1887

Abstract

SUMMARY: About 25% of the total cellular invertase and trehalase activity were found in a purified Neurospora wall preparation. Attempts were made to dissociate these enzymes from the walls with chemical reagents and hydrolytic enzymes. A detergent (Triton X-100), a sulphydryl reducing agent (-mercaptoethanol), a chelating agent (ethylenediaminetetraacetate), a concentrated salt solution (1 -KCl), and buffers ranging in pH from 3 to 10 did not release them significantly. Snail-gut juice released more than 90% of both enzymes. -1,3-Glucanase, prepared from -12, also released similar amounts. Chitinase released about 80% of invertase and 60% of trehalase. Cellulase did not release any significant amount of either enzyme. Trypsin released only a few per cent of invertase and severely inactivated trehalase. Thus it appears that these two wall-bound enzymes are released only when covalent bonds of the Neurospora wall constituents are disrupted.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-70-1-13
1972-04-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/70/1/mic-70-1-13.html?itemId=/content/journal/micro/10.1099/00221287-70-1-13&mimeType=html&fmt=ahah

References

  1. Beadle G. W., Tatum E. L. 1945; Neurospora. II. Methods of producing and detecting mutations concerned with nutritional requirements. American Journal of Botany 32:678–686
    [Google Scholar]
  2. Berger L. R., Reynolds D. M. 1958; The chitinase system of a strain of Streptomyces griseus. Bio-chimica et biophysica acta 29:522–534
    [Google Scholar]
  3. Burnett J. H. 1968 Fundamentals of Mycology pp. 17–59 London: Edward Arnold;
    [Google Scholar]
  4. Chung P. L. Y., Trevithick J. R. 1970; Biochemical and histochemical localization of invertase in Neurospora crassa during conidial germination and hyphal growth. Journal of Bacteriology 102:423–429
    [Google Scholar]
  5. Coles N. W., Gross R. 1967; Liberation of surface-located penicillinase from Staphylococcus aureus. Biochemical Journal 102:742–747
    [Google Scholar]
  6. Costerton J. W. 1970; The structure and function of the cell envelope of Gram-negative bacteria. Revue canadienne de biologie 29:299–316
    [Google Scholar]
  7. De Terra N., Tatum E. L. 1963; A relationship between cell wall structure and colonial growth in Neurospora crassa. American Journal of Botany 50:669–677
    [Google Scholar]
  8. Drysdale R. B., Fling M. 1965; Assay of proteolytic enzyme(s) from Neurospora crassa. Neurospora Newsletter 8:14–15
    [Google Scholar]
  9. Eberhart B. M. 1961; Exogenous enzymes of Neurospora conidia and mycelia. Journal of Cellular and Comparative Physiology 58:11–16
    [Google Scholar]
  10. Eberhart B. M., Beck R. S. 1970; Localization of the β-glucosidases in Neurospora crassa. Journal of Bacteriology 101:408–417
    [Google Scholar]
  11. Galsworthy S. B. 1966 Biochemical Aspects of Temperature Sensitivity in Neurospora Ph.D Thesis University of Wisconsin, Madison, Wisconsin:
    [Google Scholar]
  12. Hill E. P., Sussman A. S. 1964; Development of trehalase and invertase activity in Neurospora. Journal of Bacteriology 88:1556–1566
    [Google Scholar]
  13. Huggett A. STG., Nixon D. A. 1957; Enzymic determination of blood glucose. Biochemical Journal 66:12p
    [Google Scholar]
  14. Kidby D. K., Davies R. 1970; Thiol induced release of invertase from cell walls of Saccharomyces fragilis. Biochimica et biophysica acta 201:261–266
    [Google Scholar]
  15. Lampen J. O. 1968; External enzymes of yeast: their nature and formation. Antonie van Leeuwenhoek 34:1–18
    [Google Scholar]
