Skip to main content
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1985 May;49(5):1314–1322. doi: 10.1128/aem.49.5.1314-1322.1985

Production and regulation of cellulase by two strains of the rumen anaerobic fungus Neocallimastix frontalis.

D O Mountfort, R A Asher
PMCID: PMC238548  PMID: 3923931

Abstract

Cellulase production was examined in two strains of Neocallimastix frontalis, namely, PN-1 isolated from the ovine rumen, and PN-2 from the bovine rumen. For both strains, carboxymethylcellulase (CMCase) had a pH optimum of 6.0 and a temperature optimum of 50 degrees C. CMCase resided mainly in the culture fluid, and activities up to 170 U ml-1 (1 U represents 1 microgram of glucose equivalents released per min) were obtained for cultures grown on 2.5 mg of cellulose ml-1. For resting cultures of strain PN-1, the yield of CMCase increased from 9.9 X 10(3) to 10.4 X 10(4) U per g of cellulose degraded, as the initial cellulose concentration decreased from 10 to 0.58 mg ml-1. The range for PN-2 was 8.1 X 10(3) to 11 X 10(4) U g-1. Shaking cultures improved yields for strain PN-1 but not for PN-2. Decreased CMCase production at high initial cellulose concentrations concurred with accumulation of glucose, and addition of glucose (4 mg ml-1) to cultures grown on low cellulose in which none of the sugar accumulated repressed CMCase. Adsorption of CMCase was excluded as a likely explanation for decreased yields at high initial cellulose as only a low proportion (less than 20%) of the enzyme was adsorbed onto the growth substrate. Exoglucanase, measured with alkali-treated Sigmacell or Avicel, gave low levels of activity in the culture fluid (less than 2 U ml-1) and did not appear to be associated with the fungal rhizoid, as treatment with various solubilizing agents failed to give increased activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Full text

PDF
1314

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BAILEY R. W. The reaction of pentoses with anthrone. Biochem J. 1958 Apr;68(4):669–672. doi: 10.1042/bj0680669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balch W. E., Wolfe R. S. New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressureized atmosphere. Appl Environ Microbiol. 1976 Dec;32(6):781–791. doi: 10.1128/aem.32.6.781-791.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bauchop T., Mountfort D. O. Cellulose fermentation by a rumen anaerobic fungus in both the absence and the presence of rumen methanogens. Appl Environ Microbiol. 1981 Dec;42(6):1103–1110. doi: 10.1128/aem.42.6.1103-1110.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bauchop T. Rumen anaerobic fungi of cattle and sheep. Appl Environ Microbiol. 1979 Jul;38(1):148–158. doi: 10.1128/aem.38.1.148-158.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Breuil C., Kushner D. J. Cellulase induction and the use of cellulose as a preferred growth substrate by Cellvibrio gilvus. Can J Microbiol. 1976 Dec;22(12):1776–1781. doi: 10.1139/m76-264. [DOI] [PubMed] [Google Scholar]
  6. Eriksson K. E., Hamp S. G. Regulation of Endo-1,4-beta-glucanase production in Sporotrichum pulverulentum. Eur J Biochem. 1978 Sep 15;90(1):183–190. doi: 10.1111/j.1432-1033.1978.tb12589.x. [DOI] [PubMed] [Google Scholar]
  7. Forsberg C. W., Beveridge T. J., Hellstrom A. Cellulase and Xylanase Release from Bacteroides succinogenes and Its Importance in the Rumen Environment. Appl Environ Microbiol. 1981 Nov;42(5):886–896. doi: 10.1128/aem.42.5.886-896.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fusee M. C., Leatherwood J. M. Regulation of cellulase from Ruminococcus. Can J Microbiol. 1972 Mar;18(3):347–353. doi: 10.1139/m72-053. [DOI] [PubMed] [Google Scholar]
  9. HUGGETT A. S., NIXON D. A. Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose. Lancet. 1957 Aug 24;273(6991):368–370. doi: 10.1016/s0140-6736(57)92595-3. [DOI] [PubMed] [Google Scholar]
  10. Lee B. H., Blackburn T. H. Cellulase production by a thermophilic clostridium species. Appl Microbiol. 1975 Sep;30(3):346–353. doi: 10.1128/am.30.3.346-353.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MANDELS M., REESE E. T. Induction of cellulase in fungi by cellobiose. J Bacteriol. 1960 Jun;79:816–826. doi: 10.1128/jb.79.6.816-826.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mountfort D. O., Asher R. A., Bauchop T. Fermentation of Cellulose to Methane and Carbon Dioxide by a Rumen Anaerobic Fungus in a Triculture with Methanobrevibacter sp. Strain RA1 and Methanosarcina barkeri. Appl Environ Microbiol. 1982 Jul;44(1):128–134. doi: 10.1128/aem.44.1.128-134.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mountfort D. O., Asher R. A. Role of catabolite regulatory mechanisms in control of carbohydrate utilization by the rumen anaerobic fungus Neocallimastix frontalis. Appl Environ Microbiol. 1983 Dec;46(6):1331–1338. doi: 10.1128/aem.46.6.1331-1338.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ng T. K., Weimer T. K., Zeikus J. G. Cellulolytic and physiological properties of Clostridium thermocellum. Arch Microbiol. 1977 Jul 26;114(1):1–7. doi: 10.1007/BF00429622. [DOI] [PubMed] [Google Scholar]
  15. Nisizawa T., Suzuki H., Nisizawa K. Catabolite repression of cellulase formation in Trichoderma viride. J Biochem. 1972 Jun;71(6):999–1007. doi: 10.1093/oxfordjournals.jbchem.a129872. [DOI] [PubMed] [Google Scholar]
  16. Ram S. P., Sullivan P. A., Shepherd M. G. The in situ assay of Candida albicans enzymes during yeast growth and germ-tube formation. J Gen Microbiol. 1983 Aug;129(8):2367–2378. doi: 10.1099/00221287-129-8-2367. [DOI] [PubMed] [Google Scholar]
  17. Shewale J. G., Sadana J. C. Cellulase and beta-glucosidase production by a basidiomycete species. Can J Microbiol. 1978 Oct;24(10):1204–1216. doi: 10.1139/m78-195. [DOI] [PubMed] [Google Scholar]
  18. Smith W. R., Yu I., Hungate R. E. Factors affecting cellulolysis by Ruminococcus albus. J Bacteriol. 1973 May;114(2):729–737. doi: 10.1128/jb.114.2.729-737.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sternberg D. Production of cellulase by Trichoderma. Biotechnol Bioeng Symp. 1976;(6):35–53. [PubMed] [Google Scholar]
  20. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  21. Traynor O. J., Costa N. L., Wood C. B. A scanning electron microscopy study of changes in the colonic mucus layer during chemical carcinogenesis. Cancer. 1983 May 15;51(10):1847–1853. doi: 10.1002/1097-0142(19830515)51:10<1847::aid-cncr2820511016>3.0.co;2-4. [DOI] [PubMed] [Google Scholar]
  22. Updegraff D. M. Semimicro determination of cellulose in biological materials. Anal Biochem. 1969 Dec;32(3):420–424. doi: 10.1016/s0003-2697(69)80009-6. [DOI] [PubMed] [Google Scholar]
  23. Wood T. M., Wilson C. A., Stewart C. S. Preparation of the cellulase from the cellulolytic anaerobic rumen bacterium Ruminococcus albus and its release from the bacterial cell wall. Biochem J. 1982 Jul 1;205(1):129–137. doi: 10.1042/bj2050129. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES