Efficient production of thermostable Thermus thermophilus xylose isomerase in Escherichia coli and Bacillus brevis

1992 ◽  
Vol 36 (6) ◽  
Author(s):  
Koen Dekker ◽  
Ayumu Sugiura ◽  
Hideo Yamagata ◽  
Kenji Sakaguchi ◽  
Shigezo Udaka
2010 ◽  
Vol 162 (3) ◽  
pp. 823-829 ◽  
Author(s):  
Toru Matsui ◽  
Takashi Togari ◽  
Satoru Misawa ◽  
Tomoyuki Namihira ◽  
Naoya Shinzato ◽  
...  

2011 ◽  
Vol 236-238 ◽  
pp. 968-973
Author(s):  
Wei Xu ◽  
Rong Shao ◽  
Yan Li ◽  
Ming Yan ◽  
Ping Kai Ouyang

Compared withThermus thermophilusHB8 xylose isomerase(TthXI), the increase of the substrate specificity on D-xylose of its N91D mutant (TthXI-N91D) was observed in the previous study. In order to clarify the structural mechanism of TthXI-N91D, the complex model of TthXI with D-xylose was constructed by molecular docking method. The TthXI-N91D homology model was built by WATH IF5.0 based on the above complex. The results indicate that the distance between the conserved residue H53 NE2 and D-xylose O5 has decreased in 0.083 nm in the TthXI-N91D active site. The short distance is propitious to transfer the hydrogen atom during the open ring process of substrate. At the same time, the distance between the conserved residue T89 OG1, involving in combining glucose, and D-xylose C5 has reduced 0.133 nm. The shrunken space has an unfavorable effect on accommodating the larger glucose than xylose, and lead to the enhanced specificity for D-xylose.The above phenomenon maybe the main reason for explaining that TthXI-N91D is easy to combine D-xylose showing enhanced specificity. The results paly an important role in understanding the catalytic mechanism of xylose isomerase and provides the base for its molecular design.


FEBS Letters ◽  
1997 ◽  
Vol 415 (2) ◽  
pp. 155-159 ◽  
Author(s):  
Natalia L Davydova ◽  
Alexey V Rak ◽  
Olga I Gryaznova ◽  
Anders Liljas ◽  
Bengt-Harald Jonsson ◽  
...  

2017 ◽  
Vol 249 ◽  
pp. 73-81 ◽  
Author(s):  
Peiching Chang ◽  
Grey S. Chen ◽  
Hsiang-Yuan Chu ◽  
Ken W. Lu ◽  
Claire R. Shen

2020 ◽  
Vol 47 (12) ◽  
pp. 1117-1132
Author(s):  
Katharina Novak ◽  
Juliane Baar ◽  
Philipp Freitag ◽  
Stefan Pflügl

AbstractThe aim of this study was to establish isobutanol production on chemically defined medium in Escherichia coli. By individually expressing each gene of the pathway, we constructed a plasmid library for isobutanol production. Strain screening on chemically defined medium showed successful production in the robust E. coli W strain, and expression vector IB 4 was selected as the most promising construct due to its high isobutanol yields and efficient substrate uptake. The investigation of different aeration strategies in combination with strain improvement and the implementation of a pulsed fed-batch were key for the development of an efficient production process. E. coli W ΔldhA ΔadhE Δpta ΔfrdA enabled aerobic isobutanol production at 38% of the theoretical maximum. Use of cheese whey as raw material resulted in longer process stability, which allowed production of 20 g l−1 isobutanol. Demonstrating isobutanol production on both chemically defined medium and a residual waste stream, this study provides valuable information for further development of industrially relevant isobutanol production processes.


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