Efficient secretion of two fungal cellobiohydrolases by Saccharomyces cerevisiae

Merja E. Penttilä*, Lars André, Päivi Lehtovaara, Michael Bailey, Tuula T. Teeri, Jonathan K.C. Knowles

*Corresponding author for this work

    Research output: Contribution to journalArticleScientificpeer-review

    156 Citations (Scopus)

    Abstract

    Two different cellobiohydrolases, CBHI and CBHII, of the filamentous fungus Trichoderma reesei both hydrolyse highly crystalline cellulose. Cellulolytic strains of the yeast Saccharomyces cerevisiae were constructed by transferring cDNAs coding for these enzymes into yeast on an expression plasmid. These cellulolytic yeasts were able to secrete efficiently the large, heterologous proteins to the culture medium. The recombinant cellulases were observed to be heterogeneous in Mr due, at least partly, to variable N-glycosylation. Recombinant CBHII was able to bind to crystalline cellulose, although slightly less efficiently than the native enzyme. Both of the two recombinant cellulases were able to degrade amorphous cellulose. In a fermenter cultivation, around 100 μg/ml of CBHII was secreted into the yeast growth medium.

    Original languageEnglish
    Pages (from-to)103-112
    JournalGene
    Volume63
    Issue number1
    DOIs
    Publication statusPublished - 15 Mar 1988
    MoE publication typeA1 Journal article-refereed

    Keywords

    • cellulases
    • cellulolytic yeast
    • glycosylation
    • Recombinant DNA

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