A simple method for enrichment of β-lactoglobulin from bovine milk whey involving selective hydrolysis by two fungal protease preparations

Abstract

Two commercially available food grade fungal protease preparations (Fungal Protease 31,000 and Fungal Protease 60000) were found to hydrolyse bovine acid whey proteins but left the beta-lactoglobulin (β-Lg) intact under the processing conditions used. Comparative analysis before and after hydrolysis of bovine acid whey, by 1D- and 2D-PAGE, RP-HPLC and intact-mass mass spectrometry showed that the β-Lg remains intact and in high yield after hydrolysis by the fungal proteases. The β-Lg could be separated from the whey protein peptide hydrolysate by ultrafiltration. Subjecting whey fraction to hydrolysis with the fungal protease preparations provides a procedure, under relatively mild conditions, to generate a highly enriched β-Lg fraction. β-Lg is recognised as a valued material in the food, pharmaceutical and cosmetic industries due to its properties such as gelling and foaming. The enriched β-Lg preparation would also have application in areas such as nanoencapsulation.