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Characterization and Properties of Cellulases Purified from Trichoderma Reesei Strain L27

Bio/Technology volume 1, pages 687–690 (1983)Cite this article

Abstract

Trichoderma reesei strain L27 produces multiple 1,4–β–D–glucan cellobiohydrolases, endo–1,4–β–D–glucanases, and 1,4–β–D–glucosidases. The major cellobiohydrolase (CBHI) and endoglucanase (EGI) have been purified to homogeneity and a β–glucosidase (BGI) has been substantially purified. Specific antibodies have been raised against these proteins. Amino terminal protein sequencing of the first 30 amino acid residues of CBHI and EGI indicates significant homology. High pressure liquid chromatography (HPLC) analysis of tryptic peptides, however, revealed little or no homology between these two proteins.

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Authors and Affiliations

  1. Cetus Corporation, 1400 Fifty-Third Street, Emeryville, CA, 94608

    S. Shoemaker, K. Watt, G. Tsitovsky & R. Cox

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  1. S. Shoemaker
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  2. K. Watt
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  3. G. Tsitovsky
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  4. R. Cox
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Shoemaker, S., Watt, K., Tsitovsky, G. et al. Characterization and Properties of Cellulases Purified from Trichoderma Reesei Strain L27. Nat Biotechnol 1, 687–690 (1983). https://doi.org/10.1038/nbt1083-687

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