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.

Aspects of the disclosure relate to biosynthesis of histidine in host cells. For example, host cells may comprise: a promoter; a ribosome binding site (RBS); and a nucleic acid comprising: hisG; hisD; hisC hisB; hisH; hisA; hisF; and/or hisI. Host cells may further comprise a nucleic acid encoding a ribose phosphate pyrophosphokinase (RPPK), optionally comprising one or more amino acid substitutions relative to the sequence of wildtype E. coli RPPK. Host cells of the disclosure may comprise a nucleic acid encoding a 5,10-methylene-tetrahydrofolate dehydrogenase/5,10-methylene-tetrahydrofolate cyclohydrolase (MTHFDC) enzyme. Further aspects of the disclosure relate to production of purine pathway metabolites and/or plasmid DNA in host cells.

Provided are a mycosporine-like amino acid-producing microorganism and a method for production of mycosporine-like amino acids by using same. The microorganism can produce mycosporine-like amino acids from xylose.

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.

Compositions comprising (i) lactate oxidase (LOX) and Catalase (CAT), preferably in a 1:1 molar ratio; or (ii) a fusion polypeptide comprising both LOX and CAT, e.g., LOXCAT, and methods of use thereof for reducing blood lactate levels, increasing blood pyruvate levels, and/or decreasing blood lactate/pyruvate ratio in a subject.

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.