Actividad 1 Tema 1
Actividad 1 Tema 1
Actividad 1 Tema 1
NOMBRE Y APELLIDOS……………………………………………………………..
A typical casein micelle contains thousands of casein molecules, most of which form
thermodynamically stable complexes with nanoclusters of amorphous calcium
phosphate. The structure and biological functions of the casein micelle are intimately
related. The 3 biological functions of the casein micelle considered here are (1) the safe
secretion of high concentrations of calcium and phosphate so that the mammary gland
does not become calcified, (2) the safe secretion of high concentrations of potentially
toxic fibrillogenic casein proteins through the mammary gland, and (3) retention of
micelles in the stomach of the neonate so that nutrients can be digested and absorbed.
Like many other unfolded proteins, caseins have an actual or potential tendency to
assemble into amyloid fibrils, particularly at the high concentrations found in milk. Fibrils
do not form in milk because an alternative aggregation pathway is followed that results
in formation of the casein micelle. As a result of forming micelles, nutritious milk can be
secreted and stored without causing either pathological calcification or amyloidosis of
the mother’s mammary tissue. The ability to sequester nanoclusters of amorphous
calcium phosphate in a stable complex is not unique to caseins. It has been
demonstrated using a number of noncasein secreted phosphoproteins and may be of
general physiological importance in preventing calcification of other biofluids and soft
tissues. Thus, competent noncasein phosphoproteins have similar patterns of
phosphorylation and the same type of flexible, unfolded conformation as caseins. The
ability to suppress amyloid fibril formation by forming an alternative amorphous
aggregate is also not unique to caseins and underlies the action of molecular chaperones
such as the small heat-shock proteins. The open structure of the protein matrix of casein
micelles is fragile and easily perturbed by changes in its environment. Perturbations can
cause the polypeptide chains to segregate into regions of greater and lesser density. As
a result, the reliable determination of the native structure of casein micelles continues to
be extremely challenging. The biological functions of caseins, such as their chaperone
activity, are determined by their composition and flexible conformation and by how the
casein polypeptide chains interact with each other. These same properties determine
how caseins behave in the manufacture of many dairy products and how they can be
used as functional ingredients in other foods. Holt, C 2013 J. Dairy Sci. 96 :6127–6146