ABSTRACT
Unlike NAD- and NADP-dependent aldehyde dehydrogenases, quinoprotein aldehyde dehydrogenases catalyze aldehyde oxidation in the presence of artificial dyes in vitro. Several quinoprotein aldehyde dehydrogenases have been reported with properties that vary according to the source of the enzyme. Hommel and Kleber have reported the purification of a quinoprotein aldehyde dehydrogenase from the membrane fraction of Acetobacter rancens CCM 1774. Quinoprotein aldehyde dehydrogenases, which are located in the soluble fraction of cells, can be divided into two species. The potential applicability of quinoprotein aldehyde dehydrogenases in diagnostic tests has been indicated. On the other hand, the applicability of the membrane-bound quinoprotein aldehyde dehydrogenase for these purposes has been reported. With the use of the heat-treated membrane, the instability of solubilized and purified quinoprotein aldehyde dehydrogenase can be overcome, and an ideal aldehyde determination has become possible. Another interesting application of the quinoprotein aldehyde dehydrogenase of acetic acid bacteria relates to the enzymatic or microbial production of sorbic acid from sorbaldehyde.
