<abstract xmlns="http://www.w3.org/1999/xhtml">

Proteases derived from <italic>Streptomyces</italic> demonstrate numerous commendable properties, rendering it extensively applicable in biotechnology and various industrial sectors. This study focused on the purification and characterization of the thermostable protease obtained from <italic>Streptomyces</italic> sp. CNXK100. The purified protease exhibited an estimated molecular weight of 27 kDa, with optimal activity at 75°C and pH 8.0. Notably, the enzyme remained active even without any metal ions and fully active in the presence of Na+, K+, Mg2+, and Cu2+metal ions. The kinetic parameters were determined with a <italic>KM</italic> value of 3.13 mg/ml and a <italic>Vmax</italic> value of 3.28 × 106 U/mg. Furthermore, the protease has demonstrated notable stability when subjected to a treatment temperature of up to 65°C for 60 minutes, and across a broad pH range extending from 5.0 to 10.0. This protease also demonstrated resilience against a spectrum of harsh conditions, including exposure to organic solvents, surfactants, bleaching agents, and proteolytic enzymes. Additionally, the enzyme maintained its activity following treatment with commercial detergents, accomplishing complete thrombus lysis at a concentration of 2.50 mg/ml within 4 hours. Remarkably, the protease exhibited stability in terms of activity and protein concentration for 70 days at 4°C. These findings underscore the potential industrial applications of the thermostable protease from <italic>Streptomyces</italic> sp. CNXK100.
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</abstract>

Proteases derived from Streptomyces demonstrate numerous commendable properties, rendering it extensively applicable in biotechnology and various industrial sectors. This study focused on the purification and characterization of the thermostable protease obtained from Streptomyces sp. CNXK100. The purified protease exhibited an estimated molecular weight of 27 kDa, with optimal activity at 75°C and pH 8.0. Notably, the enzyme remained active even without any metal ions and fully active in the presence of Na+, K+, Mg2+, and Cu2+metal ions. The kinetic parameters were determined with a KM value of 3.13 mg/ml and a Vmax value of 3.28 × 106 U/mg. Furthermore, the protease has demonstrated notable stability when subjected to a treatment temperature of up to 65°C for 60 minutes, and across a broad pH range extending from 5.0 to 10.0. This protease also demonstrated resilience against a spectrum of harsh conditions, including exposure to organic solvents, surfactants, bleaching agents, and proteolytic enzymes. Additionally, the enzyme maintained its activity following treatment with commercial detergents, accomplishing complete thrombus lysis at a concentration of 2.50 mg/ml within 4 hours. Remarkably, the protease exhibited stability in terms of activity and protein concentration for 70 days at 4°C. These findings underscore the potential industrial applications of the thermostable protease from Streptomyces sp. CNXK100.

Purification and Characterization of a Small Thermostable Protease from <italic>Streptomyces</italic> sp. CNXK100

Polish Journal of Microbiology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Purification and Characterization of a Small Thermostable Protease from  sp. CNXK100

Proteases derived from Streptomyces demonstrate numerous commendable properties, rendering it extensively applicable in biotechnology and various industrial...

Purification and Characterization of a Small Thermostable Protease from Streptomyces sp. CNXK100

Article Category: Original Paper

Publicado en línea: 28 abr 2024

Páginas: 155 - 165

Recibido: 16 dic 2023

Aceptado: 13 mar 2024

DOI: https://doi.org/10.33073/pjm-2024-014

Palabras clave
characterization, purification, thermostable protease

© 2024 Tan Viet Pham et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Purification and Characterization of a Small Thermostable Protease from Streptomyces sp. CNXK100

Article Category: Original Paper

Publicado en línea: 28 abr 2024

Páginas: 155 - 165

Recibido: 16 dic 2023

Aceptado: 13 mar 2024

DOI: https://doi.org/10.33073/pjm-2024-014

Palabras clavecharacterization, purification, thermostable protease

© 2024 Tan Viet Pham et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Palabras clave
characterization, purification, thermostable protease