Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.
- 1 July 1980
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 26 (7) , 833-838
- https://doi.org/10.1139/m80-143
Abstract
Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The MW of the enzyme was estimated to be 100,000. The enzyme had maximal activity at pH 11.5. the enzyme was completely inhibited by 1 mM EDTA. Divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl- > Br- > NO3- > CIO4- > SCN-. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa [kilopascal]), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.Keywords
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