Messina, LucianoGavira, Jose APernagallo, SalvatoreUnciti-Broceta, Juan DSanchez Martin, Rosario MDiaz-Mochon, Juan JVaccaro, SusannaConejero-Muriel, MaytePineda-Molina, EstelaCaruso, SalvatoreMusumeci, LucaDi Pasquale, RobertaPontillo, AngelaSincinelli, FrancescaPavan, MauroSecchieri, Cynthia2023-01-252023-01-252016-07-04http://hdl.handle.net/10668/10184Hyaluronidases (Hyals) are broadly used in medical applications to facilitate the dispersion and/or absorption of fluids or medications. This study reports the isolation, cloning, and industrial-scale recombinant production, purification and full characterization, including X-ray structure determination at 1.45 Å, of an extracellular Hyal from the nonpathogenic bacterium Streptomyces koganeiensis. The recombinant S. koganeiensis Hyal (rHyal_Sk) has a novel bacterial catalytic domain with high enzymatic activity, compared with commercially available Hyals, and is more thermostable and presents higher proteolytic resistance, with activity over a broad pH range. Moreover, rHyal_Sk exhibits remarkable substrate specificity for hyaluronic acid (HA) and poses no risk of animal cross-infection.enStreptomyces koganeiensishyaluronic acid or hyaluronanhyaluronidaseBacterial ProteinsEnzyme StabilityHyaluronoglucosaminidaseRecombinant ProteinsStreptomycesresearch article27311405open access10.1002/1873-3468.122581873-3468https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1002/1873-3468.12258