Purification of beta-lactoglobulin from whey protein concentrate by pepsin treatment.
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.
Kinekawa
Y
Y
Research Institute for Food Science, Kyoto University, Japan.
Kitabatake
N
N
D000645:Ammonium Sulfate; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003956:Dialysis; D004591:Electrophoresis, Polyacrylamide Gel; D005374:Filtration; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007782:Lactoglobulins / Q000302:isolation & purification*; D008894:Milk Proteins / Q000737:chemistry*; D010434:Pepsin A / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D000067816:Whey Proteins
D007782:Lactoglobulins; D008894:Milk Proteins; D000067816:Whey Proteins; D010434:Pepsin A; D000645:Ammonium Sulfate