A method for preparing chiral compounds containing hydroxyl groups
A chiral compound and compound technology, applied in the biological field, can solve the problems of high price, impossibility and instability of reduced coenzyme
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[0066] (1) The method for preparing (S)-1-(2,6-dichloro-3-fluorophenyl)ethanol provided by the present invention has high conversion rate, does not need to use coenzyme II, and has low preparation cost;
[0067] (2) The present invention adopts the method of biocatalysis, which is environmentally friendly, has mild conditions and stable process;
[0068] (3) Using the reaction system constructed by the co-expression strain of the present invention, under optimized enzyme expression conditions and optimized reaction conditions, the conversion rate can reach more than 90%, and the product is single, which is very easy to purify.
Embodiment 1
[0070] Embodiment 1 Construction of glucose dehydrogenase and alcohol dehydrogenase recombinant strain
[0071] Alcohol dehydrogenase gene ADH derived from Lactobacillus caucasus was codon optimized and artificially synthesized. Using the same method, the codon optimization of the glucose dehydrogenase (GDH) gene derived from Bacillus was carried out and the gene was artificially synthesized. The genes ADH and GDH were connected with pET-28a respectively, and each was introduced into E.coli BL21(DE3) to obtain recombinant bacteria E.coli BL21-ADH and E.coli BL21-GDH. The recombinant bacteria were tested for expression, and the products ADH and GDH were verified by SDS-PAGE. Finally, a series of optimizations were carried out on its expression conditions.
[0072] Experimental Materials
[0073] 1 experimental equipment
[0074] Table 1-1 Experimental Instruments
[0075]
[0076]
[0077] 2 experimental reagents
[0078] Table 1-2 Experimental Reagents
[0079] ...
Embodiment 2
[0221] Example 2 Co-expression of glucose dehydrogenase and alcohol dehydrogenase
[0222] Lactobacillus caucasus contains alcohol dehydrogenase, which can catalyze the reduction of 2,6-dichloro-3-fluoroacetophenone to (S)-1-(2,6-dichloro-3-fluorophenyl ) ethanol, but the process of this asymmetric reduction reaction requires the reduced coenzyme NADPH to provide reducing hydrogen. Therefore, when using the recombinant Escherichia coli cloned with the alcohol dehydrogenase gene to carry out the reduction reaction of 2,6-dichloro-3-fluoroacetophenone, it is necessary to add expensive NADPH or provide a high-efficiency coenzyme regeneration system. Glucose dehydrogenase can catalyze glucose to gluconic acid, and at the same time convert NAD(P) + Reduction to NAD(P)H. Using genetic engineering means, the key enzyme GDH in coenzyme regeneration and alcohol dehydrogenase ADH are coupled and expressed, and the endogenous coenzyme regeneration is also provided while catalyzing in a...
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