  16. Lampen J. O., Neumann N. P., Gascon S., Montenecourt B. S. 1967; Invertase biosynthesis and the yeast cell membrane. In Organisational Biosynthesis pp. 363–372 Vogel H. J., Lampen J. O., Bryson V. Edited by New York: Academic Press;
    [Google Scholar]
  17. Mcmurrough I., Bartnicki-Garcia S. 1970; Chitin synthesis in Mucor rouxii. Biochemical Journal 119:11p
    [Google Scholar]
  18. Mahadevan P. R., Mahadkar U. R. 1970; Role of enzymes in growth and morphology of Neurospora crassa: cell-wall bound enzymes and their possible role in branching. Journal of Bacteriology 101:941–947
    [Google Scholar]
  19. Mahadevan P. R., Menon C. P. S. 1968; Laminarinase of Neurospora crassa. I. Enzyme activity associated with conidia and conidial wall. Indian Journal of Biochemistry 5:6–8
    [Google Scholar]
  20. Mahadevan P. R., Tatum E. L. 1965; Relationship of the major constituents of the Neurospora crassacell wall to wild-type and colonial morphology. Journal of Bacteriology 90:1073–1081
    [Google Scholar]
  21. Malamy M. H., Horecker B. L. 1964; Release of alkaline phosphatase from cells of Escherichia coliupon lysozyme spheroplast formation. Biochemistry 3:1889–1893
    [Google Scholar]
  22. Mandels G. R. 1953; Localization of carbohydrases at the surface of fungus spores by acid treatment. Experimental Cell Research 5:48–55
    [Google Scholar]
  23. Matile PH. 1964; Die Funktion proteolytischer Enzyme bei der Proteinaufnahme durch Neurospora crassa. Naturwissenschaften 51:489–490
    [Google Scholar]
  24. Merchant D. J., Kahn R. H., Murphy W. H. 1964; . Handbook of Cell and Organ Culture pp. 162–166 Minneapolis: Burgess Publishing Co;
    [Google Scholar]
  25. Metzenberg R. L. 1962; A gene affecting the repression of invertase and trehalase in Neurospora. Archives of Biochemistry and Biophysics 96:468–474
    [Google Scholar]
  26. Mitchell R., Sabar N. 1966; Autolytic enzymes in fungal cell walls. Journal of General Microbiology 42:39–42
    [Google Scholar]
  27. Pollock M. R. 1962; Exoenzymes. In The Bacteria 4 pp. 121–178 Gunsalus I. C., Stanier R. Y. Edited by New York: Academic Press;
    [Google Scholar]
  28. Scott W. A., Metzenberg R. L. 1970; Location of aryl sulfatase in conidia and young mycelia of Neurospora crassa. Journal of Bacteriology 104:1254–1265
    [Google Scholar]
  29. Tanaka H., Phaff H. J. 1965; Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes. Journal of Bacteriology 89:1570–1580
    [Google Scholar]
  30. Tonomura K., Tanabe O. 1964; Localization of cell-bound α-amylase in Aspergillus oryzae demonstrated by fluorescent-antibody technique. Journal of Bacteriology 87:226–227
    [Google Scholar]
  31. Trevithick J. R., Metzenberg R. L. 1964; The invertase isozyme formed by Neurospora protoplasts. Biochemical and Biophysical Research Communications 16:319–325
    [Google Scholar]
  32. Trevithick J. R., Metzenberg R. L. 1966; Molecular sieving by Neurospora cell walls during secretion of invertase isozymes. Journal of Bacteriology 92:1010–1015
    [Google Scholar]
  33. Weimberg R., Orton W. L. 1966; Elution of exocellular enzymes from Saccharomyces fragilis and Saccharomyces cerevisiae. Journal of Bacteriology 91:1–13
    [Google Scholar]
  34. Yabuki M., Fukui S. 1970; Presence of binding site for α-amylase and of masking protein for this site on mycelial cell walls of Aspergillus oryzae. Journal of Bacteriology 104:138–144
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-70-1-13
Loading
/content/journal/micro/10.1099/00221287-70-1-13
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error