The stonefish, Synanceja horrida, is found in the waters around Singapore, Malaysia and Indonesia. It consists of 13 dorsal spines in which the venom glands are located.
Stonefish Synanceja horrida venom hyaluronidase is the first of such enzymes to be purified to homogeneity from a marine source. Studies on the reaction products and enzymatic properties stonefish hyaluronidase have shown that it acts as an endo-b-N-acetyl-D-hexosaminidase with an enzymic action similar to that of mammalian testicular hyaluronidase. ). It has a pI of 9.2 and a molecular weight of 62 kDa, and acts as a spreading factor by degrading hyaluronic acid and hence, facilitates the diffusion and absorption of other stonefish venom constituents (including stonustoxin, a multifunctional lethal protein factor isolated from the venom), thereby leading to systemic envenomation. The high potency of the enzyme is probably responsible for the extensive necrosis associated with envenomation.
Moreover, stonefish venom hyaluronidase hyaluronidase has been found to be more specific for hyaluronic acid, as well as exhibits higher specific activity compared to the testicular hyaluronidase (which is currently in clinical use). It has also been demonstrated to require a shorter time for the dispersion of oocyte cumulus than that of the commercially available sheep hyaluronidase, and has no detrimental effects on murine fertilization. Furthermore, intravenous injection of the purified enzyme did not lead to the lethal effects of the stonefish venom. This suggests the potency and safety for stonefish venom hyaluronidase for murine in-vitro fertilization (IVF) research. Therefore, stonefish hyaluronidase may serve as a safe and useful alternative to the currently available enzyme preparations for medical and pharmacological applications.