Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1978 Oct;36(4):606–612. doi: 10.1128/aem.36.4.606-612.1978

Cellulolytic Enzyme System of Thermoactinomyces sp. Grown on Microcrystalline Cellulose

Bärbel G R Hägerdal 1,†, John D Ferchak 1, E Kendall Pye 1
PMCID: PMC243098  PMID: 16345322

Abstract

The carboxymethyl-cellulase and Avicelase activities of Thermoactinomyces sp., strain YX, were produced simultaneously with cell growth. Throughout the growth phase these activities were primarily extracellular, with up to 50% adsorbed to residual cellulosic substrate at any one time. On the other hand, the β-glucosidase activity was associated with the culture solids throughout the entire fermentation and appears to be intracellular. Preparative isoelectric focusing of the culture filtrate, in the pH range 3 to 5, separated three major fractions with cellulolytic activities towards both carboxymethyl-cellulose and Avicel. Based on the carboxymethyl-cellulase and Avicelase activities of these separated fractions, it was not possible to discriminate between endo- and exoglucanases produced by Thermoactinomyces sp. Analytical isoelectric focusing of culture filtrates obtained throughout the growth phase of Thermoactinomyces indicated that all the extracellular cellulolytic enzymes are produced and released into the culture filtrate simultaneously, with no evidence of a sequential appearance of the various enzymes or isoenzymes.

Full text

PDF
606

Images in this article

609Image
on p.609
610Image
on p.610

Selected References

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

  1. Almin K. E., Eriksson K. E. Enzymic degradation of polymers. I. Viscometric method for the determination of enzymic activity. Biochim Biophys Acta. 1967 Jul 11;139(2):238–247. doi: 10.1016/0005-2744(67)90028-9. [DOI] [PubMed] [Google Scholar]
  2. Berg B., Pettersson G. Location and formation of cellulases in Trichoderma viride. J Appl Bacteriol. 1977 Feb;42(1):65–75. doi: 10.1111/j.1365-2672.1977.tb00670.x. [DOI] [PubMed] [Google Scholar]
  3. Berghem L. E., Pettersson L. G., Axiö-Fredriksson U. B. The mechanism of enzymatic cellulose degradation. Purification and some properties of two different 1,4beta-glucan glucanohydrolases from Trichoderma viride. Eur J Biochem. 1976 Jan 15;61(2):621–630. doi: 10.1111/j.1432-1033.1976.tb10058.x. [DOI] [PubMed] [Google Scholar]
  4. Berghem L. E., Pettersson L. G. The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose. Eur J Biochem. 1973 Aug 1;37(1):21–30. doi: 10.1111/j.1432-1033.1973.tb02952.x. [DOI] [PubMed] [Google Scholar]
  5. Eriksson K. E., Pettersson B. Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cellulose. 1. Separation, purification and physico-chemical characterization of five endo-1,4-beta-glucanases. Eur J Biochem. 1975 Feb 3;51(1):193–206. doi: 10.1111/j.1432-1033.1975.tb03919.x. [DOI] [PubMed] [Google Scholar]
  6. Gong C. S., Ladisch M. R., Tsao G. T. Cellobiase from Trichoderma viride: purification, properties, kinetics, and mechanism. Biotechnol Bioeng. 1977 Jul;19(7):959–981. doi: 10.1002/bit.260190703. [DOI] [PubMed] [Google Scholar]
  7. Gum E. K., Jr, Brown R. D., Jr Comparison of four purified extracellular 1,4-beta-D-glucan cellobiohydrolase enzymes from Trichoderma viride. Biochim Biophys Acta. 1977 May 27;492(1):225–231. doi: 10.1016/0005-2795(77)90229-x. [DOI] [PubMed] [Google Scholar]
  8. Gum E. K., Jr, Brown R. D., Jr Structural characterization of a glycoprotein cellulase, 1,4-beta-D-glucan cellobiohydrolase C from Trichoderma viride. Biochim Biophys Acta. 1976 Oct 28;446(2):371–386. doi: 10.1016/0005-2795(76)90004-0. [DOI] [PubMed] [Google Scholar]
  9. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  10. Mandels M., Andreotti R., Roche C. Measurement of saccharifying cellulase. Biotechnol Bioeng Symp. 1976;(6):21–33. [PubMed] [Google Scholar]
  11. Nakayama M., Tomita Y., Suzuki H., Nisizawa K. Partial proteolysis of some cellulase components from Trichoderma viride and the substrate specificity of the modified products. J Biochem. 1976 May;79(5):955–966. doi: 10.1093/oxfordjournals.jbchem.a131163. [DOI] [PubMed] [Google Scholar]
  12. SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]
  13. Wood T. M., McCrae S. I. The purification and properties of the C 1 component of Trichoderma koningii cellulase. Biochem J. 1972 Aug;128(5):1183–1192. doi: 10.1042/bj1281183. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES