Organization and Sequence of Histidine Biosynthesis Genes hisH , -A , -F , and -IE in Thermoanaerobacter ethanolicus

2000 ◽  
Vol 40 (2) ◽  
pp. 140-142 ◽  
Author(s):  
Milutin Erbeznik ◽  
Herbert J. Strobel ◽  
Karl A. Dawson
2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity

Biologia ◽  
2009 ◽  
Vol 64 (6) ◽  
Author(s):  
Yue-Hong Wang ◽  
Yu Jiang ◽  
Zuo-Ying Duan ◽  
Wei-Lan Shao ◽  
Hua-Zhong Li

AbstractIn this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70°C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70°C, pH 5.5), K m and V max of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).


1964 ◽  
Vol 239 (6) ◽  
pp. 1848-1855 ◽  
Author(s):  
David W.E. Smith ◽  
Bruce N. Ames

1994 ◽  
Vol 269 (20) ◽  
pp. 14386-14390
Author(s):  
G. Rieder ◽  
M.J. Merrick ◽  
H. Castorph ◽  
D. Kleiner

1973 ◽  
Vol 123 (3) ◽  
pp. 225-232 ◽  
Author(s):  
Serena Russi ◽  
A. Carere ◽  
Alessandra Siracusano ◽  
A. Ballio

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