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Updated: May 1, 2026

GST-His purification: A Two-step Affinity Purification Protocol Yielding Full-length Purified Proteins
Published on: October 29, 2013
Secretory expression in Bacillus subtilis, purification, and characterization of a persistent protein-degrading
Aoto Takano1, Mamiko Yano1, Tomoka Nakamura2
1Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan.
Abstract:
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.

