36 results about "Propanediol oxidoreductase" patented technology

The invention belongs to the field of biochemical industry and discloses a 1,3-propanediol-producing genetically engineered bacterium as well as a preparation method and application thereof. The strain is named Klebsiella pneumoniae ATCC 25955-pUC18-yqhD-TetR, which is composed of the 1,3-propanediol oxidoreductase isoenzyme gene yqhD from Escherichia coli and the tetracycline resistance gene TetR from the plasmid pHY300PLK, and inserted into the vector pUC18 , obtained by transforming Klebsiella pneumoniae ATCC25955. The bacteria can significantly improve the ability of glycerol to convert 1,3-propanediol, improve the utilization ability and conversion rate of the substrate glycerol, increase the final concentration of the product 1,3-propanediol, and shorten the fermentation time, which is convenient for microbial fermentation. Industrial production of 1,3-propanediol.

The invention discloses recombination klebsiella pneumonia capable of co-producing 3-HP and P3HP, and a preparation method and application thereof. The recombination bacterium is obtained by introducing glycerol dehydratase gene, glycerol dehydratase reactivation enzyme gene, aldehyde dehydrogenase gene, propionyl coenzyme A synthetase gene and polyhydroxyalkanoate synthetase gene into a host recombination klebsiella pneumonia in which 1, 3-propylene glycol oxidoreductase gene and aldehyde reductase / alcohol dehydrogenase gene are knocked out. According to the technical scheme, the production cost of 3-hydroxypropionic acid and poly(3-hydroxypropionic acid) is reduced, and 3-hydroxypropionic acid and poly(3-hydroxypropionic acid) can be synthesized at the same time by taking a same thallus as the host.

The invention relates to a genetically engineered bacterium capable of efficiently producing 1,3-propanediol and a construction method and application thereof. The present invention strengthens the expression of 1,3-propanediol oxidoreductase in Klebsiella pneumoniae to enhance the enzymatic activity of 1,3-propanediol oxidoreductase, and simultaneously constructs a NADH regeneration pathway to reduce the accumulation of 3-hydroxypropionaldehyde, Enhances the conversion of 3-hydroxypropionaldehyde to 1,3-propanediol, thereby increasing the yield of 1,3-propanediol. The enzymatic activity of the 1,3-propanediol oxidoreductase of the genetically engineered bacteria constructed by the present invention is 3.25-3.5 times that of the starting strain; the enzymatic activity of the formate dehydrogenase is 0.414-0.45 U / mg. Using the genetically engineered bacteria constructed by the present invention to carry out fed-batch fermentation for 29 hours, the yield of 1,3-propanediol is increased by 43.89%-97.93% compared with the starting strain, and the synergistic effect of the double genes significantly increases the yield of 1,3-propanediol and yield.

The invention relates to new glycerin dehydrase gene cloning and its expression in relative host. The enzyme gene is cloned form clostridium perfringens which can transform the glycerin into 3-hydroxyl propionic aldehyde at normal biological chemical reacting condition. Based on the invention, it can recombine the 1,3-propylene glycol redox enzyme relative gene into Escherichia coli to gain a newmetabolism engineering fungus which can be transformed into 1, 3-propylene glycol by fermenting tapioca hydrolyzate, glucose, or glycerol.

The subject invention pertains to the discovery that the NADH-dependent propanediol oxidoreductase (FucO) can reduce furfural. This allows for a new approach to improve furfural tolerance in bacterial and / or yeast cells used to produce desired products. Thus, novel biocatalysts (bacterial, fungal or yeast cells) exhibiting increased tolerance to furfural and 5-hydroxymethylfurfural (5-HMF) are provided as are methods of making and using such biocatalysts for the production of a desired product.

Recombinant organisms are provided comprising genes encoding genes encoding glycerol dehydratase, 1,3-propanediol, 1,3-propanediol oxidoreductase, a gene encoding vitamin B12 receptor precursor (BtuB), a gene encoding vitamin B12 transport system permease protein (BtuC) and a gene encoding vitamin B12 transport ATP-binding protein (BtuD). The recombinant microorganism is contacted with a carbon substrate and 1,3-propanediol is isolated from the growth media.

The invention relates to a recombined bacterial strain for modifying the specificity of a 1,3-propanediol redoxase coenzyme and an application of the recombined bacterial strain to 1,3-propanediol preparation, belonging to the technical field of biological engineering. The recombined bacterial strain is characterized in that the specificity of the 1,3-propanediol redoxase coenzyme is modified by rational design to obtain a mutant enzyme; and a recombinant expression vector in a gene sequence containing the mutant enzyme is constructed and converted into a host cell to obtain a recombined bacterial strain. Compared with an original bacterial strain, the invention has the advantage that the 1,3-propanediol yield is improved by 10-50 percent by utilizing the recombined bacterial strain for fermentation.

The present invention provides an improved method for the biological production of 1,3-propanediol from a fermentable carbon source in a single microorganism. In one aspect of the present invention, an improved process for the conversion of glucose to 1,3-propanediol is achieved by the use of an E. coli transformed with the Klebsiella pneumoniae dha regulon genes dhaR, orfY, dhaT, orfX, orfW, dhaB1, dhaB2, dhaB3, and orfZ, all these genes arranged in the same genetic organization as found in wild type Klebsiella pneumoniae. In another aspect of the present invention, an improved process for the production of 1,3-propanediol from glucose using a recombinant E. coli containing genes encoding a G3PDH, a G3P phosphatase, a dehydratase, and a dehydratase reactivation factor compared to an identical process using a recombinant E. coli containing genes encoding a G3PDH, a G3P phosphatase, a dehydratase, a dehydratase reactivation factor and a 1,3-propanediol oxidoreductase (dhaT). The dramatically improved process relies on the presence in E. coli of a gene encoding a non-specific catalytic activity sufficient to convert 3-hydroxypropionaldehyde to 1,3-propanediol.