scholarly journals Major Role of NAD-Dependent Lactate Dehydrogenases in the Production of l-Lactic Acid with High Optical Purity by the Thermophile Bacillus coagulans

2014 ◽  
Vol 80 (23) ◽  
pp. 7134-7141 ◽  
Author(s):  
Limin Wang ◽  
Yumeng Cai ◽  
Lingfeng Zhu ◽  
Honglian Guo ◽  
Bo Yu

ABSTRACTBacillus coagulans2-6 is an excellent producer of optically purel-lactic acid. However, little is known about the mechanism of synthesis of the highly optically purel-lactic acid produced by this strain. Three enzymes responsible for lactic acid production—NAD-dependentl-lactate dehydrogenase (l-nLDH; encoded byldhL), NAD-dependentd-lactate dehydrogenase (d-nLDH; encoded byldhD), and glycolate oxidase (GOX)—were systematically investigated in order to study the relationship between these enzymes and the optical purity of lactic acid.Lactobacillus delbrueckiisubsp.bulgaricusDSM 20081 (ad-lactic acid producer) andLactobacillus plantarumsubsp.plantarumDSM 20174 (adl-lactic acid producer) were also examined in this study as comparative strains, in addition toB. coagulans. The specific activities of key enzymes for lactic acid production in the three strains were characterizedin vivoandin vitro, and the levels of transcription of theldhL,ldhD, and GOX genes during fermentation were also analyzed. The catalytic activities ofl-nLDH andd-nLDH were different inl-,d-, anddl-lactic acid producers. Onlyl-nLDH activity was detected inB. coagulans2-6 under native conditions, and the level of transcription ofldhLinB. coagulans2-6 was much higher than that ofldhDor the GOX gene at all growth phases. However, for the twoLactobacillusstrains used in this study,ldhDtranscription levels were higher than those ofldhL. The high catalytic efficiency ofl-nLDH toward pyruvate and the high transcription ratios ofldhLtoldhDandldhLto the GOX gene provide the key explanations for the high optical purity ofl-lactic acid produced byB. coagulans2-6.

2016 ◽  
Vol 211 ◽  
pp. 398-405 ◽  
Author(s):  
Anna-Katrin Neu ◽  
Daniel Pleissner ◽  
Kerstin Mehlmann ◽  
Roland Schneider ◽  
Gloria Inés Puerta-Quintero ◽  
...  

2010 ◽  
Vol 77 (5) ◽  
pp. 1892-1895 ◽  
Author(s):  
Mohamed Ali Abdel-Rahman ◽  
Yukihiro Tashiro ◽  
Takeshi Zendo ◽  
Katsuhiro Hanada ◽  
Keisuke Shibata ◽  
...  

ABSTRACTEnterococcus mundtiiQU 25, a newly isolated lactic acid bacterium, efficiently metabolized xylose intol-lactate. In batch fermentations, the strain produced 964 mMl-(+)-lactate from 691 mM xylose, with a yield of 1.41 mol/mol xylose consumed and an extremely high optical purity of ≥99.9% without acetate production.


2017 ◽  
Vol 66 (2) ◽  
pp. 273-276 ◽  
Author(s):  
Guoping Lv ◽  
Chengchuan Che ◽  
Li Li ◽  
Shujing Xu ◽  
Wanyi Guan ◽  
...  

The traditional CaCO3-based fermentation process generates huge amount of insoluble waste. To solve this problem, we have developed an efficient and green D-lactic acid fermentation process by using ammonia as neutralizer. The 106.7 g/l of D-lactic acid production and 0.89 g/g of consumed sugar were obtained by Sporolactobacillus inulinus CASD with a high optical purity of 99.7% by adding 100 mg/l betaine in the simple batch fermentation. The addition of betaine was experimentally proven to protect cell at high concentration of ammonium ion, increase the D-lactate dehydrogenase specific activity and thus promote the production of D-lactic acid.


2015 ◽  
Vol 82 (4) ◽  
pp. 1295-1304 ◽  
Author(s):  
S. Andreas Angermayr ◽  
Aniek D. van der Woude ◽  
Danilo Correddu ◽  
Ramona Kern ◽  
Martin Hagemann ◽  
...  

ABSTRACTBoth enantiomers of lactic acid,l-lactic acid andd-lactic acid, can be produced in a sustainable way by a photosynthetic microbial cell factory and thus from CO2, sunlight, and water. Several properties of polylactic acid (a polyester of polymerized lactic acid) depend on the controlled blend of these two enantiomers. Recently, cyanobacteriumSynechocystissp. strain PCC6803 was genetically modified to allow formation of either of these two enantiomers. This report elaborates on thed-lactic acid production achieved by the introduction of ad-specific lactate dehydrogenase from the lactic acid bacteriumLeuconostoc mesenteroidesintoSynechocystis. A typical batch culture of this recombinant strain initially shows lactic acid production, followed by a phase of lactic acid consumption, until production “outcompetes” consumption at later growth stages. We show thatSynechocystisis able to used-lactic acid, but notl-lactic acid, as a carbon source for growth. Deletion of the organism's putatived-lactate dehydrogenase (encoded byslr1556), however, does not eliminate this ability with respect tod-lactic acid consumption. In contrast,d-lactic acid consumption does depend on the presence of glycolate dehydrogenase GlcD1 (encoded bysll0404). Accordingly, this report highlights the need to match a product of interest of a cyanobacterial cell factory with the metabolic network present in the host used for its synthesis and emphasizes the need to understand the physiology of the production host in detail.


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