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Characterization of a new, recombinant thermo-active subtilisin-like serine protease derived from Shewanella arctica

Journal of Molecular Catalysis B: Enzymatic(2015)

Cited 14|Views3
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Abstract
•The hydrolase enzyme family proteases comprise the commercially most important activities with application in the food/feed, cosmetics, pharmaceutical and fine chemical sector.•We have identified and characterized a new, subtilisin-like serine protease from the psychrotophic eubacterium Shewanella arctica.•The recombinant enzyme is active over a very broad temperature (T: 0–80°C) and pH (pH 6–10) range, with optimal proteolytic activity at 60°C and pH 8 respectively.•The enzyme exhibits an extremely long half-life of 45h and 1.5h at 40°C and 70°C, respectively.•The enzyme tolerates the presence of several metal ions and detergents without affecting activity.
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Key words
Protease,Serine-like,Characterization,Industrial,Shewanella arctica
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