Skip to main content
Log in

Amylase activity ofTorulopsis ingeniosa Di Menna

  • Published:
Folia Microbiologica Aims and scope Submit manuscript

Abstract

Torulopsis ingeniosaDi Menna was found to possess an α-amylase strongly attached to the cell wall, its pH optimum being at 5.5, optimum temperature at 50 °C, highly sensitive to thermal inactivation. The enzyme was found to be induced by starch but the synthesis is not subject to a glucose effect.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Bernfeld P.: Amylases α and β.Methods in Enzymology, Vol. 1, p. 149 (eiS. P. Colowick, N. O. Kaplan, Eds.). Academic Press, New York 1955.

    Chapter  Google Scholar 

  • Bergmeyeb H. U., Bernt E., Schmid F., Stork N.:d-Glucose determination with hexokinase and gluoose-6-phosphate deshydrogenase.Methods of Enzymatic Analysis, Vol. 3, p. 1196 (H. U. Bergmeyer, Ed.). Academic Press, London 1974.

    Google Scholar 

  • Darling S., Theillade J., Birch A.: Kinetic and morphological observations onSaccharomyces cerevisiae during spheroplast formation.J. Bacteriol. 98, 797 (1969).

    PubMed  CAS  Google Scholar 

  • Ebertová H.: Study of the formation and properties of the amylolytic system ofCandida japonica.Folia Microbiol.8, 333 (1963).

    Article  Google Scholar 

  • Ebertová H.: Amylolytic enzymes ofEndomycopsis capsularis. I. Formation of the amylolytic system in cultures ofEndomycopsis capsularis.Folia Microbiol.11, 14 (1966a).

    Article  Google Scholar 

  • Ebebtová H.: Amylolytic enzymes ofEndomycopsis capsularis. II. A study of the properties of isolated α-amylase, amyloglucosidase and maltase transglucosidase.Folia Microbiol.11, 422 (1966b).

    Article  Google Scholar 

  • Hattori Y.: Studies on amylolytic enzymes produced byEndomyces sp. Part I. Production of extra cellular amylase byEndomyces sp.Agr. Biol. Chem. 25, 737 (1961a).

    CAS  Google Scholar 

  • Hattori Y., Takeuchi I.: Studies on amylolytic enzymes produced byEndomyces sp. Part II. Purification and general properties of amyloglucosidase.Agr. Biol. Chem. 25, 895 (1961b).

    CAS  Google Scholar 

  • Hattori Y., Takeuchi I.: Studies on amylolytic enzymes produced byEndomyces sp. Part III. Hydrolysis of starch and glucosyl saccharides with amyloglucosidase.Agr. Biol. Chem. 26, 316 (1962).

    CAS  Google Scholar 

  • Lowry O. H., Rosenbrough A., Farr A. L., Randall R. J.: Protein measurement with the folin phenol reagent.J. Biol. Chem. 193, 265 (1951).

    PubMed  CAS  Google Scholar 

  • Moulin G.: Etude de l’activité de quelques levures. Thèse U. S. T. L., Montpellier 1977.

  • Moulin G., Galzy P.: Etude de l’α-amylase de la paroi dePichia burtonii BOidin.Z. Allg. Mikrobiol. 18, 269 (1978).

    Article  PubMed  CAS  Google Scholar 

  • Sawai T.: An amylase ofCandida tropicalis var.japonica. I. Maltase and transglucosidase activities of the amylase.J. Biochem. (Japan) 45, 49 (1958).

    CAS  Google Scholar 

  • Sawai T.: An amylase ofCandida tropicalis var.japonica. II. Further evidence for broard specificity of the amylase.J. Biochem. 48, 382 (1960).

    CAS  Google Scholar 

  • Smith B. W., Roe J. H.: A photometric method for the determination of α amylase in blood and urine with use of starch iodine color.J. Biol. Chem. 179, 53 (1949).

    PubMed  CAS  Google Scholar 

  • Strickland L. H.: The determination of small quantities of bacteria by means of the biuret reaction.J. Gen. Microbiol. 5, 698 (1951).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Moulin, G., Galzy, P. Amylase activity ofTorulopsis ingeniosa Di Menna. Folia Microbiol 23, 423–427 (1978). https://doi.org/10.1007/BF02885569

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02885569

Keywords

Navigation