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Do cellulose binding domains increase substrate accessibility?

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Abstract

This article provides an overview of various theories proposed during the past five decades to describe the enzymatic hydrolysis of cellulose highlighting the major shifts that these theories have undergone. It also describes the effect of the cellulose-binding domain (CBD) of an exoglucanase/xylanase from bacterium Cellulomonas fimi on the enzymatic hydrolysis of Avicel. Pretreatment of Avicel with CBDCex at 4 and 37°C as well as simultaneous addition of CBDCex to the hydrolytic enzyme (Celluclast, Novo, Nordisk) reduced the initial rate of hydrolysis owing to irreversible binding of CBD proteins to the substrate's binding sites. Nonetheless, near complete hydrolysis was achieved even in the presence of CBDCex. Protease treatment of both pure and CBDCex-treated Avicel reduced the substrates' hydrolyzability, perhapsowing to proteolysis of the hydrolyzing enzyme (Celluclast) by the residual Proteinase K remaining in the substrate. Better protocols for comptete removal of CBD proteins from the substrate need to be developed to investigate the effect of CBD adsorption on cellulose digestibility.

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References

  1. Tolan, J. S. and Foody, B. (1999), Adv. Biochem. Eng./Biotechnol. 65, 41–67.

    CAS  Google Scholar 

  2. Cavaco-Paulo, A. (1998), in Enzyme Applications in Fiber Processing, Eriksson, K. E. and Cavaco-Paulo, A., eds., ACS Symposium Series 687, American Chemical Society, Washington, DC, pp. 180–189.

    Google Scholar 

  3. Csiszar, E., Szakacs, G., and Rusznak, I. (1998), in Enzyme Applications in Fiber Processing, Eriksson, K. E. and Cavaco-Paulo, A., eds., ACS Symposium Series 687, American Chemical Society, Washington, DC, pp. 204–211.

    Google Scholar 

  4. Eriksson, L., Heitmann, J., and Venditti, R. (1998), in Enzyme Applications in Fiber Processing, Eriksson, K. E. and Cavaco-Paulo, A., eds., ACS Symposium Series 687, American Chemical Society, Washington, DC, pp. 41–54.

    Google Scholar 

  5. Mansfield, S., Swanson, D. J., Roberts, N., Olson, J., and Saddler, J. (1999). Tappi 5, 152–158.

    Google Scholar 

  6. Sheehan, J. and Himmel, M. (1999), Biotechnol. Prog. 15, 817–827.

    Article  CAS  Google Scholar 

  7. Mansfield, S., Mooney, C., and Saddler, J. N. (1999), Biotechnol. Prog. 15, 804–816.

    Article  CAS  Google Scholar 

  8. Boussaid, A. and Saddler, J. (1999), Enzyme Microb. Technol. 24, 138–143.

    Article  CAS  Google Scholar 

  9. Yu, A., Lee, D., and Saddler, J. (1995), Biotechnol. Appl. Biochem. 21, 203–216.

    CAS  Google Scholar 

  10. Reese, E. T., Siu, R. G. H., and Levinson, H. S. (1950), J. Bacteriol. 59, 485–497.

    CAS  Google Scholar 

  11. Wood, T. and McCrae, S. (1972), Biochem. J. 128, 1183.

    CAS  Google Scholar 

  12. Wood, T. and McCrae, S. (1979), in Hydrolysis of Cellulose: Mechanism of Enzymatic and Acid Catalysis, Brown, R. D. and Jurasek, L., eds., ACS Series 181, American Chemical Society, Washington, DC, pp. 181–209.

