Abstract
A soluble, NADP+-dependent alcohol dehydrogenase (ADH) with a pH optimum at 8.7 was found in A. calcoaceticus EB 104 after growth on different carbon sources. n-Alkanols with short and medium chain length were employed as test substrates. The Km values decreased with increasing chain length. The Vmax values remained nearly unchanged. The activities determined were independent of the carbon source. Furthermore, a n-alkanol-dependent reduction of DCPIP was measured in membrane fractions of cells grown on different carbon sources. The optimum pH for this reaction was at 7.5. Further proof for the presence of a pyridine nucleotide-independent ADH was derived from the oxidation of 14C-decanol in the absence of NADP+ or NAD+.
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