SEPARATION OF BETA-LACTOGLOBULIN VARIANT-A AND VARIANT-B FROM CHEESE WHEY BY BIOSPECIFIC SUBUNIT EXCHANGE AFFINITY-CHROMATOGRAPHY

Studies were carried out to selectively isolate beta-lactoglobulin fro m cheese whey using biospecific subunit exchange affinity chromotograp hy (BSEAC) under varied environmental conditions, that included temper ature, pH and protein concentration. The isolation of beta-lactoglobul in was achieved by the interaction between the covalently bound beta-l actoglobulin to sepharose S-CNBr-4B matrix and the protein in solution . A direct linear plotting method showed the Bt values to be temperatu re, pH and concentration independent. The Bt values for room temperatu re and 4 degrees C were 0.65 and 0.66 mu Mol, respectively. The averag e Kd values for the cheese whey extraction model were 0.36 and 0.17 mu Mol at room temperature and 4 degrees C, respectively. The highest se paration efficiencies achieved were 91.15% and 84.21% for room tempera utre and 4 degrees C, respectively, with the initial beta-lactoglobuli n loading in the 15.0 mg range. It has been shown that beta-lactoglobu lin can be separated from cheese whey by BSEAC. This process may resul t in the commercial manufacture of beta-lactoglobulin reduced whey pro tein concentrates as well as native pure beta-lactoglobulin fraction. Both products may have specific nutritional/pharmaceutical application s.