    Google Scholar 

  13. Coughlan, M. (1985), Biotechn. Genet. Eng. Rev. 3, 39–109.

    CAS  Google Scholar 

  14. Koenigs, J. W. (1975), Biotech. Bioeng. Symp. 5, 151–159.

    CAS  Google Scholar 

  15. Griffin, H., Dintzis, F. R., Krull, L., and Baker, F. L. (1984), Biotech. Bioeng. 26, 296–300.

    Article  CAS  Google Scholar 

  16. Chanzy, H., Henrissat, B., Vuong, R., and Schulein, M. (1983), FEBS Lett. 15, 113–117.

    Article  Google Scholar 

  17. Krull, L., Dintzis, F., Griffin, H., and Baker, F. (1988), Biotech. Bioeng. 31, 321–327.

    Article  CAS  Google Scholar 

  18. Woodward, J., Affholter, K., Noles, K., Troy, N., and Gaslightwala, S. (1992), Enzyme Microb. Technol. 14, 625–630.

    Article  CAS  Google Scholar 

  19. Banka, R., Mishra, S., and Ghose, T. (1998), World J. Microbiol. Biotechnol. 14, 551–558.

    Article  CAS  Google Scholar 

  20. Din, N., Gilkes, N., Tekant, B., Miller, R., Warren, R., and Kilburn, D. (1991), Bio/Technology 9, 1096–1099.

    Article  CAS  Google Scholar 

  21. Klyosov, A., Mitkevich, O., and Sinitsyn, A. (1986), Biochemistry 25, 540–542.

    Article  CAS  Google Scholar 

  22. Klyosov, A. (1990), Biochem. 29(47), 10,577–10,585.

    CAS  Google Scholar 

  23. Wood, T. (1989), in Enzyme Systems for Lignocellulose Degradation, Coughlan, M. P., ed., Elsevier, London, pp. 17–36.

    Google Scholar 

  24. Swanson, B. A., Ward, M., Pentilla, M., and Saloheimo, M. (1999), International Patent, WO 99/02693.

  25. Teeri, T., Reinikainen, T., and Ruohonen, L. (1992), J. Biotechnol. 24, 169–176.

    Article  CAS  Google Scholar 

  26. Jervis, E. J., Haynes, C. A., and Kilburn, D. G. (1997), J. Biol. Chem. 272, 24,016–24,023.

    Article  CAS  Google Scholar 

  27. McGhee, J. D. and von Hippel, P. H. (1974), J. Mol. Biol. 86, 460–489.

    Article  Google Scholar 

  28. Creagh, L., Ong, E., Jervis, E., Kilburn, D., and Haynes, C. (1996), Proc. Natl. Acad. Sci. USA 93, 12,229–12,234.

    Article  CAS  Google Scholar 

  29. Gilkes, N. R., Warren, R., Miller, R. C., and Kilburn, D. G. (1988), J. Biol. Chem. 263, 10,401–10,407.

    CAS  Google Scholar 

  30. Tomme, P., Boraston, A., McLean, B., Kormos, J., Creagh, A., Sturch, K., Gilkes, N., Haynes, C., Warren, R., and Kilbrun, D. (1998), J. Chromatogr. B. 715, 283–296.

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Wood Science, 4th Floor, Forest Sciences Center, The University of British Columbia, V6T 1Z4, Vancouver, British Columbia, Canada

    Ali R. Esteghlalian (Chair of Forest Products Biotechnology) & John N. Saddler

  2. Department of Microbiology and Immunology, The University of British Columbia, V6T 1Z4, Vancouver, British Columbia, Canada

    Vinit Srivastava, Neil R. Gilkes, Douglas G. Kilburn, R. Antony J. Warren & John N. Saddler

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  1. Ali R. Esteghlalian
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  2. Vinit Srivastava
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  3. Neil R. Gilkes
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  4. Douglas G. Kilburn
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  5. R. Antony J. Warren
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  6. John N. Saddler
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Correspondence to John N. Saddler.

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Esteghlalian, A.R., Srivastava, V., Gilkes, N.R. et al. Do cellulose binding domains increase substrate accessibility?. Appl Biochem Biotechnol 91, 575–592 (2001). https://doi.org/10.1385/ABAB:91-93:1-9:575

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  • DOI: https://doi.org/10.1385/ABAB:91-93:1-9:575

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