摘要

A simple and rapid procedure for the purification of beta-lactoglobulin (-LG) from bovine milk is described. The procedure exploits the major difference in molecular mass of -LG and other whey components and the existence of the former in monomeric form at acidic pH. Gel filtration of whey was carried out using a Bio-Gel P10 column at pH 3.0. Residual caseins and other milk proteins were excluded from the gel and -LG and alpha-lactalbumin (-LA) emerged as two fully resolved peaks. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that -LG was purified to apparent homogeneity, while absorption, fluorescence, and circular dichroism spectroscopy indicated the native-like conformation of the protein. Western blot analysis revealed that the antibodies raised against the purified -LG in rabbits also readily react with the commercial bovine protein. This procedure requires only 4-5hr for the purification of about 10mg of -LG from a single run while using a small column (2.3cmx83cm) of Bio-Gel P10 and has the potential for scaling up.

  • 出版日期2010