[Behavior of iron fixed on bovine and phosphorylated casein after hydrolysis produced by digestive proteases].
The phosphate groups of the native and phosphorylated casein have the property of sequestering the iron. This metal fixation depends on the casein's degree of phosphorylation. The phosphate groups either, naturally present or chemically binded, are the preferential fixation sites for iron. They modify the affinity constant of the casein respecto to iron. Both, phosphorylation and ironfixation influence negatibily the caseins sensibility to digestive protease. Whichever the enzyme might be, the hydrolysis of the casein with fixed iron produces fixed iron peptides. It seems that iron retention is a function of the number of phosphate groups associated to casein.
Medina Gallardo
A L
AL
Escuela de Ingeniería Química, Facultad de Ingeniería, Universidad de Los Andes Edo, Mérida, Venezuela.
D000818:Animals; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D006868:Hydrolysis; D007501:Iron / Q000378:metabolism*; D010194:Pancreatin / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D014357:Trypsin / Q000378:metabolism
D002364:Caseins; D010194:Pancreatin; D007501:Iron; D014357:Trypsin; D010434:Pepsin A
Estudio del comportamiento del hierro fijado sobre la caseína bovina y fosforilada luego de la hidrólisis producida por las proteasas digestivas.