The invention relates to an enzymatic method for producing 2-hydroxy-4-methylmercaptobutanoic acid from 3-methylthio-propanal (3-methylmercaptopropanal (MMP) or methional) and carbon dioxide.

The disclosure relates to host cells having altered NADPH availability, allowing for increased production of compounds produced using NADPH, and methods of use thereof. NADPH availability is altered by one or more of: expressing an altered GAPDH, expressing a variant glutamate dehydrogenase (gdh), aspartate semialdehyde dehydrogenase (asd), dihydropicolinate reductase (dapB), and meso-diaminopimelate dehydrogenase (ddh), expressing a novel nicotinamide nucleotide transhydrogenase, expressing a novel threonine aldolase, and expressing or modulating the expression of a pyruvate carboxylase in the host cells.

The present invention relates to a recombinant microorganism for producing formic acid, which has a formate dehydrogenase 1 alpha subunit (FDH1)-encoding endogenous gene deleted therefrom and an FDH1-encoding exogenous gene introduced thereinto, and a method for production of formic acid by using the microorganism.

In a process for producing formate, a mixed enzyme by mixing hydrogenase (H.sub.2ase) with oxygen tolerance and formate dehydrogenase (FDH) with oxygen tolerance is prepared, and the mixed enzyme and a gas including H.sub.2, CO.sub.2 and NAD.sup.+ are mixed such that formate may be produced even in the presence of oxygen, and thereby utilizing hydrogen sources including oxygen, such as coke oven gas.

The disclosure discloses construction and application of an engineered strain of E. coli for producing malic acid by fixing CO.sub.2, and belongs to the field of fermentation. The engineered strain is obtained by performing genetic engineering transformation on Escherichia coli MG1655; the genetic engineering transformation includes knocking out a fumarate reductase gene, a fumarase gene, a lactate dehydrogenase gene and an alcohol dehydrogenase gene and freely overexpressing a formate dehydrogenase, an acetyl coenzyme A synthetase, an acylated acetaldehyde dehydrogenase, a formaldehyde lyase, a dihydroxyacetone kinase, a malic enzyme and a phosphite oxidoreductase to obtain a strain GH0407. The strain is used for producing malic acid by fermentation, anaerobic fermentation is performed for 72 hours with CO.sub.2 and glucose as a co-substrate, the production of malic acid reaches 39 g/L, the yield is 1.53 mol/mol, and accumulation of malic acid in the original strain is not achieved.

The invention relates to an enzymatic method for producing 2-hydroxy-4-methylmercaptobutanoic acid from 3-methylthio-propanal (3-methylmercaptopropanal (MMP) or methional) and carbon dioxide.

The present invention relates to an L-lysine-producing microorganism of the genus Corynebacterium and a method for producing L-lysine using the same.

An exemplary embodiment of the present disclosure provides a method of converting formate to a desired compound. The method comprises providing a biocatalyst and formate to form a reaction mixture and reacting at least the biocatalyst with formate to produce a first reaction product.

Provided are an immobilized enzyme and an application thereof in continuous production. The immobilized enzyme is a Polyethyleneimine (PEI)-modified immobilized enzyme, and includes: an enzyme, which includes Amine Dehydrogenase (AmDH) and/or Formate Dehydrogenase (FDH); and a carrier, which is a cyanuric chloride-activated amino carrier. The problem in the prior art of poor performance of an immobilized enzyme is solved, the catalytic activity and reusability of the immobilized enzyme are improved, and the immobilized enzyme is suitable for the field of enzyme immobilization.

There is disclosed a highly stable biocatalytic multi-enzyme system on hydrophobic support for the efficient and continuous hydrogenation of carbon dioxide (CO.sub.2) to formate. The system immobilizes formate dehydrogenase (FDH), glucose dehydrogenase (GDH), and carbonic anhydrase (CA) enzymes on a hydrophobic surface-modified metal-organic framework (MOF), SA-HKUST-1. The hydrophobic surface modification with stearic acid enhances the enzyme stability and reusability, maintaining 95% activity after four cycles. The hydrophobicity of SA-HKUST-1 improves CO.sub.2 diffusion to the immobilized enzymes, significantly boosting the formate production. Enzyme specificity ensures selective reactions, with FDH facilitating CO.sub.2 bioconversion, CA accelerating CO.sub.2 hydration and GDH facilitating cofactor regeneration within the system. The system demonstrates superior performance, producing 255.8 mM formate per gram of MOF per hour. Operating under mild conditions with simple equipment, it reduces costs and eliminates harmful by-products. This invention offers an eco-friendly, sustainable approach for CO.sub.2 mitigation, with potential applications in industrial CO.sub.2 conversion processes.