Influence of the reaction condistions on the chemical phosphorylation of milk proteins

International audienc

Study of the formation of complexes between DNA and esterified dairy proteins

International audienc

Proteolytic degradation of food proteins

International audienc

Peptic hydrolysis of methyl-, ethyl-, and propyl-esters of beta-casein and alpha-lactalbumin

International audienc

Phosphorylation chimique des protéines du lait. Influence des conditions de la réaction

National audienc

Specific limited hydrolysis and phosphorylation of food proteins for improvement of functional and nutritional properties

illus. 50 ref.International audienc

Improvement of solubility and emulsifying properties of milk proteins at acid pHs by esterification

International audienc

Phosphorylation of beta-lactoglobulin under mild conditions

International audienc

Phosphorylation of β-lactoglobulin using amino acids as the sole base and nucleophile of the reaction

International audienceβ-Lactoglobulin was phosphorylated with 20, 40, and 80 mol of POCl3/mol protein in the presence of 4, 5, and 6 molar excess of basic amino acid per mol POCl3. Maximal phosphorylation yields of 5 and 3 mol P/mol protein were achieved when the highest stoichiometries of POCl3/arginine and lysine were used. Proportional high amounts of basic amino acids were also grafted to the protein molecule during its phosphorylation through the phosphoamide bond. Modified proteins displayed increased negative charges and reduced isoelectric points and were monomeric. The phosphorylated and phosphoamidatedβ-lactoglobulin showed improved functional properties

Factors influencing pepsinolysis of methyl-, ethyl- and propyl-ester derivatives of beta-lactoglobulin

International audienc