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 language | English |
|---|---|
| Pages (from-to) | 103-112 |
| Journal | Gene |
| Volume | 63 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 15 Mar 1988 |
| MoE publication type | A1 Journal article-refereed |
Funding
We thank Drs. S. and A. Kingsman and their colleagues for providing the expression vector pMA91 and the yeast host strain. Dr. Marja-Leena Niku-Paavola is thanked for many useful discussions and for providing the antisera and Drs. M. Claeyssens and H. van Tilbeurgh for their gifts of substratesa nd much good advice. The skilled technical assistance of Pirkko Veijola-Bailey and Kariitta Berg is warmly acknowledged. This study was supported by the Neste Oy Foundation, Oy Alko Ab and the Biotechnical Foundation (Sweden).
Keywords
- cellulases
- cellulolytic yeast
- glycosylation
- Recombinant DNA
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