Heat-shock transformation of Escherichia coli in nanolitre droplets formed in a capillary-composited microfluidic device

2011 ◽  
Vol 3 (9) ◽  
pp. 1988 ◽  
Author(s):  
Jun Sha ◽  
Yaolei Wang ◽  
Jianchun Wang ◽  
Wenming Liu ◽  
Qin Tu ◽  
...  
2011 ◽  
Vol 112 (4) ◽  
pp. 373-378 ◽  
Author(s):  
Jun Sha ◽  
Yaolei Wang ◽  
Jianchun Wang ◽  
Li Ren ◽  
Qin Tu ◽  
...  

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).


1988 ◽  
Vol 263 (24) ◽  
pp. 11718-11728 ◽  
Author(s):  
D T Chin ◽  
S A Goff ◽  
T Webster ◽  
T Smith ◽  
A L Goldberg

1998 ◽  
Vol 30 (3) ◽  
pp. 583-593 ◽  
Author(s):  
Takashi Tatsuta ◽  
Toshifumi Tomoyasu ◽  
Bernd Bukau ◽  
Masanari Kitagawa ◽  
Hirotada Mori ◽  
...  

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