ISOLATION, MOLECULAR AND BIOCHEMICAL CHARACTERIZATION OF GOAT MILK CASEIN AND ITS FRACTIONS

The SDS-PAGE electrophoretic pattern of goats´ milk has a unique pattern compared to those of cow and human milk. β-casein is the major fraction and comprises 70.2% of total goat-milk caseins, while αs- is a minor fraction (29.85 %). This pattern is similar to that of human casein but different t...

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Detalles Bibliográficos
Autores: Salem, Samir Ahmed, Elagamy, Elsayed Ibrahim, Salama, Fatma, Abosoliman, Nagwa Hussein
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:México
Institución:UNIVERSIDAD AUTÓNOMA DE YUCATÁN
Repositorio:Tropical and Subtropical Agroecosystems
Idioma:inglés
español
OAI Identifier:oai:ojs.www.revista.ccba.uady.mx:article/67
Acceso en línea:https://www.revista.ccba.uady.mx/ojs/index.php/TSA/article/view/67
Access Level:acceso abierto
Palabra clave:agriculture
Goat milk casein- fractions of casein- human casein-essential amino acids
Descripción
Sumario:The SDS-PAGE electrophoretic pattern of goats´ milk has a unique pattern compared to those of cow and human milk. β-casein is the major fraction and comprises 70.2% of total goat-milk caseins, while αs- is a minor fraction (29.85 %). This pattern is similar to that of human casein but different to that of cow casein. Purified casein fractions of goat milk showed different electrophoretic migration compared to those of bovine milk. The corresponding Mr(s) of goat αs- and β-casein were estimated at 30.2 for αs and 26.6 & 23.9 for β1 and β2 versus 32.6 and 26.6 for bovine αs- and β-casein, respectively. The amino acid composition of goat-milk whole casein appeared to be similar to those of cow, sheep and camel caseins. Meanwhile, goat casein has the satisfactory balance of essential amino acids equal to or exceeding the FAO/ WHO/ UNU requirements for each amino acid. Goat αs-casein was characterized by the presence of higher contents of both acidic and basic amino acids than β-casein. Peptide mapping profiles of goat, cow and human caseins were completely different. This means that each protein has its own unique peptide mapping.