Advanced search

Coexpression of the Bacillus pumilus β-xylosidase (xynB) gene with the Trichoderma reesei β-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae

Author
Organization
Abstract
The xynB gene encoding the Bacillus pumilus beta-xylosidase was expressed separately and jointly with the Trichoderma reesei beta-xylanase (xyn2) gene in the yeast Saccharomyces cerevisiae. Both genes were placed under the transcriptional control of the glucose-derepressible alcohol dehydrogenase 2 promoter (ADH2(p)) and terminator (ADH2(T)) sequences. The xynB gene was fused in frame to the yeast mating factor al secretion sequence (MF alpha 1(s)) to effect secretion in S. cerevisiae. The fusion protein was designated Xlo1. Xlo1 produced in S. cerevisiae exhibited low affinity for xylobiose, but eventually hydrolyzed xylobiose and xylotriose to the monomeric constituent, D-xylose. Coproduction of: Xyn2 and Xlo1 by S. cerevisiae led to a 25% increase in the amount of reducing sugars released from birchwood xylan compared to S. cerevisiae producing only the Xyn2 beta-xylanase. However, no D-xylose was produced from birchwood xylan, presumably due to very low Xlo1 beta-xylosidase activity and its low affinity for xylobiose.
Keywords
EXPRESSION, CLONING, XYLOSE

Citation

Please use this url to cite or link to this publication:

Chicago
La Grange, DC, Marc Claeyssens, IS Pretorius, and WH Van Zyl. 2000. “Coexpression of the Bacillus Pumilus Β-xylosidase (xynB) Gene with the Trichoderma Reesei Β-xylanase 2 (xyn2) Gene in the Yeast Saccharomyces Cerevisiae.” Applied Microbiology and Biotechnology 54 (2): 195–200.
APA
La Grange, D., Claeyssens, M., Pretorius, I., & Van Zyl, W. (2000). Coexpression of the Bacillus pumilus β-xylosidase (xynB) gene with the Trichoderma reesei β-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 54(2), 195–200.
Vancouver
1.
La Grange D, Claeyssens M, Pretorius I, Van Zyl W. Coexpression of the Bacillus pumilus β-xylosidase (xynB) gene with the Trichoderma reesei β-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 2000;54(2):195–200.
MLA
La Grange, DC, Marc Claeyssens, IS Pretorius, et al. “Coexpression of the Bacillus Pumilus Β-xylosidase (xynB) Gene with the Trichoderma Reesei Β-xylanase 2 (xyn2) Gene in the Yeast Saccharomyces Cerevisiae.” APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 54.2 (2000): 195–200. Print.
@article{172297,
  abstract     = {The xynB gene encoding the Bacillus pumilus beta-xylosidase was expressed separately and jointly with the Trichoderma reesei beta-xylanase (xyn2) gene in the yeast Saccharomyces cerevisiae. Both genes were placed under the transcriptional control of the glucose-derepressible alcohol dehydrogenase 2 promoter (ADH2(p)) and terminator (ADH2(T)) sequences. The xynB gene was fused in frame to the yeast mating factor al secretion sequence (MF alpha 1(s)) to effect secretion in S. cerevisiae. The fusion protein was designated Xlo1. Xlo1 produced in S. cerevisiae exhibited low affinity for xylobiose, but eventually hydrolyzed xylobiose and xylotriose to the monomeric constituent, D-xylose. Coproduction of: Xyn2 and Xlo1 by S. cerevisiae led to a 25\% increase in the amount of reducing sugars released from birchwood xylan compared to S. cerevisiae producing only the Xyn2 beta-xylanase. However, no D-xylose was produced from birchwood xylan, presumably due to very low Xlo1 beta-xylosidase activity and its low affinity for xylobiose.},
  author       = {La Grange, DC and Claeyssens, Marc and Pretorius, IS and Van Zyl, WH},
  issn         = {0175-7598},
  journal      = {APPLIED MICROBIOLOGY AND BIOTECHNOLOGY},
  keyword      = {EXPRESSION,CLONING,XYLOSE},
  language     = {eng},
  number       = {2},
  pages        = {195--200},
  title        = {Coexpression of the Bacillus pumilus \ensuremath{\beta}-xylosidase (xynB) gene with the Trichoderma reesei \ensuremath{\beta}-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae},
  volume       = {54},
  year         = {2000},
}

Web of Science
Times cited: