Study on enzymatic characteristics of hyaluronidase from bovine testicular

The enzyme used in this study was a partially purified sample of hyaluronidase, extracted and purified from bovine testicular. Using sodium hyaluronate as substrate, the pH optimum for the enzyme was pH4.5 and maximum activity was obtained at 37 ℃. The enzyme also required NaCl and BSA at a concentration of0.2mol/L and 0.45mol/L in the final incubation mixture for optimum activity. The hyaluronidase from bovine testicular was shown to be heat instable, and inhibited by metal ions, the inhibiting capacity was Fe3 +>Mn2 +>Zn2+>Al3+>Ca2+>K+>Mg2+. Chondroitin-sulphate A and C was inhibitor of bovine hyaluronidase, causing up to31.08% and 45.07% inhibition at 1.2mg/mL concentration. The enzyme activity was enhanced 1.36% and 1.05%by chondroitin-sulphate B and human serum protein at 0.012mg/mL concentration, respectively. Heparin inhibited enzyme activity at 0.012mg/mL concentration. Cysteine completely inhibited enzyme activity.