Folia Microbiologica

, Volume 25, Issue 1, pp 32–39 | Cite as

Inulinase activity ofDebaromyces cantarellii

  • I. Beluche
  • J. P. Guiraud
  • P. Galzy


Debaromyces cantarellii Capriotti contains an inulinase activity which is inducible by growth on inulin but not on other β-fructosides. The induction is inhibited by glucose and fructose. The system is situated in the cell wall and can be best extracted with a 20 mm phosphate buffer at pH 8.5. The inulinase activity shows pH optima at 4 and 6, suggesting the presence of two enzymes, the latter being more tightly bound to the cell wall. Both enzymes degrade inulin from the nonreducin end. The cells also contain a constitutive β-fructofuranosidase with a specificity partly overlapping with that of the inulinase(s).


Fructose Inulin Raffinose Jerusalem Artichoke Inulinase Activity 


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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1980

Authors and Affiliations

  • I. Beluche
    • 1
  • J. P. Guiraud
    • 2
  • P. Galzy
    • 2
  1. 1.Laboratoire de Biochimie AppliquéeSciences et Technologies des Industries AlimentaireMontpellier CedexFrance
  2. 2.Laboratoire de Génétique et MicrobiologieEcole Nationale Supérieure AgronomiqueMontpellier CedexFrance

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