Selective removal of beta-lactoglobulin directly from cow's milk and preparation of hypoallergenic formulas: a bioaffinity method.
beta-Lactoglobulin, a major allergen of cow's milk, can pass into the breast milk of mothers consuming dairy products and thus sensitize a predisposed infant with a family history of atopic allergy. beta-Lactoglobulin coupled to Sepharose 4B can be used as a specific affinity matrix to remove beta-lactoglobulin from milk without the use of buffer systems. The tendency of beta-lactoglobulin to polymerize reversibly in milk promotes binding of the soluble protein to the coupled protein and a significant retardation in its elution with respect to the other milk proteins. The matrix can be regenerated with water and used repeatedly. These unique characteristics can be exploited in bioreactors designed to treat milk for the preparation of new hypoallergenic hyposensitizing milk formulas to be used by lactating mothers.
CNR Center of Molecular Biology, Department of Biochemical Sciences A. Rossi Fanelli, University La Sapienza, Rome, Italy.
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D000485:Allergens / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D002846:Chromatography, Affinity; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007223:Infant; D007225:Infant Food; D007782:Lactoglobulins / Q000276:immunology / Q000302:isolation & purification*; D008892:Milk / Q000737:chemistry / Q000276:immunology*; D016269:Milk Hypersensitivity; D011485:Protein Binding; D012685:Sepharose
D000485:Allergens; D007782:Lactoglobulins; D012685:Sepharose; D003488:Cyanogen Bromide