A highly active alkaline phosphatase from the marine bacterium cobetia

An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg o...

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Bibliographic Details
Published in:Marine biotechnology (New York, N.Y.) N.Y.), 2005-05, Vol.7 (3), p.173-178
Main Authors: Yu Plisova, E, Balabanova, L A, Ivanova, E P, Kozhemyako, V B, Mikhailov, V V, Agafonova, E V, Rasskazov, V A
Format: Article
Language:English
Subjects:
5'-Nucleotidase - isolation & purification
Alkaline Phosphatase - isolation & purification
Animals
Cations
Enzymes
Halomonadaceae - enzymology
Hydrogen-Ion Concentration
Isoelectric Point
Microbiology
Molecular Weight
Mytilidae - microbiology
Pacific Ocean
Phosphatase
Substrate Specificity
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Summary:An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5).
ISSN:1436-2228
1436-2236
DOI:10.1007/s10126-004-3022-4