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The phosphorylation and characterisation of soybean isolate and its β‐conglycinin component by casein kinase II
Author(s) -
Burghoffer Chantal,
Chardot Thierry,
Meunier JeanClaude
Publication year - 1999
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/(sici)1097-0010(19990701)79:9<1179::aid-jsfa345>3.0.co;2-q
Subject(s) - solubility , phosphorylation , yarrowia , casein kinase 2 , casein , chemistry , biochemistry , phosphate , protein phosphorylation , soy protein , protein kinase a , kinase , chromatography , yeast , organic chemistry , cyclin dependent kinase 2
A commercial soybean isolate was phosphorylated using casein kinase II purified from the yeast Yarrowia lipolytica . Both major reserve proteins, β‐conglycinin and glycinin, were phosphorylated in a sequential way. The soybean isolate incorporated up to 0.7 mol phosphate per mole in 2 h. It was found that the phosphoester bonds were stable over time. The solubility of the phosphorylated isolate with respect to pH was not dramatically increased in comparison with the native one. However, counting the radioactivity of 32 P incorporated into the proteins (only the solubility of the phosphorylated proteins was measured in this case) showed that the solubility of the proteins was dramatically improved (up to 90% solubility for phosphorylated β‐conglycinin at pH 4). β‐Conglycinin became more soluble in the presence of CaCl 2 upon phosphorylation; this was not the case for the isolate. The iron‐binding capacity of the soy isolate and β‐conglycinin was significantly improved after phosphorylation (two and six times respectively). © 1999 Society of Chemical Industry