Archives of Microbiology

, Volume 114, Issue 3, pp 255–259 | Cite as

Multiplicity and control of alcohol dehydrogenase isozymes in various strains of wine yeasts

  • Rajendra Singh
  • Ralph E. Kunkee
Article

Abstract

The control of formation of alcohol dehydrogenase (ADH) (EC 1.1.1.1) isozymes and their activity toward some of the higher alcohols (n-propanol, isobutanol, isopentanol, and active pentanol) was studied in ten different wine yeast strains under various physiological conditions of growth. Multiple forms of ADH were demonstrated by starch gel electrophoresis in all the strains. When grown anaerobically on glucose or under vinification conditions, the cells of most strains had a single isozyme band for ADH I. However, during aerobic growth on glucose or on ethanol, 2 to 4 additional bands were observed for ADH II and ADH III. With the higher alcohols as substrates, only ADH I bands were evident in all strains under anaerobic or vinification conditions. In glucose derepressed and aerobically grown cultures, ADH II and ADH III bands were also found with the higher alcohols as enzyme substrates. The increases in numbers of isozymes in derepressed or aerobic cultures were reflected as increased specific ADH activities in cell-free extracts. The results suggest that multiplicity of ADH isozymes, and their control by glucose repression and aerobic induction, are common phenomena in yeast; and that only one enzyme, ADH I, is involved in the formation of higher alcohols during vinification.

Key words

Alcohol dehydrogenase Isozymes Glucose repression Aerobic induction Wine yeasts 

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References

  1. Barron, E. S. G., Levine, S.: Oxidation of alcohols by yeast alcohol dehydrogenase and by living cells: The thiol group of the enzyme. Arch. Biochem. Biophys. 41, 175–187 (1952)Google Scholar
  2. Ebisuzaki, K., Barron, E. S. G.: Yeast alcohol dehydrogenase II. Arch. Biochem. Biophys. 69, 555–564 (1957)Google Scholar
  3. Fowler, P. W., Ball, A. J. S., Griffiths D. E.: The control of alcohol dehydrogenase isozyme synthesis in Saccharomyces cerevisiae. Can. J. Biochem. 50, 35–42 (1972)Google Scholar
  4. Gornall, A. G., Bardawill, C. J., David, M. M.: Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751–766 (1949)Google Scholar
  5. Heick, H. M. C., Willomot, J., Begin-Heick, N.: The subcellular localization of alcohol dehydrogenase activity in Baker's yeast. Biochim. Biophys. Acta 191, 493–501 (1969)Google Scholar
  6. Kunkee, R. E., Guymon, J. F., Crowell, E. A.: Formation of n-propyl alcohol by cell-free extracts of Saccharomyces cerevisiae. J. Inst. Brew. 72, 530–536 (1966)Google Scholar
  7. Kunkee, R. E., Singh, R.: Dehydrogenase activity for higher alcohols in cell-free extracts of Saccharomyces cerevisiae. J. Inst. Brew. 81, 214–217 (1975)Google Scholar
  8. Lutstorf, U., Megnet, R.: Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae. I. Physiological control of ADH-2 and ADH-4. Arch. Biochem. Biophys. 126, 933–944 (1968)Google Scholar
  9. Racker, E.: Alcohol dehydrogenase from Baker's yeast. In: Methods in enzymology, Vol. 1 (S. P. Colowick, N. O. Kaplan, eds.), pp. 500–503. New York: Academic Press 1955Google Scholar
  10. Rouche, B., Azoulay, E.: Régulation des alcool déshydrogénases chez Saccharomyces cerevisiae. Eur. J. Biochem. 8, 426–434 (1969)Google Scholar
  11. Schimpfessel, L.: Presénce et régulation de la synthése de deux alcool déshydrogénases chez la levure Saccharomyces cerevisiae. Biochim. Biophys. Acta 151, 317–329 (1968)Google Scholar
  12. SentheShanmuganathan, S.: The mechanism of formation of higher alcohols from amino acids by Saccharomyces cerevisiae. Biochem. J. 74, 568–576 (1960)Google Scholar
  13. SentheShanmuganathan, S., Elsden, S. R.: The mechanism of the formation of tyrosol by Saccharomyces cerevisiae. Biochem. J. 69, 210–218 (1958)Google Scholar
  14. Singh, R., Kunkee, R. E.: Alcohol dehydrogenase activities of wine yeasts in relation to higher alcohol formation. Appl. Environ. Microbiol. 32, 666–670 (1976)Google Scholar
  15. Smithies, O.: Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem. J. 61, 629–641 (1955)Google Scholar
  16. Sugar, J., Schimpfessel, L., Rosen, E., Crokaert, R.: The mitochondrial alcohol dehydrogenase of the yeast Saccharomyces cerevisiae. Arch. Int. Physiol. Biochim. 78, 1009–1010 (1970)Google Scholar
  17. Sugar, J., Schimpfessel, L., Rosen, E., Crokaert, R.: Electrophoretic study of the multiple molecular forms of yeast alcohol dehydrogenase. Arch. Int. Physiol. Biochim. 79, 849–850 (1971)Google Scholar
  18. Tatasova, N. A., Latysheva, N. N., Galun, N. I., Gololobov, A. D.: Effect of carbon source on yeast synthesis of alcohol dehydrogenases. Prikl. Biokhim. Mikrobiol 8, 172 (1972)Google Scholar
  19. Tustanoff, E. R., Bartley, W.: Development of respiration in yeast grown anaerobically on different carbon sources. Biochem. J. 91, 595–600 (1964)Google Scholar
  20. Webb, A. D., Ingraham, J. L.: Fusel oil. Adv. Appl. Microbiol. 5, 317–353 (1963)Google Scholar
  21. Wiesenfeld, M., Schimpfessel, L., Crokaert, R.: Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 405, 500–512 (1975)Google Scholar

Copyright information

© Springer-Verlag 1977

Authors and Affiliations

  • Rajendra Singh
    • 1
  • Ralph E. Kunkee
    • 1
  1. 1.Department of Viticulture and EnologyUniversity of CaliforniaDavisUSA

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