Purification and characterization of recombinant Escherichia coli-expressed Pichia etchellsii ?-glucosidase II with high hydrolytic activity on sophorose

2004 ◽  
Vol 66 (5) ◽  
pp. 527-535 ◽  
Author(s):  
Yukti Bhatia ◽  
Saroj Mishra ◽  
Virendra S. Bisaria
1986 ◽  
Vol 160 (3) ◽  
pp. 491-497 ◽  
Author(s):  
Paul WINGFIELD ◽  
Mark PAYTON ◽  
Jean TAVERNIER ◽  
Marjory BARNES ◽  
Alan SHAW ◽  
...  

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).


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