Effects of detergents and phospholipids on the pyridine nucleotide-independent aldehyde dehydrogenase from membranes of Acetobacter rancens.

The pyridine nucleotide-independent aldehyde dehydrogenase solubilized and purified from membranes of Acetobacter rancens CCM 1774 requires the presence of detergents for activity. While several detergents could stimulate the enzyme activity the stability of the enzyme-detergent complexes was rather low. Phospholipid substitution experiments revealed the reversibility of the loss of activity caused by phospholipid removal. Enzyme-phospholipid complexes generated from a complex phospholipid fraction exhibited an increased stability. The predominant effect of phosphatidylglycerol on both enzyme activity and stability is discussed in terms of essential boundary layer phospholipids.