Application of dioldehydrase gene pduCDE

Abstract

The invention discloses application of dioldehydrase gene pduCDE, and particularly discloses application of engineering bacteria containing the gene to preparation of 3-hydroxypropionic acid, 1,3-propylene glycol and 3-hydroxypropionic acid with fermented glycerinum. The gene is expressed successfully in escherichia coli for the first time, and an encoded enzyme of the gene can be used for catalyzing dehydration of the glycerinum to generate 3-hydroxy-propionaldehyde. On the basis of the application, a 1,3-propylene oxidordeuctase gene or an adlehyde dehydrogenase gene can be recombined into escherichia coli, and recombinant bacteria can transform the glycerinum into 1,3-propylene glycol or 3-hydracrylic acid through fermentation.

Description

technical field [0001] The invention belongs to the technical field of genetic engineering and fermentation engineering, in particular to the application of a diol dehydratase gene pduCDE. Background technique [0002] Diol dehydratase (Dioldehydratase, EC4.2.1.28) and glycerol dehydratase (Glyceroldehydratase, EC4.2.1.30) are isoenzymes, which can use glycerol, 1,2-propanediol or 1,2-ethylene glycol as Substrates are transformed into important chemical raw materials 3-hydroxypropionaldehyde, propionaldehyde or acetaldehyde. The most noteworthy thing is that this enzyme is the rate-limiting enzyme and key to catalyze the dehydration of glycerol to generate the important intermediate product 3-hydroxypropionaldehyde Enzymes (Lee H.A., J.R. and Abeles R.H., 1963, Purification and properties of dioldehydrase, and enzyme requiring acobamidecoenzyme, J. Biol. Chem., 238: 2367-2373). Because 3-hydroxypropionaldehyde can be used as an antibacterial agent for food preservation, it ...

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Problems solved by technology

Although their research team isolated, purified and studied the enzymatic properties of the diol dehydratase in the natural bacteria, however, when the diol dehydratase gene cloned from the strain was expressed in Escherichia coli, no matter what expression conditions and method, did not detect the activity of the enzyme, which may be due to the limitation of fermentation conditions or the lack of some modification systems in Escherichia coli, so that some foreign proteins cannot be folded correctly, which seriously limits the further research and application of this dehydratase (NicolasS , VianneyP, Lo1cL, et.al.2002. Purification, characterization and subunit identification of thedioldehydratase of Lactobacillus collinoides. Eur. J. Biochem. 269: 5731 ~ 5737.)

[0008] So far, no papers or patents related to the successful cloning, expression and application of the diol dehydratase gene of Lactobacillus collinoides in Escherichia coli have been retrieved, nor have any papers or patents on the use of this recombinant enzyme to convert glycerol to prepare 3-hydroxypropanol Literature on Aldehydes, 1,3-Propanediol, and 3-Hydroxypropionic Acid

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