Alginate immobilization of recombinant Escherichia coli whole cells harboring l-arabinose isomerase for l-ribulose production

2009 ◽  
Vol 33 (6) ◽  
pp. 741-748 ◽  
Author(s):  
Ye-Wang Zhang ◽  
Ponnandy Prabhu ◽  
Jung-Kul Lee
2008 ◽  
Vol 74 (8) ◽  
pp. 2307-2313 ◽  
Author(s):  
Jin-Ha Kim ◽  
Byung-Chul Lim ◽  
Soo-Jin Yeom ◽  
Yeong-Su Kim ◽  
Hye-Jung Kim ◽  
...  

ABSTRACT An Escherichia coli galactose kinase gene knockout (ΔgalK) strain, which contains the l-arabinose isomerase gene (araA) to isomerize d-galactose to d-tagatose, showed a high conversion yield of tagatose compared with the original galK strain because galactose was not metabolized by endogenous galactose kinase. In whole cells of the ΔgalK strain, the isomerase-catalyzed reaction exhibited an equilibrium shift toward tagatose, producing a tagatose fraction of 68% at 37°C, whereas the purified l-arabinose isomerase gave a tagatose equilibrium fraction of 36%. These equilibrium fractions are close to those predicted from the measured equilibrium constants of the isomerization reaction catalyzed in whole cells and by the purified enzyme. The equilibrium shift in these cells resulted from the higher uptake and lower release rates for galactose, which is a common sugar substrate, than for tagatose, which is a rare sugar product. A ΔmglB mutant had decreased uptake rates for galactose and tagatose, indicating that a methylgalactoside transport system, MglABC, is the primary contributing transporter for the sugars. In the present study, whole-cell conversion using differential selectivity of the cell membrane was proposed as a method for shifting the equilibrium in sugar isomerization reactions.


2017 ◽  
Vol 125 ◽  
pp. 180-189 ◽  
Author(s):  
Alejandra B. Cardillo ◽  
María Perassolo ◽  
Mariela Sartuqui ◽  
Julián Rodríguez Talou ◽  
Ana M. Giulietti

PLoS ONE ◽  
2015 ◽  
Vol 10 (10) ◽  
pp. e0140477 ◽  
Author(s):  
Zhaojuan Zheng ◽  
Ying Xu ◽  
Ye Sun ◽  
Wending Mei ◽  
Jia Ouyang

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