Two steps purification, biochemical characterization, thermodynamics and structure elucidation of thermostable alkaline serine protease from Nocardiopsis alba strain OM-5

The Nocardiopsis alba strain OM-5 showed maximum protease production in submerged culture. The OM-5 protease was purified by hydrophobic interaction chromatography. The purified protease of 68 kDa showed maximum activity (3312 ± 1.64 U/mL) at 70 °C and was quite stable at 80 °C up to 4 M NaCl (w/v)...

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Veröffentlicht in:	International journal of biological macromolecules 2021-02, Vol.169, p.39-50
Hauptverfasser:	Chauhan, Jagruti V., Mathukiya, Riddhi P., Singh, Satya P., Gohel, Sangeeta D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinobacteria - chemistry Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Circular dichroism spectroscopy Detergents Endopeptidases - chemistry Endopeptidases - isolation & purification Enzyme Stability - physiology Hydrogen-Ion Concentration Kinetics Nocardiopsis - enzymology Nocardiopsis - metabolism Salt-tolerant Actinomycetes Serine - chemistry Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Proteases - isolation & purification Submerged cultivation Surface-Active Agents Temperature Thermodynamics Thermostable protease
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