Summary: The phosphate-irrepressible alkaline phosphatase of the ethanol-producing bacterium was solubilized from membranes by the cationic detergent -cetyl--trimethylammonium bromide (CTAB) and purified by fast protein liquid chromatography. The purified enzyme was a monomeric protein of molecular mass 54 kDa, highly resistant to heat and to ionic strength. The alkaline phosphatase of growing cells (ZAPase), remained active in the presence of an ethanol concentration as high as 100 g I. However, , the stability of the purified ZAPase was severely affected at low ethanol concentration (7.8 g I), showing the importance of the membrane environment . ZAPase differed from other bacterial alkaline phosphatases by having a higher affinity for the substrate 4-nitrophenylphosphate, a higher for phosphate, only a partial reactivation by Zn after EDTA inhibition, and a higher specific activity.


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