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 |
|---|---|
| Pages (from-to) | 369-373 |
| Number of pages | 5 |
| Journal | Molecules and cells |
| Volume | 28 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2009 |
Bibliographical note
Funding Information:We thank Roy H. Doi (University of California, Davis) for critical reading of the manuscript. This work was supported in part by the Korea Science and Tngineering Foundation grant funded by the Korea Government (Ministry of Science and Technology) (No. R01-2008-000-20438-0) and National Research Foundation of Korea Grant funded by the Korea Government (2009-0073856).
Keywords
- Beta-glucosidase
- Cellulose degradation
- Clostridium thermocellum
- Endoglucanase
- Ethanol production
- Extracellular expression
- Saccharomyces cerevisiae
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology