Purification of β-Lactoglobulin from Whey Protein Concentrate by Pepsin Treatment
Authors:
- Naofumi KitabatakeNKNaofumi Kitabatake
Open Access
- 1 March 1996
- journal article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 79 (3) , 350-356
Abstract
Beta-Lactoglobulin was purified from whey protein concentrate by a combination of pepsin treatment and membrane filtration. Porcine pepsin was added to whey protein (1:200, wt/wt), and the mixture was then incubated at pH 2.0 and 37 degrees C for 60 min. The protein fraction was collected by ammonium sulfate precipitation, and the precipitate was either dialyzed against water using a dialysis membrane (20-kDa pore size) or filtered using an UF membrane (30-kDa pore size). The beta-LG did not differ from standard beta-LG as measured by chromatography, SDS-PAGE, native PAGE, differential scanning calorimetry, or UV spectrum. Based on the results, a simplified procedure was developed, consisting of pepsin treatment and UF, to purify beta-LG directly from whey.Keywords
This publication has 16 references indexed in Scilit:
- Simple and Rapid Method for Measuring Turbidity in Gels and Sols from Milk Whey ProteinJournal of Food Science, 1994
- Ultrafiltration and Manufacture of Whey Protein Concentrates1992
- Effects of In Vitro Proteolysis on the Allergenicity of Major Whey ProteinsJournal of Food Science, 1989
- Structural and conformational basis of the resistance of .beta.-lactoglobulin to peptic and chymotryptic digestionJournal of Agricultural and Food Chemistry, 1988
- Separation and Quantification of Whey Proteins by Size Exclusion ChromatographyCanadian Institute of Food Science and Technology Journal, 1986
- The structure of β-lactoglobulin and its similarity to plasma retinol-binding proteinNature, 1986
- Hydrophobic interaction fast protein liquid chromatography of milk proteinsJournal of Chromatography A, 1986
- Determination of native and denatured milk proteins by high-performance size exclusion chromatographyJournal of Chromatography A, 1983
- [20] The porcine pepsins and pepsinogens1970
- Molecular Interactions in β-Lactoglobulin. II. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin below its Isoelectric Point2Journal of the American Chemical Society, 1960