Abstract: In an alcohol fermentation process, oil derived from biomass is chemically converted into an extractant available for in situ removal of a product alcohol such as butanol from a fermentation broth. The glycerides in the oil can be chemically converted into a reaction product, such as fatty acids, fatty alcohols, fatty amides, fatty acid methyl esters, fatty acid glycol esters, and hydroxylated triglycerides, and mixtures thereof, which forms a fermentation product extractant having a partition coefficient for a product alcohol greater than a partition coefficient of the oil of the biomass for the product alcohol. Oil derived from a feedstock of an alcohol fermentation process can be chemically converting into the fermentation product extractant.

Abstract: An isolated nucleic acid encoding an FX protein having a serine at position 79, a lysine at position 90, a leucine at position 136, an arginine at position 211, a serine at position 289, and a combination thereof is provided. Cells having a gene encoding a modified FX protein are provided, wherein the cells exhibit a reduced ability to fucosylate a glycoprotein at a first temperature, but exhibit the ability to fucosylate the glycoprotein at a second temperature. Methods and compositions for making glycoproteins with reduced fucosylation are provided.

Abstract: Provided herein are metabolically-modified microorganisms useful for producing biofuels. More specifically, provided herein are methods of producing high alcohols including isobutanol, 1-butanol, 1-propanol, 2-methyl-1-butanol, 3-methyl-1-butanol, and 2-phenylethanol from a suitable substrate and a recombinant acetolactate synthase having both synthase and decarboxylase activity.

Abstract: The present invention relates to isolated polypeptides having cellobiohydrolase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

Abstract: The present invention relates to novel mutant thioesterase enzymes and naturally-occurring equivalents thereof, compositions made from such enzymes and uses of thioesterase enzymes. In particular, the present invention provides mutant thioesterase enzymes that have altered properties, for example, altered substrate specificity, altered activity, altered selectivity, and/or altered proportional yields in the product mixtures. The present invention also provides polynucleotides encoding such mutant thioesterase enzymes, and vectors and host cells comprising such polynucleotides. The invention further provides for novel uses of thioesterases in the production of various fatty acid derivatives, which are useful as, or as components of, industrial chemicals and fuels.

Abstract: The present invention provides a method for preparing a variant lipid acyltransferase enzyme by expressing a nucleotide sequence encoding a lipid acyltransferase which may comprise at least one modification at a position(s) which corresponds in the encoded amino acid sequence to an amino acid(s) located in a) the canyon region of the enzyme (i.e. preferably amino acid residues 31, 27, 85, 86, 119, and 120); and/or b) insertion site 1 (i.e. amino acid residues 22-36) and/or c) insertion site 2 (i.e. amino acid residues 74-88), wherein the canyon region, insertion site 1 and/or insertion site 2 are defined as that region which when aligned based on primary or tertiary structure corresponds to the canyon region, insertion site 1 or insertion site 2 (or the corresponding amino acid residues taught above) of the enzyme shown herein as SEQ ID No. 16 or 6 in a host organism.

Abstract: The present invention relates to a method for producing phytase variants has at least 70% identity to a phytase derived from Buttiauxella and comprises at least one additional disulfide bond as compared to this phytase. These phytase variants have modified, preferably improved, properties, such as thermostability, temperature profile, pH profile, specific activity, performance in animal feed, reduced protease sensitiliby, and/or an modified glycosylation pattern. The invention also relates to the variants produced, DNA encoding these phytases, methods of their production, as well as the use thereof, e.g. in animal feed and animal feed additives.

Abstract: An engineering method was developed to allow genetic modification and isolation of lactic acid bacteria cells that lack lactate dehydrogenase and acetolactate decarboxylase activities. In cells with these modifications and an isobutanol biosynthetic pathway, improved production of isobutanol was observed.

Abstract: The invention provides lipolytic enzyme variants having improved in-detergent stability and polynucleotides encoding same. Lipolytic enzyme variants with improved in-detergent stability are obtained by substituting certain specified amino acid residues in a parent lipolytic enzyme.

Abstract: The present invention relates to the use of a bacterium having an high indole-3-acetic acid (IAA) content for solubilizing phosphate rock (PR) in the ground, wherein said bacterium is obtained by transformation with a gene encoding an agent able to increase the IAA content.

Abstract: Isolated glycyl-tRNA synthetase polypeptides and polynucleotides having non-canonical biological activities are provided, as well as compositions and methods related thereto.

