Lactalbumin is a milk protein obtained from whey by acidifying to
ph 5.2, the isoelectric point, followed by coagulation by heat. it is
not coagulated by rennin as is casein and is nonfunctional in its
properties. it is used for nutritional purposes as a source of protein.
it is used in cereals and breads where its relative inertness minimizes
complications caused by other milk proteins during baking. it is also
termed milk albuminate.
α-Lactalbumin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.
LACTALBUMIN is a protein, belonging to the albumins, derived from milk.
α-Lactalbumin is a small, globular, whey protein that has been found in all milk studied to date. It is a metalloprotein of approximately 14 kDa produced in the mammary glands.
α-Lactalbumin consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. α-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native α-lactalbumin from the reduced, denatured form. α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. The mature protein consists of 123 amino acid residues (14 kDa), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four a-helices and a triple stranded antiparallel β-sheet.
