1887

Abstract

Summary: Enzyme preparations active against crystalline cellulose, marble-milled filter paper, carboxymethyicellulose (CM-cellulose), hemicellulose and xylan were obtained from cultures of . These preparations also contained swelling factor, pectin methylesterase, pectin lyase and low levels of aryl β-glucosidase and aryl β-xylosidase. CM-cellulase and xylanase activities were present in a high molecular weight complex, but substrate competition studies showed that different active sites were probably responsible for each activity. Analysis of products and viscosity changes during enzymic hydrolysis of CM-cellulose and xylan indicated that the most active enzymes were of the exo-1, 4-β-glycosidase type. A variety of reducing sugars were released from cell walls of (perennial ryegrass) by enzyme preparations.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-110-1-21
1979-01-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/110/1/mic-110-1-21.html?itemId=/content/journal/micro/10.1099/00221287-110-1-21&mimeType=html&fmt=ahah

References

  1. Andrews P. 1965; The gel filtration behaviour of proteins related to their molecular weights over a wide range.. Biochemical Journal 96:595–606
    [Google Scholar]
  2. Carlsson J. 1973; Simplified gas chromatographic procedure for identification of bacterial metabolic products.. Applied Microbiology 25:287–289
    [Google Scholar]
  3. Dehority B. A. 1973; Hemicellulose degradation by rumen bacteria.. Federation Proceedings 32:1819–1825
    [Google Scholar]
  4. Dekker R. F. H., Richards G. N. 1976; Hemicellulases: their occurrence, purification, properties and mode of action.. Advances in Carbohydrate Chemistry and Biochemistry 32:277–352
    [Google Scholar]
  5. Gradel C. M., Dehority B. A. 1972; Fermentation of isolated pectin and pectin from intact forages by pure cultures of rumen bacteria.. Applied Microbiology 23:332–340
    [Google Scholar]
  6. Halliwell G. 1961; The action of cellulolytic enzymes from Myrothecium verrucaria. Biochemical Journal 79:185–192
    [Google Scholar]
  7. Halliwell G., Riaz M. 1971; Interactions between components of the cellulase complex of Trichoderma koningii on native substrates.. Archiv für Mikrobiologie 78:295–309
    [Google Scholar]
  8. Hungate R. E. 1966 The Rumen and its Microbes. New York and London: Academic Press;
    [Google Scholar]
  9. King K. W. 1963; Endwise degradation of cellulose. In Enzymic Hydrolysis of Cellulose and Related Materials pp. 159–170 Edited by Reese E. T. London: Pergamon Press;
    [Google Scholar]
  10. Latham M. J., Brooker B. E., Pettipher G. L., Harris P. J. 1978; Ruminococcus flavefaciens cell coat and adhesion to cotton cellulose and to cell walls in leaves of perennial ryegrass (Lolium per erne).. Applied and Environmental Microbiology 35:156–165
    [Google Scholar]
  11. Leatherwood J. M. 1969; Cellulase complex of Ruminococcus and a new mechanism for cellulose degradation. In Cellulases and Their Applications Advances in Chemistry Series 95, pp. 53–57 Edited by Gould R. F. Washington: American Chemical Society;
    [Google Scholar]
  12. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent.. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  13. Nisizawa K. 1973; Mode of action of cellulases.. Journal of Fermentation Technology 51:267–304
    [Google Scholar]
  14. Nisizawa T., Suzuki H., Nisizawa K. 1966; Swelling factor activity of Trichoderma cellulase for absorbent cotton.. Journal of Fermentation Technology 44:659–668
    [Google Scholar]
  15. Pettipher G. L., Latham M. J. 1976; Extracellular cellulases and xylanases of Ruminococcus flavefaciens. Proceedings of the Society for General Microbiology 4:42
    [Google Scholar]
  16. Pierce Chemical Co 1976; In General Catalog, 1976–1977. pp. 242–244 Rockford, III., U.S.A.: Pierce Chemical Co;
    [Google Scholar]
  17. Reese E. T., Siu R. G. H., Levinson H. S. 1950; Biological degradation of soluble cellulose and its relationship to the mechanism of cellulose hydrolysis.. Journal of Bacteriology 59:485–497
    [Google Scholar]
  18. Rombouts F. M. 1972 Occurrence and properties of bacterial pectate lyases. Ph.D. thesis Wageningen Agricultural University, The Netherlands;
    [Google Scholar]
  19. Sharma M. 1968 Immunochemical studies of cellulases from several strains of Ruminococcus flavefaciens. Ph.D. thesis North Carolina State University, U.S.A.;
    [Google Scholar]
  20. Shikata S., Nisizawa K. 1975; Purification and properties of an exo-cellulase component of novel type from Trichoderma viride. Journal of Biochemistry 78:499–512
    [Google Scholar]
  21. Smith W. R., Yu I., Hungate R. E. 1973; Factors affecting cellulolysis by Ruminococcus albus. Journal of Bacteriology 114:729–737
    [Google Scholar]
  22. Suzuki H., Yamane K., Nisizawa K. 1969; Extracellular and cell-bound cellulase components of bacteria. In Celluloses and Their Applications Advances in Chemistry Series 95, pp. 60–82 Edited by Gould R. F. Washington: American Chemical Society;
    [Google Scholar]
  23. Toda S., Suzuki H., Nisizawa K. 1971; Some enzymic properties and substrate specificities of Trichoderma cellulases with special reference to their activity towards xylan.. Journal of Fermentation Technology 49:499–521
    [Google Scholar]
  24. Wilkinson G. N. 1961; Statistical estimations in enzyme kinetics.. Biochemical Journal 80:324–332
    [Google Scholar]
  25. Wood T. M. 1968; Cellulolytic enzyme system of Trichoderma koningii. Separation of components attacking native cotton.. Biochemical Journal 109:217–227
    [Google Scholar]
  26. Wood T. M., McCrae S. I. 1975; The cellulase complex of Trichoderma koningii. In Symposium on Enzymatic Hydrolysis of Cellulose pp. 231–254 Edited by Bailey M., Enari T. -M., Linko M. Helsinki: The Finnish National Fund for Research and Development (SITRA);
    [Google Scholar]
  27. Wood T. M., McCrae S. I. 1978; The cellulase of Trichoderma koningii. Purification and properties of some endoglucanase components with special reference to their action on cellulose when acting alone and in synergism with the cello-biohydrolase.. Biochemical Journal 171:61–72
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-110-1-21
Loading
/content/journal/micro/10.1099/00221287-110-1-21
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