2017-09-132017-09-132015-12BRASIL, Rafaella Belchior; NICOLAU Edmar Soares; CABRAL, Jakeline Fernandes; SILVA, Marco Antônio Pereira da. Estrutura e estabilidade das micelas de caseína do leite bovino. Ciência Animal, Fortaleza, v. 25, n. 2, p. 71-80, jun./set. 2015.0104-3773http://repositorio.bc.ufg.br/handle/ri/12468Milk proteins are natural vehicles, which provides essential micronutrients, amino acids, and components of the immune system, in addition, possess properties characteristic of fundamental importance in many dairy products.The caseins are the major milk proteins comprise about80%of milk proteinandconsistsoffourmajor proteins: αs1-, αs2-, β-and κ-casein, which have high thermal stability, which provides industriesdairymilkperform the treatmentat elevated temperatures, such as milk UltraHigh Temperature(UHT). However, certain factors such as the enzymatic hydrolysis of kcasein, temperature, pH, excessive addition of Ca2+ and ethanol affect the stability of these proteins, whicharelargelypresent in milkin the form ofcolloidal particles, known as micelles. The internal structure ofthe caseinmicelleconsists predominantly ofαs1-, αs2-, β-casein, nanoparticlecolloidalcalcium phosphate, whereas κ-casein ispreferably locatedon the surfaceof the micelle, assuming an important role inmicellestability. Interest in micellar casein remains constant over the years, and research on the subject continue to be made, so the relevance of understanding the structure and the factors that affect the micellar stability.porAcesso AbertoCaseínaEstabilidade térmicaEstrutura micelarHidróliseProteínasCaseinThermal stabilityMicellar structureHydrolysisProteinArtigo