scholarly journals Enhancement of lactate fraction in poly(lactate-co-3-hydroxybutyrate) synthesized by Escherichia coli harboring the D-lactate dehydrogenase gene from Lactobacillus acetotolerans HT

2019 ◽  
Vol 65 (4) ◽  
pp. 204-208 ◽  
Author(s):  
Saki Goto ◽  
Naoyuki Suzuki ◽  
Ken'ichiro Matsumoto ◽  
Seiichi Taguchi ◽  
Kenji Tanaka ◽  
...  
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.


ISRN Zoology ◽  
2011 ◽  
Vol 2011 ◽  
pp. 1-5 ◽  
Author(s):  
Yoshikazu Nishiguchi ◽  
Akira Uchida ◽  
Noriko Oshima ◽  
Mitsumasa Okada

Amplified Eptatretus okinoseanus cDNA was digested with NdeI and EcoRI, cloned into pCold trigger factor (TF), and transformed with Escherichia coli strain BL 21 in which a csp A promoter was introduced to inhibit the expression of foreign peptides. Recombinant lactate dehydrogenase (LDH) was obtained in the soluble fraction after sonication of the cells. The protein was digested by HRC 3C protease, thrombin, and factor Xa. The specific activity of TF-tagged protein and tagless protein were  mIU/mg and  mIU/mg, respectively. The deletion of the TF tag enhanced the activity compared with the native protein to  mIU/mg, showing that this expression method is effective for the mass production of the protein to allow further study of the structure of LDH.


1992 ◽  
Vol 208 (3) ◽  
pp. 799-805 ◽  
Author(s):  
Sunil KOCHHAR ◽  
Herbert HOTTINGER ◽  
Nathalie CHUARD ◽  
Paul G. TAYLOR ◽  
Tony ATKINSON ◽  
...  

2013 ◽  
Vol 12 (1) ◽  
pp. 166 ◽  
Author(s):  
Hyun-Il Shin ◽  
Jung-Yeon Kim ◽  
Won-Ja Lee ◽  
Youngjoo Sohn ◽  
Sang-Wook Lee ◽  
...  

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