In this study, a simple purification protocol is developed to reduce the bovine serum albumin (BSA) content in commercially available bovine submaxillary mucin (BSM). This involved purification of the BSM by one-column anion exchange chromatography protocol resulting in BSM with greatly reduced BSA content, homogeneously distributed size, and in a high yield of ∼ 43% from BSM as received from the manufacturer. The purity and composition of commercially acquired BSM was assessed by SDS-PAGE and mass spectrometry, which verified that BSA is the most abundant non-mucinous protein component. The purification effect was evident from a significantly altered CD spectrum of BSM after anion exchange chromatography.