Hyaluronidase

Hyaluronidase degrades hyaluronic acid through the cleavage of glycosidic bonds. Initially discovered in bacteria, this enzyme is known to be widely distributed in nature and has been found in various species, including insects, snakes, fish, and mammals. In humans, six different hyaluronidases have been identified, namely HYAL 1-4, HYAL-P1, and PH-20. PH-20 exhibits the strongest biological activity, with high concentrations found in the testes and localization on the head and acrosome of human sperm. Currently, hyaluronidases sourced from animal testes, such as bovine or ovine, as well as synthetic hyaluronidases, are applied clinically as adjuncts for increasing drug bioavailability, treating extravasation, or managing complications associated with cosmetic injections using hyaluronic acid-based fillers^[1].

References:
[1] Buhren B A , Schrumpf H , Hoff N P ,et al. Hyaluronidase: from clinical applications to molecular and cellular mechanisms[J].European Journal of Medical Research, 2016, 21(1).DOI:10.1186/s40001-016-0201-5.