Purification and properties of dihydroxyacetone reductase and 2,3‐butanediol dehydrogenase from <i>Candida utilis</i> CBS 621

Verduyn, Cornelis; Breedveld, Guido J.; Scheffers, W. A.; Dijken, Johannes P. van

doi:10.1002/yea.320040206

Cited by 16 publications

(7 citation statements)

References 7 publications

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“…Dihydroxyacetone reductase is known in the literature as glycerol dehydrogenase (EC l. l. l .6). We prefer the former term since various yeasts, among others Candida utilis, contain an enzyme which is capable of reducing dihydroxyacetone, but is inactive with glycerol (Verduyn et al, 1988). The enzyme from H .…”

Section: Discussionmentioning

confidence: 99%

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

Verduyn¹,

Breedveld²,

Schreuder³

et al. 1988

Yeast

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Nunsmulu poljworpha CBS 4732 grown on a variety of substrates contained very high activities of enzymes catalyzing the NADH-linked reduction of dihydroxyacetone, acetoin, diacetyl, acetol, methylglyoxal and acetone. The enzymes catalyzing these reductions have been purified and their kinetic properties are described. Three different enzymes were found responsible for the above-mentioned activities, namely: (1) dihydroxyacetone reductase; (2) acetone reductase; and (3) alcohol dehydrogenase.So far, the physiological function of dihydroxyacetone reductase and acetone reductase is obscure. The kinetic properties of dihydroxyacetone reductase and the regulation of the synthesis of this enzyme suggest that it does not function as a glycerol dehydrogenase.

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Section: Discussionmentioning

confidence: 99%

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

Verduyn¹,

Breedveld²,

Schreuder³

et al. 1988

Yeast

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“…Butyrate and 2,3-butanediol metabolism have not been studied extensively in yeasts. It has been assumed that butyrate is assimilated via acetyl CoA, without a net loss of CO 2 , 2,3-Butanediol is first converted into acetoin by an NAD+-dependent butanediol dehydrogenase (Verduyn et al 1988b). The next steps are not known, but since cells grown on butanediol have a high isocitrate lyase activity (Verduyn et al 1988c), it is likely that acetate is an intermediate.…”

Section: Weak Acidsmentioning

confidence: 99%

Physiology of yeasts in relation to biomass yields

Verduyn¹

1992

Quantitative Aspects of Growth and Metabolism of Microorganisms

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The stoichiometric limit to the biomass yield (maximal assimilation of the carbon source) is determined by the amount of CO 2 lost in anabolism and the amount of carbon source required for generation of NADPH. This stoichiometric limit may be reached when yeasts utilize formate as an additional energy source. Factors affecting the biomass yield on single substrates are discussed under the following headings: -Energy requirement for biomass formation (YATP)' YATP depends strongly on the nature of the carbon source. Cell composition. The macroscopic composition of the biomass, and in particular the protein content, has a considerable effect on the ATP requirement for biomass formation. Hence, determination of for instance the protein content of biomass is relevant in studies on bioenergetics. Transport of the carbon source. Active (i.e. energy-requiring) transport, which occurs for a number of sugars and polyols, may contribute significantly to the calculated theoretical ATP requirement for biomass formation. Pia-ratio. The efficiency of mitochondrial energy generation has a strong effect on the cell yield. The Pia-ratio is determined to a major extent by the number of proton-translocating sites in the mitochondrial respiratory chain. Maintenance and environmental factors. Factors such as osmotic stress, heavy metals, oxygen and carbon dioxide pressures, temperature and pH affect the yield of yeasts. Various mechanisms may be involved, often affecting the maintenance energy requirement. Metabolites such as ethanol and weak acids. Ethanol increases the permeability ofthe plasma membrane, whereas weak acids can act as proton conductors. Energy content of the growth substrate. It has often been attempted in the literature to predict the biomass yield by correlating the energy content of the carbon source (represented by the degree of reduction) to the biomass yield or the percentage assimilation of the carbon source. An analysis of biomass yields of Candida uti/is on a large number of carbon sources indicates that the biomass yield is mainly determined by the biochemical pathways leading to biomass formation, rather than by the energy content of the substrate.

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“…Thus the former enzymes seem to be more suitable for enzymic alcohol assays. In this respect it is worth mentioning that the activities of ADH in 2,3-butanediol-grown C. utilis (Verduyn et al, 1988b) are exceptionally high. Furthermore, the enzyme from this source is much more stable than the classical ADH from baker's yeast.…”

Section: Resultsmentioning

confidence: 93%

Substrate specificity of alcohol dehydrogenase from the yeast Hansenyls polymorpha CBS 4732 and Candida utilis CBS 621

Verduyn

Breedveld

Scheffers

et al. 1988

Yeast

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The substrate specificity of alcohol dehydrogenase (ADH) from Hansenula polymorpha and Candidu utilis has been compared with that of the classical ADH from baker's yeast. Cell-free extracts of H. polymorpha and C. utiiis exhibited a much higher ratio of butanol to ethanol oxidation than baker's yeast ADH. This was also observed with the purified enzymes. The ratio ofactivities with ethanol and butanol was pH-dependent. With the baker's yeast enzyme the activity strongly decreased with increasing chain length, whereas the enzymes from H. polymorpha and C. utilis showed a high reactivity with long-chain alcohols. In addition, the affinity constant for ethanol was more than tenfold lower than that of the baker's yeast enzyme. The purified preparations yielded several protein bands on polyacrylamide slab gels, each of which showed activity with both ethanol and butanol.KEY WORD -Alcohol dehydrogenase.

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Purification and properties of dihydroxyacetone reductase and 2,3‐butanediol dehydrogenase from Candida utilis CBS 621

Cited by 16 publications

References 7 publications

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

Properties of enzymes which reduce dihydroxyacetone and related compounds in hansenula polymorpha CBS 4732

Physiology of yeasts in relation to biomass yields

Substrate specificity of alcohol dehydrogenase from the yeast Hansenyls polymorpha CBS 4732 and Candida utilis CBS 621

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