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Novel sialidase from non-pathogenic bacterium Oerskovia paurometabola strain O129

  • Rumyana T. Eneva ORCID logo EMAIL logo , Stephan A. Engibarov , Yana G. Gocheva ORCID logo , Simona L. Mitova and Penka M. Petrova
Published/Copyright: November 10, 2022

Abstract

Bacterial sialidases are enzymes that are involved in a number of vital processes in microorganisms and in their interaction with the host or the environment. Their wide application for scientific and applied purposes requires the search for highly effective and non-pathogenic producers. Here, we report the first description of sialidase from Oerskovia paurometabola. The extracellular enzyme preparation was partially purified. The presence of sialidase was confirmed in native PAGE treated with the fluorogenic substrate 4MU-Neu5Ac. Maximum enzyme activity was registered at 37 °C and in the pH range of 4.0–5.5. The influence of metal ions and EDTA was examined. It was demonstrated that EDTA, Mn2+ and Ba2+ ions inhibit the sialidase activity to different extent, while Cd2+, Fe2+ and Fe3+ have stimulating effect on it. These features are studied for the first time concerning sialidase of Oerskovia representative. Cell bound sialidase and sialate aldolase were also established.


Corresponding author: Rumyana T. Eneva, The Stephan Angeloff Institute of Microbiology, 1113 Sofia, Bulgaria, E-mail:

  1. Author contribution: All authors contributed to the study conception and design. All authors read and approved the final manuscript.

  2. Research funding: No funding was received for conducting this study.

  3. Conflict of interest statement: The authors declare that they have no conflict of interests.

  4. Compliance with ethical standards: This article does not contain any studies involving animal or human participants performed by any of the authors.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/znc-2022-0051).


Received: 2022-03-10
Revised: 2022-06-14
Accepted: 2022-10-20
Published Online: 2022-11-10
Published in Print: 2023-01-27

© 2022 Walter de Gruyter GmbH, Berlin/Boston

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