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Molecular and biochemical characterization of an extracellular serine-protease fromVibrio metschnikoviiJ1

โœ Scribed by Kemel Jellouli; Ali Bougatef; Laila Manni; Rym Agrebi; Rayda Siala; Islem Younes; Moncef Nasri

Publisher
Springer-Verlag
Year
2009
Tongue
English
Weight
636 KB
Volume
36
Category
Article
ISSN
1476-5535

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A serine protease was purified from Natronococcus occultus stationary phase culture medium (328-fold, yield 19%) and characterized at the biochemical level. The enzyme has a native molecular mass of 130 kDa, has chymotrypsin-like activity, is stable and active in a broad pH range (5.5 -12), is rathe