Engineering the <i>N</i>-terminal end of CelA results in improved performance and growth of <i>Caldicellulosiruptor bescii</i> on crystalline cellulose [electronic resource]

• Tác giả: National Renewable Energy Laboratory (U.S.), United States, United States. Dept. of Energy. Office of Science
• Ngôn ngữ: eng
• Ký hiệu phân loại: 620.1 Engineering mechanics and materials
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2016
• Mô tả vật lý: Size: p. 945-950 : , digital, PDF file.
• Bộ sưu tập: Báo, Tạp chí
• ID: 263335
• Chủ đề: 1. 09 biomass fuels; 2. Biomass deconstruction; 3. Caldicellulosiruptior; 4. Cela; 5. Repeated aspartate residues

Tóm tắt

 Here, CelA is the most abundant enzyme secreted by <
 i>
 Caldicellulosiruptor bescii<
 /i>
  and has been shown to outperform mixtures of commercially available exo- and endoglucanases in vitro. CelA contains both a glycoside hydrolase family 9 endoglucanase and a glycoside hydrolase family 48 exoglucanase known to be synergistic in their activity, connected by three cellulose-binding domains via linker peptides. Here, repeated aspartate residues were introduced into the <
 i>
 N<
 /i>
 -terminal ends of CelA GH9 and GH48 domains to improve secretion efficiency and/or catalytic efficiency of CelA. Among several constructs, the highest activity on carboxymethylcellulose (CMC), 0.81 � 0.03 mg/mL was observed for the <
 i>
 C. bescii<
 /i>
  strain containing CelA with 5-aspartate tag at the N-terminal end of GH9 domain ? an 82% increase over wild type CelA. In addition, Expression of CelA with <
 i>
 N<
 /i>
 -terminal repeated aspartate residues in <
 i>
 C. bescii<
 /i>
  results in a dramatic increase in its ability to grow on Avicel.