By Allen I. Laskin (Eds.)
Meant for researchers in utilized microbiology and environmental engineers, this booklet covers such issues as environmental review of biotechnological methods and microbial differences of haloaromatic and haloaliphatic compounds.
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Extra info for Advances in Applied Microbiology, Vol. 31
5 and is CoA and NADH dependent (legend, Fig. 10). In contrast, the butanol dehydrogenase is an NADPH-dependent enzyme in both C . acetobutylicurn and C. beijerinckii (Rogers and Hansen, 1983; George and Chen, 1983). Both enzymes require added sulfhydryl reagents to demonstrate activity. Extracts from solvent-producing cells show a 70- to 90-fold higher specific activity of both of these enzymes than acid-producing cells (Rogers and Hansen, 1983). Figure 10 shows that the increase in butyraldehyde dehydrogenase activity occurs in batch culture just prior to butanol production and then decays rapidly when cells cease biomass increase.
8 consists of hydrogenase and the NADH: and NADPH:ferredoxin oxidoreductases. It was shown by Petitdemange et al. (1976)that extracts ofC. acetobutylicum contain a NADH:ferredoxin oxidoreductase that both oxidizes NADH and reduces NAD, the former reaction being strongly activated by acetyl-CoA and the latter reaction being inhibited by NADH very much like the situation in C. , 1973). The NADPH: ferredoxin oxidoreductase apparently works only to produce NADPH for biosynthesis. As shown in Fig. 8, there is a high net flow ofelectrons from both NADH and pyruvate through ferredoxin to molecular hydrogen during acid- 32 PALMER ROGERS ogenesis, whereas during solvent formation extra electrons flow into the NADH pool to the more reduced end products such as butanol and ethanol.
1983). The specific activity of this enzyme increases 10-fold in solvent-producing cells. The acetoacetate is decarboxylated by acetoacetate decarboxylase to form acetone. This enzyme was studied and purified earlier from C. acetobutylicum (Davies, 1943; Westheimer, 1969), and recently it was found that the specific activity rises about 40-fold in solvent-producing cells of C . As shown in Fig. 8, this process may allow conservation of the CoA thioester during acetone synthesis and account for the recycling of accumulated acetate and butyrate to form solvents in batch cultures during the solvent-producing phase.
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