Applied Biochemistry and Biotechnology

, Volume 23, Issue 2, pp 139–154 | Cite as

One-step conversion of cellulose to fructose using coimmobilized cellulase, β-glucosidase, and glucose isomerase

  • Kenneth B. Storey
  • Ajoy C. Chakrabarti
Article

Abstract

Glucose isomerase was immobilized by itself and coimmobilized with cellulase and β-glucosidase using a polyurethane foam (Hypol® FHP 2002). Approximately 50% of the enzyme added was immobilized. The immobilized enzyme was active at pH values as low as 6.8. When immobilized alone, the Km for Mg2+ increased by 5.5fold and the Km for fructose increased 62%. The half-life of the immobilized glucose isomerase was approximately 160 h of continuous hydrolysis, with a substantial (about 35–40%) amount of activity remaining even after 1000 h. When all three enzymes were immobilized together, the system was found capable of functioning at pH 7.0 to produce fructose from both soluble and insoluble cellulose substrates. At this pH, the glucose:fructose ratio was 70:30. The advantageous properties of the foam as a support for enzyme immobilization and the efficiency of the one-step conversion process outlined combine to make this system appear valuable for use in high fructose syrup production.

Index Entries

Glucose isomerase polyurethane foam cellulase enzyme coimmobilization high fructose syrup β-glucosidase 

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References

  1. 1.
    Verhoff, G., Boguslawski, G., Lantero, O. J., Schlager, S. T., and Jao, Y. C. (1985),Comprehensive Biotechnology, vol. 3, chapter 42, Moo-Young, M., ed., Pergamon, Oxford.Google Scholar
  2. 2.
    Chen, W.-P. (1980), ProcessBiochemistry (June-Sept.), 30.Google Scholar
  3. 3.
    Jensen, V. and Rugh, S. (1985),Methods Enzymol. 136, 356.Google Scholar
  4. 4.
    Trevan, M. D. (1980),Immobilized enzymes, Wiley, Toronto.Google Scholar
  5. 5.
    Chakrabarti, A. C. and Storey, K. B. (1988),Appl. Biochem. Biotechnol. 19, 189.CrossRefGoogle Scholar
  6. 6.
    Chakrabarti, A. C. and Storey, K. B. (1989),Appl. Biochem. Biotechnol, in press.Google Scholar
  7. 7.
    Knapp, J. S. (1985),Comprehensive Biotechnology, vol. 4, chapter 46, Moo-Young, M., ed., Pergamon, Oxford.Google Scholar
  8. 8.
    Emsley, J. (1987),New Scientist 39, October 8.Google Scholar
  9. 9.
    Kumakura, M. and Kaetsu, I. (1982),Biosci. Reports 4, 181.CrossRefGoogle Scholar
  10. 10.
    Drioli, E., Iorio, G., Santoro, R., De Rosa, M., Gambacorta, A., and Nichlaus, B. (1982),J. Mol. Catal. 14, 247.CrossRefGoogle Scholar
  11. 11.
    Lowry, O. H. and Passonneau J. V. (1972),A flexible system of Enzymatic Analysis, Academic, New York.Google Scholar
  12. 12.
    Antrim, R. L. and Auterinen, A.-L. (1985),Oral paper presented at the 36th Detmold Starch Convention, Finnsugar Biochemics Inc., Schaumburg, IL.Google Scholar
  13. 13.
    MacAllister, R. V. (1980),Immobilized enzymes for food processing, chapter 4, Pitcher, W. H. Jr., ed., CRC Press, Boca Raton, FL.Google Scholar
  14. 14.
    Woodward, J. and Arnold, S. L. (1981),Biotechnol. Bioeng. 23, 1553.CrossRefGoogle Scholar
  15. 15.
    Woodward, J. (1987),Carbon Substrates in Biotechnology, vol. 21, chapter 4, Stowell, J., Beardsmore, A., Keevil, C., and Woodward, J., eds., IRL Press, Oxford.Google Scholar
  16. 16.
    Pitcher, W. H. (1980),Immobilized Enzymes for Food Processing, chapter 2, Pitcher, W. H. Jr., ed., CRC Press, Cleveland, OH.Google Scholar

Copyright information

© Humana Press Inc 1990

Authors and Affiliations

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

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