Abstract
We report the cloning, partial characterization, and expression in yeast of the endoglucanase I (EGI) gene from Trichoderma reesei. DNA sequencing revealed significant homology at the amino acid level between EGI and exocellobiohydrolase I (CBHI), but there are differences in codon utilization at homologous amino acids and in the intron/exon structure. These possibly reflect a mechanism for preventing recombination between closely related genes of the cellulase family. The coding sequence for the mature protein with its signal peptide was inserted into an expression plasmid containing yeast transcription control sequences. Yeast colonies transformed with this plasmid secrete enzymatically active hyperglycosylated EGI to the culture medium. This novel glycosylation appears to render the enzyme more resistant to thermal inactivation.
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Van Arsdell, J., Kwok, S., Schweickart, V. et al. Cloning, Characterization, and Expression in Saccharomyces Cerevisiae of Endoglucanase I from Trichoderma Reesei. Nat Biotechnol 5, 60–64 (1987). https://doi.org/10.1038/nbt0187-60
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DOI: https://doi.org/10.1038/nbt0187-60
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