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School of Medicine and Pharmacy, Ocean University of China, Qingdao, 266003, China; Qingdao Marine Science and Technology Center, Qingdao, 266237, China; Key Laboratory of Marine Drugs, Ministry of Education, Ocean University of China, Qingdao 266003, China; Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Ocean University of China, Qingdao, 266003, China. Electronic address:
Published: November 2024
AI Article Synopsis
Hyaluronidase is an enzyme that helps break down hyaluronic acid, which is important for medicine and beauty treatments.
Scientists discovered a new enzyme called EsHyl8 from a type of bacteria found in human intestines that also breaks down hyaluronic acid.
EsHyl8 works best at warm temperatures and is really strong, but it can be slowed down by certain metals and substances.
Article Abstract
Hyaluronidase, an enzyme that degrades hyaluronic acid (HA), is utilized in clinical settings to facilitate drug diffusion, manage extravasation, and address injection-related complications linked to HA-based fillers. In this study, a novel hyaluronate lyase EsHyl8 was cloned, expressed, and characterized from Escherichia sp. A99 of human intestinal origin. This lyase belongs to polysaccharide lyase (PL) family 8, and showed specific activity towards HA. EsHyl8 exhibited optimal degradation at 40 °C and pH 6.0. EsHyl8 exhibited a high activity of 376.32 U/mg among hyaluronidases of human gut microorganisms. EsHyl8 was stable at 37 °C and remained about 70 % of activity after incubation at 37 °C for 24 h, demonstrating excellent thermostability. The activity of EsHyl8 was inhibited by Zn, Cu, Fe, and SDS. EsHyl8 was an endo-type enzyme whose end-product was unsaturated disaccharide. This study enhances our understanding of hyaluronidases from human gut microorganisms.
