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Purification of cellobiohydrolase I fromTrichoderma reesei using monoclonal antibodies in an immunomatrix

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Journal of Industrial Microbiology

Summary

The several components of the fungal cellulase system present practical problems in devising facile and efficient schemes for their purification. We report on a new single-step affinity chromatographic method for purification of cellobiohydrolase I ofTrichoderma reesei based on its selective absorption and elution using an immunomatrix constructed with CnBr-activated Sepharose 4B and monoclonal antibody specific for the enzyme. Isoenzymes of cellobiohydrolase I were purified directly from crude culture filtrate. The method is fast, simple, and of high resolution.

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Authors and Affiliations

  1. Department of Biochemistry and Microbiology, Cook College, New Jersey Agricultural Experiment Station, Rutgers University, P.O. Box 231, 08903, New Brunswick, NJ, U.S.A.

    F. J. Riske, D. E. Eveleigh & J. D. Macmillan

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  1. F. J. Riske
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  2. D. E. Eveleigh
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  3. J. D. Macmillan
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Riske, F.J., Eveleigh, D.E. & Macmillan, J.D. Purification of cellobiohydrolase I fromTrichoderma reesei using monoclonal antibodies in an immunomatrix. Journal of Industrial Microbiology 1, 259–264 (1986). https://doi.org/10.1007/BF01569280

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  • DOI: https://doi.org/10.1007/BF01569280

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