期刊
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
卷 162, 期 3, 页码 617-624出版社
SPRINGER
DOI: 10.1007/s12010-009-8880-9
关键词
Gene expression; Signal peptide; Endoglucanase I; Yeast
资金
- National Natural Science Foundation of China [50673078]
- Ministry of Science and Technology [2007AA022004]
- Shanghai Municipal Education Commission [08ZZ21]
- Anhui Agricultural university [yj2008-25]
Ethanol production from lignocellulose by recombinant yeast with high level expression of heterologous cellulase genes has been a major anticipation. The native secretion signal sequence of the cellulase endoglucanase I (eg1) gene was replaced by Saccharomyces cerevisiae mating factor alpha prepro-leader sequence (MF alpha). The transformants containing native secretion signal (Y (1)) and MF alpha secretion signal (Y (2)) were characterized with respect to gene expression and growth on cellulose substrate. Increased enzyme activity and cellulose utilization were observed. The enzyme activity of Y (2) was 0.084 U/ml, 61.5% higher than Y (1) (0.052 U/ml). The sufficiency parameter (S value) was raised from 0.6 to 0.84. MF alpha signal peptide was more efficient than the native signal peptide of eg1 gene, suggesting that signal peptide replacement is an efficient way to enhance the cellulase expression level in yeast, for cellulose-derived ethanol production.
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