IMIS

Publications | Institutes | Persons | Datasets | Projects | Maps
[ report an error in this record ]basket (0): add | show Print this page

A highly active alkaline phosphatase from the marine bacterium Cobetia
Plisova, E.Y.; Balabanova, L.A.; Ivanova, E.P.; Kozhemyako, V.B.; Mikhailov, V.V.; Agafonova, E.V.; Rasskazov, V.A. (2005). A highly active alkaline phosphatase from the marine bacterium Cobetia. Mar. Biotechnol. 7(3): 173-178. https://dx.doi.org/10.1007/s10126-004-3022-4
In: Marine Biotechnology. Springer-Verlag: New York. ISSN 1436-2228; e-ISSN 1436-2236, more
Peer reviewed article  

Available in  Authors 

Keywords
    Alkaline phosphatase
    Chemical compounds > Alkaline earth metal compounds
    Microorganisms > Bacteria
    Processing > Purification
    Properties
    Proteins > Enzymes > Hydrolases > Esterases > Phosphoric monoester hydrolases > Alkaline phosphatase
    Purification
    Purification
    Specificity
    Cobetia marina Cobet, A.B., Wirsen, C. & Jones, 1970 [WoRMS]
    Marine/Coastal

Authors  Top 
  • Plisova, E.Y.
  • Balabanova, L.A.
  • Ivanova, E.P.
  • Kozhemyako, V.B.
  • Mikhailov, V.V.
  • Agafonova, E.V.
  • Rasskazov, V.A.

Abstract
    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).

All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy Top | Authors