Purification and characterization of a thermodynamic stable serine protease from Aspergillus fumigatus

A thermostable extracellular serine protease from Aspergillus fumigatus was purified 8.8-fold using a 4-step protocol. The enzyme was produced using a 36h solid-state culture, had a molecular weight of 88kDa and exhibited maximal enzyme activity at pH 7 and 60°C. Structural analysis revealed that th...

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Bibliographic Details
Published in:Process biochemistry (1991) 2011-10, Vol.46 (10), p.2001-2006
Main Authors: Hernández-Martínez, R., Gutiérrez-Sánchez, G., Bergmann, C.W., Loera-Corral, O., Rojo-Domínguez, A., Huerta-Ochoa, S., Regalado-González, C., Prado-Barragán, L.A.
Format: Article
Language:English
Subjects:
activation energy
Aspergillus fumigatus
denaturation
enthalpy
entropy
enzyme activity
half life
heat inactivation
molecular weight
Serine protease
serine proteinases
solid state culture
thermal stability
Thermodynamics
Thermostability
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Summary:A thermostable extracellular serine protease from Aspergillus fumigatus was purified 8.8-fold using a 4-step protocol. The enzyme was produced using a 36h solid-state culture, had a molecular weight of 88kDa and exhibited maximal enzyme activity at pH 7 and 60°C. Structural analysis revealed that the protease is monomeric and non-glycosylated. Thermal inactivation of the pure enzyme followed first-order kinetics. The half-life (t1/2) of the pure enzyme at 50, 60 and 70°C was 65, 34 and 14min, respectively. The denaturation and activation energies were 69 and 62kJmol−1, respectively. Thermodynamic parameters (entropy and enthalpy) suggested that the protease was highly thermostable. This is the first report on the thermodynamic parameters of proteases produced by A. fumigatus.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2011.07.013