Applied Biochemistry and Biotechnology

, Volume 22, Issue 3, pp 263–278 | Cite as

Enhanced glucose production from cellulose using coimmobilized cellulase and β-glucosidase

  • Ajoy C. Chakrabarti
  • Kenneth B. Storey
Article

Abstract

β-Glucosidase was covalently immobilized alone and coimmobilized with cellulase using a hydrophilic polyurethane foam (Hypol®FHP 2002). Immobilization improved the functional properties of the enzymes. When immobilized alone, the Km for cellobiose of β-glucosidase was decreased by 33% and the pH optimum shifted to a slightly more basic value, compared to the free enzyme. Immobilized β-glucosidase was extremely stable (95% of activity remained after 1000 h of continuous use). Coimmobilization of cellulase and β-glucosidase produced a cellulose-hydrolyzing complex with a 2.5-fold greater rate of glucose production for soluble cellulose and a four-fold greater increase for insoluble cellulose, compared to immobilized cellulase alone. The immobilized enzymes showed a broader acceptance of various types of insoluble cellulose substrates than did the free enzymes and showed a long-term (at least 24 h) linear rate of glucose production from microcrystalline cellulose. The pH optimum for the coimmobilized enzymes was 6.0. This method for enzyme immobilization is fast, irreversible, and does not require harsh conditions. The enhanced glucose yields obtained indicate that this method may prove useful for commercial cellulose hydrolysis.

Index Entries

β-Glucosidase cellulase  polyurethane foam enzyme immobilization 

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References

  1. 1.
    Sundstrom, D., Klei, H., Coughlin, R., Biederman, G., andBrouwer C. (1981),Biotechnol. Bioengin. 23, 473.CrossRefGoogle Scholar
  2. 2.
    Emsley, J. (1987),New Scientist 39, October 8.Google Scholar
  3. 3.
    Knowles, J., Lehtovaara, P., and Teeri, T. (1987),Trends Biotechnol. 5, 255.CrossRefGoogle Scholar
  4. 4.
    Klyosov, A. (1986),Appl. Biochem. Biotechnol. 12, 249.CrossRefGoogle Scholar
  5. 5.
    Matteau, P. and Saddler, J. (1982),Biotechnol. Lett. 4, 513.CrossRefGoogle Scholar
  6. 6.
    Srinivasan, V. and Bumm, W. (1974),Biotechnol. Bioengin. 16, 1413.CrossRefGoogle Scholar
  7. 7.
    Kumakura, M. and Kaetsu, I. (1982),Biosci. Reports 4, 181.CrossRefGoogle Scholar
  8. 8.
    Drioli, E., Iorio, G., Santoro, R., De Rosa, M., Gambacorta, A., and Nichlaus, B. (1982),J. Mol. Catal. 14, 247.CrossRefGoogle Scholar
  9. 9.
    Chakrabarti, A. and Storey, K. B. (1988),Appl. Biochem. Biotechnol. 19, 189.CrossRefGoogle Scholar
  10. 10.
    Lowry, O. H. and Passonneau, J. V. (1972),A Flexible System of Enzymatic Analysis, Academic Press, NY.Google Scholar
  11. 11.
    Atha, D. H. and Ingham, K. C. (1981),J. Biol. Chem. 256, 12108.Google Scholar
  12. 12.
    Montenecourt, B. S. (1983),Trends Biotechnol. 1, 156.CrossRefGoogle Scholar
  13. 13.
    Sternberg, D., Vijayakumar, P., and Reese, E. (1977),Can. J. Microbiol. 23 139.CrossRefGoogle Scholar
  14. 14.
    Ward, O. (1985),Comprehensive Biotechnology, vol. 3, Moo-Young, M., ed., Pergamon, Oxford, UK.Google Scholar
  15. 15.
    Tan, L. U. L., Yu, E. K. C, Louis-Seize, G. W., and Saddler, J. N. (1986),Appl. Microb. Biotechnol. 25, 250.Google Scholar

Copyright information

© Humana Press Inc. 1989

Authors and Affiliations

  • Ajoy C. Chakrabarti
    • 1
  • Kenneth B. Storey
    • 1
  1. 1.Institute of Biochemistry and Department of BiologyCarleton UniversityOttawaCanada

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