Secretory expression in <i>Bacillus subtilis</i>, purification, and characterization of a persistent protein-degrading enzyme from <i>Nocardiopsis</i> sp. TOA-1
Keratinase from Nocardiopsis sp. TOA-1 (NAPase) holds significant potential for industrial and medical applications. Here, we developed a heterologous secretory expression system for NAPase in Bacillus subtilis. The recombinant enzyme exhibited catalytic properties comparable to the native enzyme, demonstrating its suitability for further protein engineering. This work provides a foundation for enhancing NAPase activity and stability, expediting its biotechnological applications.
Authors
- Tomoka Nakamura (ORCID: https://orcid.org/0000-0002-2623-2075)
- S. Tanaka (ORCID: https://orcid.org/0000-0003-4270-0374)
- Kazufumi Takano (ORCID: https://orcid.org/0000-0002-7548-7314)
- Akira Takano
- M Yano
Institutions
- Ritsumeikan University (JP)
- Kyoto Prefectural University (JP)
- Kyoto Prefectural University of Medicine (JP)
Publication Details
- Journal
- Bioscience Biotechnology and Biochemistry
- Published
- 2024-12-10
- DOI
- https://doi.org/10.1093/bbb/zbae191
- Primary Topic
- Enzyme Production and Characterization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Japan Society for the Promotion of Science