Thermostable alkaline halophilic-protease production by Natronolimnobius innermongolicus WN18.
This study reports the production and biochemical characterisation of a thermostable alkaline halophilic protease from Natronolimnobius innermongolicus WN18 (HQ658997), isolated from soda Lake of Wadi An-Natrun, Egypt. The enzyme was concentrated by spinning through a centriplus, centrifugal ultrafiltration Millipore membrane with a total yield of 25%. The relative molecular mass of this protease determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis ranged from 67 to 43 kDa. The extracellular protease of N. innermongolicus WN18 was dependent on high salt concentrations for activity and stability, and it had an optimum temperature of 60°C in the presence of 2.5 M NaCl. This enzyme was stable in a broad pH range (6-12) with an optimum pH of 9-10 for azocasein hydrolysis. This extracellular protease, therefore, could be defined as thermostable and haloalkaliphilic with distinct properties that make the enzyme applicable for different industrial purposes.
a Department of Clinical Laboratory Science , College of Applied Medical Science, Aljouf University , Al Jouf , Saudi Arabia.
Samy
S
Selim
Nashwa
N
Hagagy
Mohamed
M
Abdel Aziz
El Syaed
el S
El-Meleigy
Enrica
E
Pessione
D001105:Archaea / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004534:Egypt; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D060106:Lakes; D008970:Molecular Weight; D012965:Sodium Chloride; D013696:Temperature
D001426:Bacterial Proteins; D012965:Sodium Chloride; D010450:Endopeptidases; C087822:alkaline protease
Archaea; Natronolimnobius innermongolicus WN18; extremozymes; haloalkaliphile; protease