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PHYSICO‐CHEMICAL CHARACTERIZATION OF MONOMERIC CHEMICALLY PHOSPHORYLATED CASEINS
Author(s) -
SITOHY MAHMOUD,
CHOBERT JEANMARC,
HAERTLE TOMASZ
Publication year - 1995
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1995.tb00524.x
Subject(s) - mole , triethylamine , monomer , chemistry , phosphorylation , mole fraction , isoelectric point , casein , phosphopeptide , isoelectric focusing , molar ratio , chromatography , biochemistry , organic chemistry , catalysis , polymer , enzyme
Casein was phosphorylated under mild conditions with low molar ratios of POCl 3 (25, 50 and 100 mole POCl 3 /mole protein) in the presence of equivalent amounts of triethylamine. Consequently, the resulting modified proteins (4–21 mole P/mole protein) had increased negative charges, lower isoelectric points and existed mainly in a monomeric form. The extent of change in functional properties depended mainly on the degree of phosphorylation and the initial caseins.