The disclosure provides genetically engineered C1-fixing microorganisms capable of producing nanobodies. Additionally, the disclosure provides engineered microorganisms comprising one or more disrupted genes to strategically divert carbon flux away from nonessential or undesirable products towards products and/or co-products of interest. The disclosure enables co-production of useful chemicals from gaseous substrates.

This invention relates to the bioproduction of substituted or unsubstituted phenylacetaldehyde, 2-phenylethanol, phenylacetic acid or phenylethylamine by subjecting a starting material comprising glucose, L-phenylalanine, substituted L-phenylalanine, styrene or substituted styrene to a plurality of enzyme catalyzed chemical transformations in a one-pot reaction system, using recombinant microbial cells overexpressing the enzymes. To produce phenylacetaldehyde from styrene, the cells are modified to overexpress styrene monooxygenase (SMO) and styrene oxide isomerase (SOI). To produce phenylacetic acid from styrene, SMO, SOI and aldehyde dehydrogenase are overexpressed. Alternatively, to produce 2-phenylethanol, SMO, SOI and aldehyde reductase or alcohol dehydrogenase are overexpressed, while to produce phenylethylamine, SMO, SOI and transaminase are overexpressed.

The present invention relates to recombinant Corynebacterium having 1,3-PDO productivity and reduced 3-HP productivity, and a method for producing 1,3-PDO by using same. When a Corynebacterium glutamicum variant according to the present invention is used, the productivity of 3-HP, which is a by-product, is inhibited by using low-cost glycerol as a carbon source, and thus 1,3-PDO can be produced with high efficiency.

The invention relates to recombinant microorganisms and methods for producing macrocyclic ketones and macrocyclic ketone precursors.

The invention provides polypeptides and encoding nucleic acids of aldehyde dehydrogenase variants. The invention also provides cells expressing aldehyde dehydrogenase variants. The invention further provides methods for producing 3-hydroxybutyraldehyde (3-HBal) and/or 1,3-butanediol (1,3-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells. The invention additional provides methods for producing 4-hydroxybutyraldehyde (4-HBal) and/or 1,4-butanediol (1,4-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells.

A composition includes two exogenous enzymes from animals for consumption by human beings to prevent, treat and/or alleviate veisalgia and/or symptoms associated therewith arising from or caused by consumption or spontaneous production of alcohol through a dual-enzyme based breakdown of the alcohol, wherein a first enzyme of the two exogenous enzymes is capable of converting alcohol into a first metabolite while a second enzyme thereof is capable of converting the first metabolite into a second metabolite which is excretable to systemic circulation after an oxidation reaction of the alcohol in the presence of the two exogenous enzymes and NAD.sup.+/NADH, and wherein the first enzyme to the second enzyme is in a molar ratio of 1:3-51 in the composition in order to avoid an elevation in the level of the first metabolite in the human being.

The present invention relates to the metabolic engineering of a microbial host for the synthesis of value-added products from oil palm empty fruit brunches (OPEFBs). In one embodiment, the genetically engineered microorganism is Escherichia coli comprising a metabolic pathway consisting of 9 enzymes (11 genes) to utilize depolymerized lignin, namely vanillin, p-coumaric acid, p-hydroxybenzaldehyde, vanillic acid, p-hydroxybenzoic acid and ferulic acid, to produce β-ketoadipic acid, which can be subsequently converted into commercially important derivatives such as adipic acid and levulinic acid. The enzymes are feruloyl-CoA synthetase (fcs), enoyl-CoA hydratase (ech), vanillin dehydrogenase (vdh), vanillate O-demethylase (vanA; vanA and vanB), p-hydroxy benzoate hydroxylase (pobA), protocatechuate 3,4-dioxygenase {pcaGH; pcaG and pcaH), 3-carboxy-cis, cis-muconate cycloisomerase (pcaB), 4-carboxymuconolactone decarboxylase (pcaC), and β-ketoadipate enol-lactone hydrolase (pcaD).

The disclosure provides genetically engineered microorganisms and methods for improved biological production of ethylene glycol and precursors of ethylene glycol. The microorganism of the disclosure produces ethylene glycol or a precursor of ethylene glycol through one or more of 5,10-methylenetetrahydrofolate, oxaloacetate, citrate, malate, and glycine. The disclosure further provides compositions comprising ethylene glycol or polymers of ethylene glycol such as polyethylene terephthalate.

The present invention provides for a mechanism to completely replace the electron accepting function of glycerol formation with an alternative pathway to ethanol formation, thereby reducing glycerol production and increasing ethanol production. In some embodiments, the invention provides for a recombinant microorganism comprising a down-regulation in one or more native enzymes in the glycerol-production pathway. In some embodiments, the invention provides for a recombinant microorganism comprising an up-regulation in one or more enzymes in the ethanol-production pathway.

The present invention discloses a method for preparing L-glufosinate ammonium by biological enzymatic de-racemization, a glufosinate ammonium dehydrogenase mutant and a use thereof. The method for preparing L-glufosinate ammonium by biological enzymatic de-racemization includes catalyzing D,L-glufosinate ammonium as a raw material by a multi-enzyme catalysis system to obtain L-glufosinate ammonium. The enzyme catalysis system includes D-amino acid oxidase for catalyzing D-glufosinate ammonium in the D,L-glufosinate ammonium to 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid, and a glufosinate ammonium dehydrogenase mutant for catalytically reducing 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid to L-glufosinate ammonium. The glufosinate ammonium dehydrogenase mutant is obtained by mutation of glufosinate-ammonium dehydrogenase in wild fungi Thiopseudomonas denitrificans at a mutation site of V377S. The glufosinate ammonium dehydrogenase mutant in the present invention has better catalytic efficiency. When racemic D, L-glufosinate ammonium is used as a substrate for a catalytic reaction, the conversion rate is much higher than the conversion rate of a wild-type enzyme, and the yield of 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid (PPO for short) is also greatly improved.