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. 1971 Feb;121(3):353–362. doi: 10.1042/bj1210353

The cellulase of Fusarium solani. Purification and specificity of the β-(1→4)-glucanase and the β-d-glucosidase components

T M Wood 1
PMCID: PMC1176581  PMID: 5119766

Abstract

1. Cell-free culture filtrates of the fungus Fusarium solani were examined for homogeneity with respect to β-d-glucosidase and Cx activities. 2. o-Nitrophenyl β-d-glucoside and cellobiose were both used as substrates for β-d-glucosidase activity. 3. No evidence for the non-identity of nitrophenyl β-d-glucosidase and cellobiase activities could be found, either by heat treatment, gel filtration on Sephadex G-100 or by isoelectric focusing. 4. The β-d-glucosidase component was also a feeble exo-β-glucanase: it had a molecular weight of approx. 400000. 5. The fall in viscosity of a solution of CM-cellulose, the formation of reducing sugars in a solution of CM-cellulose and the solubilization of phosphoric acid-swollen cellulose (Walseth cellulose), were all used for the measurement of Cx activity. 6. The ratio of the two types of CM-cellulase activity was not changed after gel filtration on Sephadex G-100 or after chromatography on DEAE-Sephadex. 7. Three peaks of Cx activity were obtained after electrofocusing, but all three possessed the same ratio of the two types of CM-cellulase activity as well as the same CM-cellulase/Walseth activity ratio, as the unfractionated enzyme; all three isoenzymes (isoelectric points, 4.75, 4.80–4.85 and 5.15) acted in synergism with a mixture of the C1 and the β-d-glucosidase components to the same extent in the solubilization of cotton fibre. 8. The molecular weight of the Cx component was approx. 37000.

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Selected References

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

  1. Bucht B., Eriksson K. E. Extracellular enzyme system utilized by the rot fungus Stereum sanguinolentum for the breakdown of cellulose. IV. Separation of cellobiase and aryl beta-glucosidase activities. Arch Biochem Biophys. 1969 Feb;129(2):416–420. doi: 10.1016/0003-9861(69)90197-0. [DOI] [PubMed] [Google Scholar]
  2. Eriksson K. E., Pettersson B. Extracellular enzyme system utilized by the rot fungus Stereum sanguinolentum for the breakdown of cellulose. II. Purification of the cellulase. Arch Biochem Biophys. 1968 Mar 20;124(1):142–148. doi: 10.1016/0003-9861(68)90313-5. [DOI] [PubMed] [Google Scholar]
  3. GILLIGAN W., REESE E. T. Evidence for multiple components in microbial cellulases. Can J Microbiol. 1954 Oct;1(2):90–107. doi: 10.1139/m55-013. [DOI] [PubMed] [Google Scholar]
  4. HASH J. H., KING K. W. Some properties of an aryl-beta-glucosidase from culture filtrates of Myrothecium verrucaria. J Biol Chem. 1958 May;232(1):395–402. [PubMed] [Google Scholar]
  5. HAY G. W., LEWIS B. A., SMITH F. THIN-FILM CHROMATOGRAPHY IN THE STUDY OF CARBOHYDRATES. J Chromatogr. 1963 Aug;11:479–486. doi: 10.1016/s0021-9673(01)80949-3. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Li L. H., Flora R. M., King K. W. Individual roles of cellulase components derived from Trichoderma viride. Arch Biochem Biophys. 1965 Aug;111(2):439–447. doi: 10.1016/0003-9861(65)90207-9. [DOI] [PubMed] [Google Scholar]
  8. Okada G., Nisizawa K., Suzuki H. Cellulase components from Trichoderma viride. J Biochem. 1968 May;63(5):591–607. doi: 10.1093/oxfordjournals.jbchem.a128818. [DOI] [PubMed] [Google Scholar]
  9. REESE E. T., SIU R. G. H., LEVINSON H. S. The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis. J Bacteriol. 1950 Apr;59(4):485–497. doi: 10.1128/jb.59.4.485-497.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. SELBY K., MAITLAND C. C. THE FRACTIONATION OF MYROTHECIUM VERRUCARIA CELLULASE BY GEL FILTRATION. Biochem J. 1965 Mar;94:578–583. doi: 10.1042/bj0940578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Selby K., Maitland C. C. The cellulase of Trichoderma viride. Separation of the components involved in the solubilization of cotton. Biochem J. 1967 Sep;104(3):716–724. doi: 10.1042/bj1040716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Vesterberg O., Svensson H. Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. IV. Further studies on the resolving power in connection with separation of myoglobins. Acta Chem Scand. 1966;20(3):820–834. doi: 10.3891/acta.chem.scand.20-0820. [DOI] [PubMed] [Google Scholar]
  13. Wood T. M. Cellulolytic enzyme system of Trichoderma koningii. Separation of components attacking native cotton. Biochem J. 1968 Sep;109(2):217–227. doi: 10.1042/bj1090217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wood T. M. The cellulase of Fusarium solani. Resolution of the enzyme complex. Biochem J. 1969 Nov;115(3):457–464. doi: 10.1042/bj1150457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Wood T. M. The relationship between cellulolytic and pseudo-cellulolytic microorganisms. Biochim Biophys Acta. 1969 Dec 30;192(3):531–534. doi: 10.1016/0304-4165(69)90405-x. [DOI] [PubMed] [Google Scholar]

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