LACTATE AND GLUCOSE OXIDATION SYSTEMS IN ACETOBACTER SUBOXYDANS |
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Authors: | IWASAKI YASUKO |
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Institution: | Biological Institute, Faculty of Science, Nagoya University Nagoya |
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Abstract: | - From a strain of Acetobacter suboxydans, a glucose and a lacticenzyme were obtained in cell-free states. The lactic enzymeshows as strong activity as the glucose enzyme but is more stablethan the latter toward various purification procedures: bothare sensitive to high temperature treatment. Activities of thetwo enzymes and the MICHAELIS constants of the glucose enzymewere determined under both aerobic and anaerobic conditions.
- Carbon monoxide inhibits the oxygen-uptake in both glucoseandlactate oxidation. WARBURG's distribution constant for lactateoxidation is 6.7. These results suggest the participation ofan heme enzyme in the oxidation system.
- Effects of copperreagents, narcotics and PCMB were also examined.
- The dehydrogenaseactivities (reduction of dye) of the enzymesare more sensitiveto high temperature than the correspondingactivities in oxygen-uptake.
- By combining a dehydrogenase preparation which has lost itsoxygen-absorbing activity through acetone treatment, with aheated extract, a partial recovery of oxygen-uptake can be realizedin lactate oxidation.
- L-Cysteine is utilized as hydrogen donorby the bacterium. Thisoxidative reaction, unlike the oxidationof lactate, is notinhibited by surface active reagents.
(Received May 16, 1960; ) |
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