Studies were carried out to selectively isolate beta-lactoglobulin from cheese whey using biospecific subunit exchange affinity chromotography (BSEAC) under varied environmental conditions, that included temperature, pH and protein concentration. The isolation of beta-lactoglobulin was achieved by the interaction between the covalently bound beta-lactoglobulin to sepharose S-CNBr-4B matrix and the protein in solution. A direct linear plotting method showed the Bt values to be temperature, pH and concentration independent. The Bt values for room temperature and 4 degrees C were 0.65 and 0.66 mu Mol, respectively. The average 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 separation efficiencies achieved were 91.15% and 84.21% for room temperautre and 4 degrees C, respectively, with the initial beta-lactoglobulin loading in the 15.0 mg range. It has been shown that beta-lactoglobulin can be separated from cheese whey by BSEAC. This process may result in the commercial manufacture of beta-lactoglobulin reduced whey protein concentrates as well as native pure beta-lactoglobulin fraction. Both products may have specific nutritional/pharmaceutical applications.
