Abstract
The phosphate-irrepressible alkaline phosphatase of the ethanol-producing bacterium Zymomonas mobilis was solubilized from membranes by the cationic detergent N-cetyl-N,N,N-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 Z. mobilis cells (ZAPase), remained active in the presence of an ethanol concentration as high as 100 g l−1. However, in vitro, the stability of the purified ZAPase was severely affected at low ethanol concentration (7·8 g l−1), showing the importance of the membrane environment in vivo. ZAPase differed from other bacterial alkaline phosphatases by having a higher affinity for the substrate 4-nitrophenylphosphate, a higher K i for phosphate, only a partial reactivation by Zn2+ after EDTA inhibition, and a higher specific activity.
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