measurement of surface hydrophobicity would be an effective parameter to evaluate rice protein denaturation.