Abstract
1. 1. Washed suspensions of Bifidobacterium bifidum ferment glucose to approx. 1.5 moles of acetate and 1 mole of lactate. Xylose yields 1 mole of acetate and 1 mole of lactate. 2. 2. Aldolase (EC 4.1.2.7) and glucsoe-6-phosphate dehydrogenase (EC 1.1.1.49) are absent from cell-free extracts of B. bifidum. 3. 3. An enzyme catalysing the conversion of fructose 6-phosphate into acetylphosphate and erythrose 4-phosphate is shown to be present in cell-free extracts: d-fructose-g-phosphate d-erythrose-4-phosphate-lyase (phosphate-acetylating). The trivial name fructose-6-phosphate phosphoketolase may be given. 4. 4. By the action of transaldolase (EC 2.2.1.2.) and transketolase (EC 2.2.1.1) pentose phosphates are formed from fructose 6-phosphate and erythrose 4-phosphate. 5. 5. Pentose phosphates are split by xylulose-5-phosphate phosphoketolase (EC 4.1.2.9) into acetylphosphate and glyceraldehyde 3-phosphate. 6. 6. Lactate dehydrogenase (EC 1.1.1.27) is shown to have an absolute requirement for fructose 1,6-diphosphate. This explains the presence of low amounts of phosphofructokinase (EC 2.7.1.11) in cell-free extracts. 7. 7. The theoretical fermentation balances of glucose and xylose agree with those found experimentally. 8. 8. The results strengthen the previous suggestions that the classification of B. bifidum in the genus Lactobacillus is not justified.
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