التفاصيل البيبلوغرافية
| العنوان: |
Efficient Production of (R)-2-Hydroxy-4-Phenylbutyric Acid by Using a Coupled Reconstructed d-Lactate Dehydrogenase and Formate Dehydrogenase System. |
| المؤلفون: |
Sheng, Binbin1, Zheng, Zhaojuan2, Lv, Min1, Zhang, Haiwei1, Qin, Tong1, Gao, Chao1, Ma, Cuiqing1, Xu, Ping1 |
| المصدر: |
PLoS ONE. Aug2014, Vol. 9 Issue 8, p1-6. 6p. |
| مصطلحات موضوعية: |
*BUTYRIC acid, *LACTATE dehydrogenase, *ACE inhibitors, *FORMATES, *NAD (Coenzyme), *CATALYSIS, *INDUSTRIAL microbiology |
| مستخلص: |
Background: (R)-2-Hydroxy-4-phenylbutyric acid [(R)-HPBA] is a key precursor for the production of angiotensin-converting enzyme inhibitors. However, the product yield and concentration of reported (R)-HPBA synthetic processes remain unsatisfactory. Methodology/Principal Findings: The Y52L/F299Y mutant of NAD-dependent d-lactate dehydrogenase (d-nLDH) in Lactobacillus bulgaricus ATCC 11842 was found to have high bio-reduction activity toward 2-oxo-4-phenylbutyric acid (OPBA). The mutant d-nLDHY52L/F299Y was then coexpressed with formate dehydrogenase in Escherichia coli BL21 (DE3) to construct a novel biocatalyst E. coli DF. Thus, a novel bio-reduction process utilizing whole cells of E. coli DF as the biocatalyst and formate as the co-substrate for cofactor regeneration was developed for the production of (R)-HPBA from OPBA. The biocatalysis conditions were then optimized. Conclusions/Significance: Under the optimum conditions, 73.4 mM OPBA was reduced to 71.8 mM (R)-HPBA in 90 min. Given its high product enantiomeric excess (>99%) and productivity (47.9 mM h−1), the constructed coupling biocatalysis system is a promising alternative for (R)-HPBA production. [ABSTRACT FROM AUTHOR] |
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