Skip to main content
Log in

Enzymatic activity of cellulase adsorbed on cellulose and its change during hydrolysis

  • Published:
Applied Biochemistry and Biotechnology Aims and scope Submit manuscript

Abstract

Hydrolysis of pure cellulose Avicel has been carried out, using Meicelase fromTrichodertna viride, where the enzymatic activity of cellulase adsorbed on cellulose and its changes during the hydrolysis were investigated. A rapid drop of the hydrolysis rate during the reaction, that is always observed in enzymatic hydrolysis of cellulose, could be explained by a decline of specific activity of adsorbed enzyme, and it was implied that the decline results from a loss of synergistic action between endoglucanase and exoglucanase. An empirical equation expresses the change of hydrolysis rate during the reaction and also shows that the change of the hydrolysis rate is caused by the decline of the specific enzymatic activity of adsorbed enzyme.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

E ads :

concentration of adsorbed enzyme (mg-protein/mL)

Et :

total concentration of enzyme (mg-protein/mL)

k :

overall inhibition constant in Eq. (1) (dimensionless)

m :

Parameter in Eq. (2) (dimensionless)

n :

parameter in Eq. (3) (dimensionless)

n 0 :

parameter in Eq. (4) (dimensionless)

q :

parameter in Eq. (4) (dimensionless)

S o :

initial concentration of cellulose (mg/mL)

t :

reaction time (h)

V :

hydrolysis rate of cellulose (mg/mL/h)

V 0 :

initial hydrolysis rate of cellulose (mg/mL/h)

X :

fractional conversion in the hydrolysis of cellulose (dimensionless)

References

  1. Ohmine, K., Ooshima, H., and Harano, Y. (1983),Biotechnol. Bioeng. 25, 2041.

    Article  CAS  Google Scholar 

  2. Burns, D. S., Ooshima, H., and Concerse, A. O. (1989),Appl. Biochem. Biotechnol. 20/21, 79.

    Article  Google Scholar 

  3. Converse, A. O., Matsuno, R., Tanaka, M., and Taniguchi, M. (1988),Biotechnol. Bioeng. 32, 38.

    Article  CAS  Google Scholar 

  4. Wood, T. M. and Macrae, S. I. (1972),Biochem. J. 128, 1183.

    CAS  Google Scholar 

  5. Okada, G. and Tanaka, Y. (1988),J. Jpn. Soc. Starch Sci. 4, 253.

    Google Scholar 

  6. Suga, K., Deden, G. van, and Moo-young, M. (1975),Biotechnol. Bioeng. 17, 185.

    Article  CAS  Google Scholar 

  7. Ooshima, H., Sakata, M., and Harano, Y. (1983),Biotechnol. Bioeng. 25, 3103.

    Article  CAS  Google Scholar 

  8. Nutor, J. R. K. and Converse, A. O. (1991),Appl. Biochem. Biotechnol. 28/29, 757.

    Google Scholar 

  9. Ooshima, H., Burns, D. S., and Converse, A. O. (1990),Biotechnol. Bioeng. 36, 446.

    Article  CAS  Google Scholar 

  10. Sakata, S., Ooshima, H., Ishitani, Y., and Harano, Y. (1985),Biotechnol. Lett. 7, 689.

    Article  CAS  Google Scholar 

  11. Lee, S. B., Kim, I. H., Ruy, D. D. Y. and Taguchi, H. (1983),Biotechnol. Bioeng. 25, 33.

    Article  CAS  Google Scholar 

  12. Matsuno, R., Taniguchi, M., Tanaka, M., and Kamikubo, T. (1984),Enzyme Eng. 7, Ann. New York Acad. Sci. 434, 158.

    Article  CAS  Google Scholar 

  13. Ooshima, H., Ohmine, K., Ishitani, Y., and Harano, Y. (1982),Biotechnol. Lett. 4, 729.

    Article  CAS  Google Scholar 

  14. Tanaka, M., Nakamura, H., Taniguchi, M., Morita, T., Matsuno, R., and Kamikubo, T. (1986),Appl. Mkrobiol. Biotechnol. 23, 263.

    CAS  Google Scholar 

  15. Grethlein, H. E., Allen, D. C, and Converse, A. O. (1984),Biotechnol. Bioeng. 16, 1498.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ooshima, H., Kurakake, M., Kato, J. et al. Enzymatic activity of cellulase adsorbed on cellulose and its change during hydrolysis. Appl Biochem Biotechnol 31, 253–266 (1991). https://doi.org/10.1007/BF02921752

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02921752

Index Entries

Navigation