Purification and Characterization of Two Aldehyde Dehydrogenases from Pseudomonas aeruginosa

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Abstract
Two soluble aldehyde dehydrogenases isoenzymes were purified and separated from extracts of a paraffin-assimilating bacterium, P. aeruginosa. The 1st one, obtained at an estimated purity of 20% (specific activity with butanal 0.33 kat/kg) was NAD-dependent. It was rapidly inactivated at pH 8.6 but was efficiently protected by NAD. It had a MW of 225,000 and presented a high affinity for aldehydes of short and middle chain lengths. The 2nd enzyme, obtained in a nearly homogeneous state (specific activity with pentanal 0.62 kat/kg) was NADP-dependent. It was activated by ions, in particular K+, and had a good affinity for aldehydes of higher chain lengths. Both enzymes were stabilized by thiols and glycerol and were inactivated by reagents of SH groups. These enzymes are constitutive and their physiological function is uncertain. When the bacteria were grown on n-paraffin a new membrane-bound NAD-dependent aldehyde dehydrogenase activity was produced.

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