Neuraminidase from Clostridium perfringens is widely used in biochemical research and industrial applications due to its ability to cleave sialic acid residues from glycoproteins, glycolipids, and oligosaccharides. In the field of glycobiology, it is employed to study the structure and function of sialylated molecules, helping researchers understand cell surface interactions, signaling pathways, and immune responses. In the pharmaceutical industry, it is utilized in the production of glycoprotein-based drugs, where the removal of sialic acid residues can enhance therapeutic efficacy or stability. Additionally, it plays a role in diagnostic assays, particularly in detecting and characterizing sialic acid-containing biomarkers associated with diseases such as cancer and infectious diseases. Its application also extends to the food industry, where it is used to modify the properties of sialylated compounds in dairy products and other foods to improve texture, flavor, or nutritional value.