Abstract
Heterologous secretory expression of endoglucanase E (Clostridium thermocellum) and β-glucosidase 1 (Saccharomycopsis fibuligera) was achieved in Saccharomyces cerevisiae fermentation cultures as an α-mating factor signal peptide fusion, based on the native enzyme coding sequence. Ethanol production depends on simultaneous saccharification of cellulose to glucose and fermentation of glucose to ethanol by a recombinant yeast strain as a microbial biocatalyst. Recombinant yeast strain expressing endoglucanase and β-glucosidase was able to produce ethanol from β-glucan, CMC and acid swollen cellulose. This indicates that the resultant yeast strain of this study acts efficiently as a whole cell biocatalyst.
Original language | English |
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Pages (from-to) | 369-373 |
Number of pages | 5 |
Journal | Molecules and cells |
Volume | 28 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- Beta-glucosidase
- Cellulose degradation
- Clostridium thermocellum
- Endoglucanase
- Ethanol production
- Extracellular expression
- Saccharomyces cerevisiae
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology