An overview on Hyaluronidase enzyme types, mode of action, assay and therapeutic applications

Document Type : Original Article

Authors

1 Botany Department, Faculty of women For Arts, Science and Education, Ain shams university, Egypt.

2 Protein Research Department, Genetic Engineering and Biotechnology Research Institute GEPRI, City of Scientific Research and Technological Applications (SRTA-City), New Borg Al Arab 21934, Alexandria, Egypt. , Pharmaceutical and Fermentation Industries Development Centre (PFIDC), City of Scientifc Research and Technological Applications (SRTA-City), New Borg Al Arab 21934, Alexandria, Egypt.

Abstract

Hyaluronidase is an enzyme of the current era.  Not only because of its medical importance for cancer therapy but also because of its great importance in many fields. Hyaluronidases have substantial biological activity in the realm of medicine in addition to being useful enzymes for producing low molecular weight hyaluronic acid. It is employed clinically as a significant drug diffusion promoter to aid in the absorption of drug and localized hematoma or edema dissipation following trauma or surgery. Hyaluronidases made from animals have some drawbacks, including few resources, poor content, high cost, and the possibility of virus infection. Contrarily, hyaluronidase generated from microorganisms are more widely used due to their abundant source, straightforward fermentation procedure, low cost, high purity, and minimal environmental contamination. Microbial hyaluronidases are known as hyaluronate lyases Owing to the unsaturated double bonds they form at non-reducing ends by breaking down hyaluronic acid through the β-elimination reaction. Streptococcus spp, Staphylococcus spp, and other microbes have all been found to have hyaluronate lyases to date.

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