Secretion of thermophilic bacterial cellobiohydrolase in Saccharomyces cerevisiae

Nobuyuki Uozumi, Akihiro Hayashi, Takaomi Ito, Arunwanich Patthra, Ichiro Yamashita, Shinji Iijima, Takeshi Kobayashi

研究成果: Article査読

4 被引用数 (Scopus)

抄録

The partial DNA sequence corresponding to the N-terminal amino acid sequence of cellobiohydrolase derived from a thermophilic anaerobe NA10 was determined. The cellobiohydrolase gene fused to the secretion signal (signal peptide and T-S region) from Saccharomyces diastaticus was expressed in an ethanologenic yeast, S. cerevisiae YIY345, under control of the glucoamylase promoter. The recombinant yeast produced cellobiohydrolase: approximately 40% of the total cellobiohydrolase activity was detected in the medium, and the remaining cellobiohydrolase was localized in the intracellular fraction. An analysis of the N-terminal amino acid sequence of the main intracellular cellobiohydrolase revealed that the signal peptide and T-S region were removed proteolytically. Alteration of the amino acid residues at the cleavage site by insertion of a Bgl II linker led to an approximately 3.5-fold increase in the total cellobiohydrolase production, but did not affect the efficiency of secretion into the medium. Cellobiohydrolase production was not repressed in the presence of glucose. The recombinant yeast hydrolyzed carboxymethyl cellulose in the medium. The results suggest the possibility of the direct bioconversion of cellulose to ethanol by the recombinant yeast.

本文言語English
ページ(範囲)399-404
ページ数6
ジャーナルJournal of Fermentation and Bioengineering
75
6
DOI
出版ステータスPublished - 1993
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー

フィンガープリント

「Secretion of thermophilic bacterial cellobiohydrolase in Saccharomyces cerevisiae」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル