Production of optically pure l-phenyllactic acid by using engineered Escherichia coli coexpressing l-lactate dehydrogenase and formate dehydrogenase

2015 ◽  
Vol 207 ◽  
pp. 47-51 ◽  
Author(s):  
Zhaojuan Zheng ◽  
Mingyue Zhao ◽  
Ying Zang ◽  
Ying Zhou ◽  
Jia Ouyang
1999 ◽  
Vol 65 (4) ◽  
pp. 1384-1389 ◽  
Author(s):  
Dong-Eun Chang ◽  
Heung-Chae Jung ◽  
Joon-Shick Rhee ◽  
Jae-Gu Pan

ABSTRACT We investigated metabolic engineering of fermentation pathways inEscherichia coli for production of optically pured- or l-lactate. Several pta mutant strains were examined, and a pta mutant of E. coli RR1 which was deficient in the phosphotransacetylase of the Pta-AckA pathway was found to metabolize glucose tod-lactate and to produce a small amount of succinate by-product under anaerobic conditions. An additional mutation inppc made the mutant produce d-lactate like a homofermentative lactic acid bacterium. When the pta ppcdouble mutant was grown to higher biomass concentrations under aerobic conditions before it shifted to the anaerobic phase ofd-lactate production, more than 62.2 g ofd-lactate per liter was produced in 60 h, and the volumetric productivity was 1.04 g/liter/h. To examine whether the blocked acetate flux could be reoriented to a nonindigenousl-lactate pathway, an l-lactate dehydrogenase gene from Lactobacillus casei was introduced into apta ldhA strain which lacked phosphotransacetylase andd-lactate dehydrogenase. This recombinant strain was able to metabolize glucose to l-lactate as the major fermentation product, and up to 45 g of l-lactate per liter was produced in 67 h. These results demonstrate that the central fermentation metabolism of E. coli can be reoriented to the production of d-lactate, an indigenous fermentation product, or to the production of l-lactate, a nonindigenous fermentation product.


2013 ◽  
Vol 12 (1) ◽  
pp. 57 ◽  
Author(s):  
Jinfang Zhao ◽  
Liyuan Xu ◽  
Yongze Wang ◽  
Xiao Zhao ◽  
Jinhua Wang ◽  
...  

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