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 disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

A chemoenzymatic process for the preparation of an oxidized glucose product comprising contacting D-glucose with an enzyme selected from the group consisting essentially of galactose oxidase (GAO), glucose oxidase (GOX), polysaccharide monooxygenase, catalase, animal peroxidase, periplasmic aldehyde oxidase (Pao), unspecific peroxygenase (UPO), lactoperoxidase (LPO), myeloperoxidase (MPO), eosinophil peroxidase (EPO), thyroid peroxidase (TPO), ovoperoxidase, salivary peroxidase, vanadium haloperoxidase, non-mammalian vertebrate peroxidase (POX), peroxidasin (Pxd), bacterial peroxicin (Pxc), invertebrate peroxinectin (Pxt), short peroxidockerin (PxDo), alpha-dioxygenase (aDox), dual oxidase (DuOx), prostaglandin H synthase (PGHS), cyclooxygenase (CyOx), linoleate diol synthase (LDS), variants thereof, and combinations thereof under conditions suitable for the formation of an oxidized intermediate; and contacting the oxidized intermediate with a metal catalyst to form an oxidized glucose product.

The present invention relates to host cells and their use wherein the host cells are capable of producing D-ribulose and incapable of or have a reduced capability of converting D-ribulose to a molecule other than ribitol, wherein the host cells comprise a heterologous nucleic acid sequence encoding a polypeptide capable of converting D-ribulose to ribitol with a cofactor preference for NADPH.

The invention provides amperometric analyte sensor systems comprising one or more electrodes designed to monitor in vivo levels of 3-hydroxybutyrate (and optionally glucose as well) in order to facilitate the management of diabetic ketoacidosis. The invention further includes compositions, elements and methods useful with such amperometric analyte sensor systems.

Provided herein is a non-naturally occurring microbial organism having a methanol metabolic pathway that can enhance the availability of reducing equivalents in the presence of methanol. Such reducing equivalents can be used to increase the product yield of organic compounds produced by the microbial organism, such as 1,2-propanediol, n-propanol, 1,3-propanediol or glycerol. Also provided herein are methods for using such an organism to produce 1,2-propanediol, n-propanol, 1,3-propanediol or glycerol.

The present invention provides for a genetically modified host cell capable of producing isopentenol and/or 3-methyl-3-butenol, comprising (a) an increased expression of phosphomevalonate decarboxylase (PMD) (b) an increased expression of a phosphatase capable of converting isopentenol into 3-methyl-3-butenol, (c) optionally the genetically modified host cell does not express, or has a decreased expression of one or more of NudB, phosphomevalonate kinase (PMK), and/or PMD, and (d) optionally one or more further enzymes capable of converting isopentenol and/or 3-methyl-3-butenol into a third compound, such as isoprene.

The present invention relates to a novel method for the affinity purification of proteins of interest in a single step, based on the lectin activity of the CRD (Carbohydrate Recognition Domain) of a galectin or part of said domain retaining the ability to bind β-galactosidase derivative.

The present invention provides for novel metabolic pathways to reduce or modulate glycerol production and increase product formation. More specifically, the invention provides for a recombinant microorganism comprising one or more native and/or heterologous proteins that function to import glycerol and one or more native and/or heterologous enzymes that function in one or more engineered metabolic pathways to convert a carbohydrate source, such as lignocellulose, to a product, such as ethanol, wherein the one or more native and/or heterologous proteins or enzymes is activated, upregulated, or downregulated. The invention also provides for a recombinant microorganism comprising one or more native or heterologous proteins that function to regulate glycerol synthesis and one or more native and/or heterologous enzymes that function in one or more engineered metabolic pathways to convert a carbohydrate source to ethanol, wherein said one or more native and/or heterologous proteins or enzymes is activated, upregulated or downregulated. Also provided are methods for increasing cellular glycerol uptake and increasing recombinant production of fuels and other chemicals using the recombinant microorganisms of the invention.

Described herein are non-natural NAD.sup.+-dependent alcohol dehydrogenases (ADHs) capable of at least two fold greater conversion of methanol or ethanol to formaldehyde or acetaldehyde, respectively, as compared to its unmodified counterpart. Nucleic acids encoding the non-natural alcohol dehydrogenases, as well as expression constructs including the nucleic acids, and engineered cells comprising the nucleic acids or expression constructs are described. Also described are engineered cells expressing a non-natural NAD.sup.+-dependent alcohol dehydrogenase, optionally include one or more additional metabolic pathway transgene(s), methanol metabolic pathway genes, target product pathway genes, cell culture compositions including the cells, methods for promoting production of the target product or intermediate thereof from the cells, compositions including the target product or intermediate, and products made from the target product or intermediate.