Cellulase Production Based on Hemicellulose Hydrolysate from Steam-Pretreated Willow

  • Zsolt Szengyel
  • Guido Zacchi
  • Kati Réczey
Part of the Applied Biochemistry and Biotechnology book series (ABAB, volume 63-65)


The production cost of cellulolytic enzymes is a major contributor to the high cost of ethanol production from lignocellulosics using enzymatic hydrolysis. The aim of the present study was to investigate the cellulolytic enzyme production of Trichoderma reesei Rut C 30, which is known as a good cellulase secreting micro-organism, using willow as the carbon source. The willow, which is a fast-growing energy crop in Sweden, was impregnated with 1–4% SO2 and steam-pretreated for 5 min at 206°C. The preheated willow was washed and the wash water, which contains several soluble sugars from the hemicellulose, was supplemented with fibrous preheated willow and used for enzyme production. In addition to sugars, the liquid contains degradation products such as acetic acid, furfural, and 5-hydroxy-methylfurfural, which are inhibitory for microorganisms. The results showed that 50% of the cellulose can be replaced with sugars from the wash water. The highest enzyme activity, 1.79 FPU/mL and yield, 133 FPU/g carbohydrate, was obtained at pH 6.0 using 20 g/L carbon source concentration. At lower pHs, a total lack of growth and enzyme production was observed, which probably could be explained by furfural inhibition.

Index Entries

Cellulase enzyme production Trichoderma reesei Rut C 30 lignocellulosics furfural inhibition 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Galbe, M. (1994), PhD thesis, Lund Institute of Technology, Lund, Sweden.Google Scholar
  2. 2.
    Eklund, R. (1994), PhD thesis, Lund Institute of Technology, Lund, Sweden.Google Scholar
  3. 3.
    von Sivers, M. and Zacchi, G. (1995), Bioresource Technol. 51, 43–52.CrossRefGoogle Scholar
  4. 4.
    Eklund, R., Galbe, M., and Zacchi, G. (1995), Bioresource Technol. 51, 225–229.CrossRefGoogle Scholar
  5. 5.
    Palmqvist, E., Hahn-Hägerdal, B., Galbe, M., and Zacchi, G. (1996), Enzyme Microb. Technol. 19, 470–476..CrossRefGoogle Scholar
  6. 6.
    Olsson, L. and Hahn-Hägerdal, B. (1993), Process Biochem. 28, 249–257.CrossRefGoogle Scholar
  7. 7.
    Mohagheghi, A., Grohmann, K., and Wyman, C. E. (1988), Appt. Biochem. Biotechnol. 17, 263–277.CrossRefGoogle Scholar
  8. 8.
    Schaffner, D. W. and Toledo, R. T. (1991), Biotehnol. Bioeng. 37,12–14.CrossRefGoogle Scholar
  9. 9.
    Réczey, K., Szengyel, Zs., Eklund, R., and Zacchi, G. (1996), Bioresource Technol. 57, 25–30.CrossRefGoogle Scholar
  10. 10.
    Palmqvist, E., Hahn-Hägerdal, B., Galbe, M., Larsson, M., Stenberg, K., Szengyel, Zs., Tengborg, C., and Zacchi, G. (1996), Bioresource Technol, 58,171–179.CrossRefGoogle Scholar
  11. 11.
    Hägglund, E. (1951), in Chemistry of Wood, Academic Press, New York, NY.Google Scholar
  12. 12.
    Mandels, M. and Weber, J. (1969), Adv. Chem. Ser. 95, 391–414.CrossRefGoogle Scholar
  13. 13.
    Mandels, M., Andreotti, R., and Roche, C. (1976), Biotechnol. Bioeng. Symp. 6, 21–33.Google Scholar
  14. 14.
    Berghem, L. E. R. and Petterson, L. G. (1974), Eur. J. Biochem. 46, 295–305.CrossRefGoogle Scholar
  15. 15.
    Sestak, S. and Farkas, V. (1993), Can. J. Microbiol. 39, 342–347.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc. 1997

Authors and Affiliations

  • Zsolt Szengyel
    • 1
  • Guido Zacchi
    • 1
  • Kati Réczey
    • 2
  1. 1.Department of Chemical Engineering 1University of LundLundSweden
  2. 2.Department of Agricultural Chemical TechnologyTechnical University of BudapestBudapestHungary

Personalised recommendations