A process is provided for bioconversion of carbon monoxide and carbon dioxide. More specifically, the process includes fermenting carbon monoxide and carbon dioxide containing substrate with acetogenic bacteria. The process provides for high levels of carbon monoxide and carbon dioxide conversions and utilization of hydrogen.

Provided is a microorganism having the capability of producing 3-hydroxypropionic acid from glucose and a method for producing 3-hydroxypropionic acid from glucose by using the microorganism. The microorganism can include a mutation adapted to utilize intracellularly introduced glucose in 3HP production rather than cell growth, and thus increases in 3HP productivity (3HP production capacity) can be achieved. Also provided is a method that can increase 3HP production yield by controlling the time of adding an inducer and/or kinds of an alkaline aqueous solution during culturing.

Provided is a microorganism having the capability of producing 3-hydroxypropionic acid from glucose and a method for producing 3-hydroxypropionic acid from glucose by using the microorganism. The microorganism can include a mutation adapted to utilize intracellularly introduced glucose in 3HP production rather than cell growth, and thus increases in 3HP productivity (3HP production capacity) can be achieved. Also provided is a method that can increase 3HP production yield by controlling the time of adding an inducer and/or kinds of an alkaline aqueous solution during culturing.

Provided is a two-step production method for 3-HP, comprising: a first step of culturing cells at a high concentration; and a second step of producing 3-HP using the high concentration-cultured cells as a catalyst, in which during the two-step culture, the energy and/or coenzyme balance are adjusted to produce 3-HP and/or improve the productivity of 3-HP. The productivity and yield of 3-HP can be improved.

Provided is a two-step production method for 3-HP, comprising: a first step of culturing cells at a high concentration; and a second step of producing 3-HP using the high concentration-cultured cells as a catalyst, in which during the two-step culture, the energy and/or coenzyme balance are adjusted to produce 3-HP and/or improve the productivity of 3-HP. The productivity and yield of 3-HP can be improved.

Yeast cells having a reductive TCA pathway from pyruvate or phosphoenolpyruvate to succinate, and which include at least one exogenous gene overexpressing an enzyme in that pathway, further contain an exogenous transhydrogenase gene.

Yeast cells having a reductive TCA pathway from pyruvate or phosphoenolpyruvate to succinate, and which include at least one exogenous gene overexpressing an enzyme in that pathway, further contain an exogenous transhydrogenase gene.

The disclosure provides recombinant bacterial host cells that metabolize and convert glycerol or volatile fatty acids (VFAs) to poly(3-hydroxybutyrate-co-3-hydroxyvalerate) or PHBV. The disclosure further provides methods of producing PHBV using the recombinant bacteria disclosed herein.

The disclosure provides recombinant bacterial host cells that metabolize and convert glycerol or volatile fatty acids (VFAs) to poly(3-hydroxybutyrate-co-3-hydroxyvalerate) or PHBV. The disclosure further provides methods of producing PHBV using the recombinant bacteria disclosed herein.

The use of microorganisms to make alpha-functionalized chemicals and fuels, (e.g. alpha-functionalized carboxylic acids, alcohols, hydrocarbons, amines, and their beta-, and omega-functionalized derivatives), by utilizing an iterative carbon chain elongation pathway that uses functionalized extender units. The core enzymes in the pathway include thiolase, dehydrogenase, dehydratase and reductase. Native or engineered thiolases catalyze the condensation of either unsubstituted or functionalized acyl-CoA primers with an alpha-functionalized acetyl-CoA as the extender unit to generate alpha-functionalized β-keto acyl-CoA. Dehydrogenase converts alpha-functionalized β-keto acyl-CoA to alpha-functionalized β-hydroxy acyl-CoA. Dehydratase converts alpha-functionalized β-hydroxy acyl-CoA to alpha-functionalized enoyl-CoA. Reductase converts alpha-functionalized enoyl-CoA to alpha-functionalized acyl-CoA. The platform can be operated in an iterative manner (i.e. multiple turns) by using the resulting alpha-functionalized acyl-CoA as primer and the aforementioned alpha-functionalized extender unit in subsequent turns of the cycle. Termination pathways acting on any of the four alpha-functionalized CoA thioester intermediates terminate the platform and generate various alpha-functionalized carboxylic acids, alcohols and amines with different β-reduction degree.