Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Properties of the β-d-glucosidase (cellobiase) from the wood-rotting fungus, Coriolus versicolor


Structural and kinetic parameters of the β-d-glucosidase (cellobiase, β-d-glucoside glucohydrolase) from Coriolus versicolor have been determined. It is a high molecular weight glycoprotein (300,000 d) composed 10% by weight of protein, 90% by weight of carbohydrate in which glucose is the primary hexose sugar. The Km for 4-nitrophenyl-β-d-glucopyranoside (4 NPG) and cellobiose are 0.276 and 2.94 mM respectively at pH 4.5 and 40°. d-Glucose is a competitive inhibitor with a Ki of 1.8 mM with 4 NPG as substrate, and at high concentrations, cellobiose exhibits a substrate inhibition effect on the enzyme, so negating attempts to overcome the competitive inhibition of glucose by increasing the concentration of the substrate.

This is a preview of subscription content, log in to check access.


  1. Abrams E (1948) Microbiological deterioration of organic materials its prevention and methods of test. National Bureau of Standards Misc. Publ. No. 188 U.S. Dept. of Commerce, Washington

  2. Albersheim P, Nevins DJ, English PD, Karr A (1967) A method for the analysis of sugars in plant cell-wall polysaccharides by gas-liquid chromatography. Carbohydrate Res 5: 340–345

  3. Bergheim LER, Pettersson LG, Axiö-Fredriksson U-B (1975) Mechanism of Enzymatic cellulose degradation — characterization and enzymatic properties of a β-1, 4-glucan cellobiohydrolase from Trichoderma viride. Eur J Biochem 53: 55–62

  4. Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1976) Colorimetric method for determination of sugars and related substances. Anal Chem 28: 350–356

  5. Eriksson KE (1978) Enzyme Mechanisms involved in cellulose hydrolysis by the rot fungus Sporotrichum pulverulentum. Biotech Bioeng 20: 317–332

  6. Evans CS, Farmer JY, Palmer JM (1984) An extracellular haem-protein from Coriolus versicolor. Phytochemistry 23: 1247–1250

  7. Ishihara T (1980) Lignin Biodegradation: Microbiology, chemistry and potential applications. Vol. 11, 17–31. CRC Press, Florida

  8. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275

  9. Pettersson G, Porath J (1963) Studies on cellulolytic enzymes. II. Multiplicity of the cellulolytic enzymes of Polyporus versicolor. Biochim Biophys Acta 67: 9–15

  10. Pettersson G, Cowling EB, Porath J (1963) Studies on cellulolytic enzymes. I. Isolation of a low molecular weight cellulase from Polyporus versicolor. Biochim Biophys Acta 67: 1–8

  11. Shewale JG (1982) β-Glucosidase: its role in cellulase synthesis and hydrolysis of cellulose. Int J Biochem 14: 435–443

  12. Woodward J, Wiseman A (1982) Fungal and other β-d-glucosidases—their properties and applications. Enz Microbiol Technol 4: 73–79

Download references

Author information

Correspondence to Christine S. Evans.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Evans, C.S. Properties of the β-d-glucosidase (cellobiase) from the wood-rotting fungus, Coriolus versicolor . Appl Microbiol Biotechnol 22, 128–131 (1985).

Download citation


  • Glucose
  • Enzyme
  • Sugar
  • Molecular Weight
  • Carbohydrate