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Deamidation and Functional Properties of Food Proteins by the Treatment with Immobilized Chymotrypsin at Alkaline pH
Author(s) -
KATO AKIO,
LEE YOSHINORI,
KOBAYASHI KUNIHIKO
Publication year - 1989
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.1365-2621.1989.tb05988.x
Subject(s) - deamidation , ovalbumin , lysozyme , chymotrypsin , chemistry , chromatography , gluten , proteolysis , glutenin , globulin , gliadin , polyacrylamide gel electrophoresis , trypsin , molecular mass , electrophoresis , solubility , biochemistry , enzyme , organic chemistry , biology , antigen , protein subunit , gene , immunology , genetics
Ovalbumin, lysozyme, 7S globulin, 11S globulin, and gluten were treated with immobilized chymotrypsin on controlled‐pore glass at pH 10 at 20°C to improve their functional properties. Optimum pH of deamidation of ovalbumin by immobilized chymotrypsin was 10, where proteolysis was very limited. Deamidation percentages of ovalbumin, lysozyme, 7S globulin, 11S globulin, and gluten were 10.0, 8.4, 6.0, 5.0, and 8.0, respectively. SDS polyacrylamide gel electrophoretic patterns of ovalbumin and lysozyme showed no difference between untreated and treated proteins, while those of soy proteins and gluten showd that larger molecular weight fractions were dissociated into smaller molecular size fractions. Solubility of gluten was greatly improved at all pHs, 2‐12. Both emulsifying and foaming properties of proteins were improved by treatment with immobilized chymotrypsin.