Abstract:In this study, polyacrylamide gel electrophoresis (PAGE) was used to explore the enzymatic properties of chondroitinase A (CSAase) produced by strain RC3. A crude solution of intracellular chondroitinase was obtained by ultrasonication of the microbial cells, which was then mixed with an equal volume of chondroitin sulfate A (CSA) and incubated. The effect of various culture conditions on enzyme activity was studied using PAGE. The results showed that the optimal temperature and pH value for fermentation of CSAase were 20 ℃ to 40 ℃ and 8.0, respectively. Magnesium ion was found to activate CSAase, while copper and zinc ions were strong inhibitors. Potassium, calcium, sodium, manganese, and barium ions did not significantly affect enzyme activity. Magnesium ions at a concentration of 10 mM showed the strongest activating effect on CSAase. Copper and zinc ions showed strong inhibitory effect on the enzyme activity at a concentration of 5 mM. Under the above optimal conditions, the low-molecular-weight products that were obtained after a 4-hour hydrolysis reaction using this enzyme, showed a higher antioxidant activity than that of CSA, which is a macromolecule. This study suggests the potential applicability of CSAase.
