1887

Abstract

Conidia of QM 9414 are able to degrade crystalline cellulose to glucose in the absence of protein synthesis, indicating the presence of a cellulase enzyme system. Measurement of enzyme activities revealed the presence of several glycanases and glycosidases. The cellulase enzyme system appeared irrespective of the conditions applied to induce conidiation. Removal of the endo-1,4--glucanase from the cellulase system could be achieved by treatment of conidia with -octylglucoside or Triton X-100. Conidia treated in this way grew poorly on cellulose but well on glycerol. The endo-1,4--glucanase released from conidia by -octylglucoside appeared as a single enzyme upon SDS-PAGE/immunoblotting with an apparent molecular mass of 68 kDa, an isoelectric point of 4·8–5·3, and a pH optimum between pH 4–6. These properties were similar to endo-1,4--glucanase I purified from culture filtrates of cellulose-grown Thermostability of the released enzyme was, however, lower than that of endo-1,4--glucanase I. Germination of conidia in a medium containing glycerol as a carbon source led to a loss of endo-1,4--glucanase activity which paralleled the decrease in the number of ungerminated conidia.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-134-5-1215
1988-05-01
2021-10-21
Loading full text...

Full text loading...

/deliver/fulltext/micro/134/5/mic-134-5-1215.html?itemId=/content/journal/micro/10.1099/00221287-134-5-1215&mimeType=html&fmt=ahah

References

  1. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  2. Chakravarti D. N., Chakravarti B., Chakrabarti P. 1981; Studies on phospholipase activities in Neurospora crassa conidia. Archives of Biochemistry and Biophysics 206:392–402
    [Google Scholar]
  3. Combepine G., Turian G. 1970; Activités de quelques enzymes associés à la conidiogénese du Neurospora crassa. Archives of Microbiology 72:36–47
    [Google Scholar]
  4. Enari T. M., Niku-Paavola M. L. 1987; Enzymatic cellulose hydrolysis. CRC Critical Reviews in Biotechnology 5:67–87
    [Google Scholar]
  5. Hill E. P., Sussman A. S. 1964; Development of trehalase and invertase activity in Neurospora. Journal of Bacteriology 88:1556–1566
    [Google Scholar]
  6. Horikoshi K., Ikeda Y. 1965; Studies on the spore coat of Aspergillus oryzae. II. Conidia coat-bound β-glucosidase. Biochimica et biophysica acta 101:352–356
    [Google Scholar]
  7. Kammel W. P., Kubicek C. P. 1985; Absence of postsecretional modification of extracellular proteins during growth of Trichodermareesei on crystalline cellulose. Journal of Applied Biochemistry 7:138–144
    [Google Scholar]
  8. Kolar H., Mischak H., Kammel W. P., Kubicek C. P. 1985; Carboxymethylcellulase and β-glucosidase secretion by protoplasts of Trichoderma reesei. Journal of General Microbiology 131:1339–1347
    [Google Scholar]
  9. Kubicek C. P. 1981; Release of carboxymethylcellulase and β-glucosidase from cell walls of Trichoderma reesei. European Journal of Applied Microbiology and Biotechnology 13:226–231
    [Google Scholar]
  10. Kubicek C. P. 1987; Involvement of a conidial endoglucanase and a plasma-membrane-bound β-glucosidase in the induction of endoglucanase synthesis by cellulose in Trichoderma reesei. Journal of General Microbiology 133:1481–1487
    [Google Scholar]
  11. Kubicek C. P., Panda T., Schreferl-Kunar G., Gruber F., Messner R. 1987; O-linked but not N-linked glycosylation is necessary for the secretion of endoglucanases I and II by Trichoderma reesei. Canadian Journal of Microbiology 33:698–703
    [Google Scholar]
  12. Labudova I., Farkas V. 1983; Multiple enzyme forms in the cellulase system of Trichoderma reesei during its growth on cellulose. Biochimica et biophysica acta 744:135–140
    [Google Scholar]
  13. 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]
  14. Mandels G. R. 1953; Localization of carbohydrases at the surface of fungus spores by acid treatment. Experimental Cell Research 5:48–55
    [Google Scholar]
  15. Mandels M., Andreotti R. E. 1978; Problems and challenges in the cellulose to cellulase fermentation. Process Biochemistry 13:6–13
    [Google Scholar]
  16. Messner R., Kubicek C. P. 1988; Intracellular precursors of endo-β-1,4-glucanase in Trichoderma reesei. FEMS Microbiology Letters (in the Press)
    [Google Scholar]
  17. Merivuori H., Siegler K. M., Sands J. A., Montenecourt B. S. 1984; Regulation of cellulase biosynthesis and secretion in fungi. Biochemical Society Transactions 13:411–414
    [Google Scholar]
  18. Metzenberg R. L. 1963; The localization of β-fructofuranosidases in Neurospora. Biochimica et biophysica acta 77:455–465
    [Google Scholar]
  19. Nisizawa T. H., Suzuki H., Nisizawa K. 1972; Catabolite repression of cellulase formation in Trichoderma viride. Journal of Biochemistry 70:375–393
    [Google Scholar]
  20. Sternberg D., Mandels G. R. 1979; Induction of cellulolytic enzymes in Trichoderma reesei by sophorose. Journal of Bacteriology 139:761–769
    [Google Scholar]
  21. Teeri T. T., Lehtovaara P., Kaupinnen S., Salovuori I., Knowles J. 1987; Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51:43–52
    [Google Scholar]
  22. Umile C., Kubicek C. P. 1986; A constitutive plasma-membrane bound β-glucosidase in Trichoderma reesei. FEMS Microbiology Letters 34:291–295
    [Google Scholar]
  23. Williams A. G., Orpin C. G. 1987; Glycoside hydrolase enzymes present in the zoospore and vegetative growth stages of the rumen fungus Neocallimastix patriciarum, Piromonascommunis, and an unidentified isolate, grown on a range of carbohydrates. Canadian Journal of Microbiology 33:427–434
    [Google Scholar]
  24. Wood T. M. 1984; Properties of cellulolytic enzyme systems. Biochemical Society Transactions 13:407–410
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-134-5-1215
Loading
/content/journal/micro/10.1099/00221287-134-5-1215
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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