Abstract
AbstractThe NADP+‐dependent aldehyde dehydrogenase of Acinetobacter calcoaceticus was inducible by alkanes. It was located in the membranes surrounding the intracellular alkane inclusions. The enzyme could not be solubilized by changing of the pH or the ionic strength but by detergents at concentrations around the critical micelle concentration. High concentrations of detergents inactivated the enzyme; reactivation was possible by addition of natural membrane phospholipids. The enzyme in intact membranes gave lower Km values than the enzyme in the micelle form. The size of the particles of cell envelopes (including the inclusion membranes) and of micelles was controlled by measurements of the wavelength dependence of turbidity. Proteinases were unable to solubilize the enzyme; in the presence of detergent they inactivated it irreversibly. Phospholipase A2 and D inactivated the enzyme reversibly.
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