Abstract: Cytochrome P450 BM-3 from Bacillus megaterium was engineered using a combination of directed evolution and site-directed mutagenesis to hydroxylate linear alkanes regio- and enantioselectively using atmospheric dioxygen as an oxidant. Mutant 9-10A-A328V hydroxylates octane primarily at the 2-position to form S-2-octanol (40% ee). Another mutant, 1-12G, hydroxylates alkanes larger than hexane primarily at the 2-position, but forms R-2-alcohols (40-55% ee). These biocatalysts are highly active for alkane substrates and support thousands of product turnovers. These regio- and enantio-selectivities are retained in whole-cell biotransformations with E. coli, where the engineered P450s can be expressed at high levels and the expensive cofactor is supplied endogenously.

Abstract: The invention provides recombinant microorganisms capable of producing isobutyraldehyde using CO2 as a carbon source. The invention further provides methods of preparing and using such microorganisms to produce isobutyraldehyde.

Abstract: Methods and compositions for producing fatty acid derivatives, for example, fatty esters, and commercial fuel compositions comprising fatty acid derivatives are described.

Abstract: The present invention concerns a new method for the biological preparation of a diol comprising culturing a microorganism genetically modified for the bioproduction of an aliphatic diol, wherein the microorganism comprises a metabolic pathway for the decarboxylation of a hydroxy-2-keto-aliphatic acid metabolite with an enzyme having a 2-keto acid decarboxylase activity, the product obtained from said decarboxylation step being further reduced into the corresponding aliphatic diol, and wherein the microorganism is genetically modified for the improved production of said hydroxy-2-keto-aliphatic acid metabolite. The invention also concerns a modified microorganism for the production of an aliphatic diol.

Abstract: The invention relates to the use of an enzyme preparation which catalyzes the degradation of formaldehyde for reducing the formaldehyde content in a formaldehyde-containing formulation. In a preferred embodiment, the enzyme preparation contains a formaldehyde dismutase from a Pseudomonas putida strain. Further, the invention refers to a process for reducing the formaldehyde content in cross-linking agents for textile finishing or in polymer dispersions used, e.g. in construction chemistry. Further the invention relates to the use of an enzyme preparation which catalyzes the degradation of aldehydes for reducing the formaldehyde content in an aldehyde-containing formulation. Furthermore, the invention relates to a novel variant of the formaldehyde dismutase from Pseudomonas putida.

Abstract: A method for fermenting coffee beans is disclosed. Bacteria secreting chimeric proteins comprising endo polygalacturane A (PGAA) and pectin methyl esterase 1 (PME1), which target the pectin coating for hydrolysis, are described. The net result of this targeted hydrolysis of the inner pectin coating can be the production of coffee beans with unique and unexpected flavor characteristics. Desirable flavors can be created or enhanced without any of the adverse taste qualities associated with artificial flavors. For lower grade coffee beans, this process serves to reduce or eliminate undesirable flavors.

Abstract: A recombinant yeast that makes an isoprenoid compound is provided. The yeast comprises an endogenous mevalonate pathway comprising (i) an enzyme that converts acetyl-CoA to acetoacetyl-CoA, (ii) an enzyme that converts acetoacetyl-CoA to hydroxymethylglutaryl-CoA, (iii) an enzyme that converts hydroxymethylglutaryl-CoA to mevalonic acid, (iv) an enzyme that converts mevalonic acid to phosphomevalonic acid, (v) an enzyme that converts phosphomevalonic acid to phosphomevalonate, and (vi) an enzyme that converts phosphomevalonate to isopentenyl pyrophosphate. The yeast further comprises heterologous nucleic acid sequences encoding an enzyme that converts hydroxymethylglutaryl-CoA to mevalonic acid, an enzyme that converts mevalonic acid to phosphomevalonic acid, an enzyme that converts phosphomevalonic acid to phosphomevalonate, and an enzyme that converts phosphomevalonate to isopentenyl pyrophosphate.

Abstract: Disclosed is a method to incorporate xylose transport related genes into a yeast strain for lignocelluloses to ethanol production. More specifically, the invention relates to novel Saccharomyces cerevisiae strains NRRL Y-50463 and yeast strains having novel xylose transporter genes, the genes deposited as GenBank JF343555, GenBank JF343556, GenBank JF343557, GenBank JF343558, and GenBank JF343559. The yeast strains having said genes are deposited as Y-50465, Y-50466, Y-50746, Y-50747, Y-50748, and Y-50749.

Abstract: Polypeptide with an amino acid sequence according to SEQ ID No. 1 or a variant in which up to 10% of the amino acids have been altered by insertions, deletions or substitution.