Purification of 57kDa Hyaluronidase from the venom of Conus betulinus (Linnaeus, 1758)

Abstract The enzyme hyaluronidase cleaves the substrate hyaluronic acid. In the study, hyaluronidase was isolated from the venom gland of C. betulinus and characterised using SDS-PAGE, FTIR, and HPLC. The protein content of crude venom is approximately 4mg/ml, whereas purification with Sepacryl S-100 yielded 0.04mg/ml protein with 0.463TRU/mg specific activity. The detected hyaluronidase had a molecular weight of 57kDa when compared to a standard protein marker. The presence of a peak at Rt 57.23 as hyaluronidase is revealed by HPLC analysis, and the wavelength pattern is similar to the standard bovine testicular hyaluronidase.