Inducible and Constitutive Formation of Fructanase in Batch and Continuous Cultures of Free

Abstract

Summary: The production of extracellular β-D-fructanase by several strains of was studied in continuous culture. When glucose was the limiting nutrient, K1-R and OMZ176 accumulated fructanase to maximum levels at low growth rates (dilution rate 0·05-0·10 h), due to the longer residence times of the bacteria in the culture vessel under these conditions. Extracellular fructanase activity was greater than has been previously reported for batch cultures. The rate of fructanase production for both strains K1-R and OMZ176 increased with increasing growth rate when glucose was limiting. Under conditions of glucose sufficiency, the rate of fructanase production was always lower than in cultures where glucose was limiting, irrespective of the growth rate. Cultures of Ingbritt (serotype ) grown with sorbitol- or glucose-limitation synthesized fructanase at a very low basal rate. When fructose was the limiting carbohydrate the enzyme was induced with a maximum rate of production occurring at a dilution rate of 0·40 h. Strains of from other serotypes () were either not affected by changing the limiting sugar from glucose to fructose or else fructanase activity was slightly decreased in the fructose-limited medium. Fructanases from various strains of readily hydrolysed (2 → 6)-β-D-fructans, but all possessed the ability to hydrolyse (2 → 1)-β-D-fructans to varying degrees.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-131-7-1625
1985-07-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/131/7/mic-131-7-1625.html?itemId=/content/journal/micro/10.1099/00221287-131-7-1625&mimeType=html&fmt=ahah

References

  1. Clarke P. H., Houldsworth M. A., Lilly M. D. 1968; Catabolite repression and the induction of amidase synthesis by Pseudomonas aeruginosa 8602 in continuous culture. Journal of General Microbiology 51:225–234
    [Google Scholar]
  2. Dacosta T., Gibbons R. J. 1968; Hydrolysis of levan by human plaque streptococci. Archives of Oral Biology 13:609–617
    [Google Scholar]
  3. Demain A. L. 1971; Increasing enzyme production by genetic and environmental manipulations. Methods in Enzymology 22:86–95
    [Google Scholar]
  4. Dygert S., Florida L. H. L. D., Thoma J. A. 1965; Determination of reducing sugar with improved precision. Analytical Biochemistry 13:367–374
    [Google Scholar]
  5. Ebisu S., Kato K., Kotani S., Misaki A. 1975; Structural differences in fructans elaborated by Streptococcus mutans and Streptococcus salivarius . Journal of Biochemistry 78:879–887
    [Google Scholar]
  6. Geddes D. A. M. 1975; Acids produced by human dental plaque metabolism in situ . Caries Research 9:98–109
    [Google Scholar]
  7. Grootwassink J. W. D., Fleming S. E. 1980; Non-specific β-fructofuranosidase (inulase) from Kluyveromyces fragilis: batch and continuous fermentation, simple recovery method and some industrial properties. Enzyme and Microbial Technology 2:45–53
    [Google Scholar]
  8. Grootwassink J. W. D., Hewitt G. M. 1983; Inducible and constitutive formation of β-fructofuranosidase (inulase) in batch and continuous cultures of the yeast Kluyveromyces fragilis . Journal of General Microbiology 129:31–41
    [Google Scholar]
  9. Hamelik R. M., McCabe M. M. 1982; An endodextranase inhibitor from batch cultures of Streptococcus mitis . Biochemical and Biophysical Research Communications 106:875–880
    [Google Scholar]
  10. van Houte J., Jansen H. M. 1968; Levan degradation by streptococci isolated from human dental plaque. Archives of Oral Biology 13:827–830
    [Google Scholar]
  11. Kaushik K. R., Gondo S., Venkatasubramanian K. 1979; Modeling of inducible enzyme biosynthesis in microbial cells. Annals of the New York Academy of Sciences 326:57–72
    [Google Scholar]
  12. Kawai G., Taniguchi H., Nakamura M. 1973; Polyfructan and oligofructans synthesized from sucrose by Conidia of Aspergillus sydowi IAM 2544. Agricultural and Biological Chemistry 37:2111–2119
    [Google Scholar]
  13. Koplove H. M., Cooney C. L. 1979; Enzyme production during transient growth. Advances in Biochemical Engineering 12:1–40
    [Google Scholar]
  14. Lilley G., Rowley B. I., Bull A. T. 1974; Exocellular β-l,3-glucanase synthesis by continuous-flow cultures of a thermophilic streptomycete. Journal of Applied Chemistry and Biotechnology 24:677–686
    [Google Scholar]
  15. Magasanik B. 1961; Catabolite repression. Cold Spring Harbor Symposia on Quantitative Biology 26:249–256
    [Google Scholar]
  16. Marshall K., Weigel H. 1980; Extracellular β-d-fructofuranosidase elaborated by Streptococcus salivarius strain 51: preparation and mode of action on a levan and on homologues of inulobiose. Carbohydrate Research 83:315–320
    [Google Scholar]
  17. McFall E., Mandelstam J. 1963; Specific metabolic repression of three induced enzymes in Escherichia coli . Biochemical Journal 89:391–398
    [Google Scholar]
  18. Reese E. T. 1972; Enzyme production from insoluble substrates. Biotechnology and Bioengineering Symposium 3:43–62
    [Google Scholar]
  19. Takahashi N., Mizuno F., Takamore K. 1983; Isolation and properties of levanase from Streptococcus salivarius KTA-19. Infection and Immunity 42:231–236
    [Google Scholar]
  20. Toda K. 1976a; Invertase biosynthesis by Saccharomyces carlsbergensis in batch and continuous cultures. Biotechnology and Bioengineering 18:1103–1115
    [Google Scholar]
  21. Toda K. 1976b; Dual control of invertase biosynthesis in chemostat culture. Biotechnology & Bioengineering 18:1117–1124
    [Google Scholar]
  22. Walker G. J., Hare M. D., Morrey-Jones J. G. 1982; Effect of variation in growth conditions on endo-dextranase production by Streptococcus mutans . Carbohydrate Research 107:111–122
    [Google Scholar]
  23. Walker G. J., Hare M. D., Morrey-Jones J. G. 1983; Activity of fructanase in batch cultures of oral streptococci. Carbohydrate Research 113:101–112
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-131-7-1625
Loading
/content/journal/micro/10.1099/00221287-131-7-1625
Loading

Data & Media loading...

Most cited Most Cited RSS feed