Alcohol dehydrogenases AdhE and AdhB with broad substrate ranges are important enzymes for organic acid reduction in Thermoanaerobacter sp. strain X514

Table 3 Substrate-dependent specific activities of purified AdhE and AdhB of Thermoanaerobacter sp. strain X514

Activities were determined in 50 mM Tris buffer (pH 7.5) supplemented with 2 mM DTE and 4 µM resazurin. Alcohol (200–500 mM) or aldehyde (10–50 mM) oxidation was determined with NAD(P)⁺ (2 mM) as electron acceptor, in the presence or absence of coenzyme A (0.2 mM; AdhE). Aldehyde or ketone (10 mM) reduction to alcohols was determined with NAD(P)H (0.5 mM) as electron donor; and absorption at 340 nm was measured. For details, please see “Methods” section. One unit (U) refers to one µmol of NADP⁺ reduced or NAD(P)H oxidized per minute. n. d.: not determined
^*Please note that CoA-dependent alcohol oxidation requires the reduction of 2 mol of NAD(P)⁺

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