E. Chiancone et M. Gattoni, SELECTIVE REMOVAL OF BETA-LACTOGLOBULIN DIRECTLY FROM COWS MILK AND PREPARATION OF HYPOALLERGENIC FORMULAS - A BIOAFFINITY METHOD, Biotechnology and applied biochemistry, 18, 1993, pp. 1-8
Beta-lactoglobulin, a major allergen of cows milk, can pass into the b
reast milk of mothers consuming dairy products and thus sensitize a pr
edisposed infant with a family history of atopic allergy. Beta-lactogl
obulin coupled to Sepharose 4B can be used as a specific affinity matr
ix to remove beta-lactoglobulin from milk without the use of buffer sy
stems. The tendency of beta-lactoglobulin to polymerize reversibly in
milk promotes binding of the soluble protein to the coupled protein an
d a significant retardation in its elution with respect to the other m
ilk proteins. The matrix can be regenerated with water and used repeat
edly. These unique characteristics can be exploited in bioreactors des
igned to treat milk for the preparation of new hypoallergenic hyposens
itizing milk formulas to be used by lactating mothers.