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Improved purification and biochemical characterization of extracellular amylopullulanase fromThermoanaerobacter ethanolicus39E

โœ Scribed by Saroj P. Mathupala; J. Gregory Zeikus


Publisher
Springer
Year
1993
Tongue
English
Weight
841 KB
Volume
39
Category
Article
ISSN
1432-0614

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Purification and biochemical characteriz
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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