Abstract: Promoter regions associated with the Yarrowia lipolytica n-alkane-hydroxylating cytochrome P450 (ALK2) gene are disclosed and have been found to be particularly effective for the expression of heterologous genes in yeast. These promoter regions will be useful for driving high-level expression of genes involved in the production of omega-3 and omega-6 fatty acids.

Abstract: Promoter regions associated with the Yarrowia lipolytica peroxisomal 2,4-dienoyl-CoA reductase (SPS19) gene are disclosed and have been found to be particularly effective for the expression of heterologous genes in yeast. These promoter regions will be useful for driving high-level expression of genes involved in the production of omega-3 and omega-6 fatty acids.

Abstract: A method and system for the enzymatic treatment of a lipid containing feedstock comprises contacting the feedstock with a processing aid, then causing the feedstock to pass at a substantially constant flow rate through a treatment system comprising a plurality of enzyme-containing fixed bed reactors connected to one another in series. The fixed bed reactors can be individually serviceable, the flow rate of the feedstock remaining substantially constant through the system when one of the fixed bed reactors is taken offline for servicing. In the most preferred embodiment, the processing aid is a substantially moisture-free silica. The processing aid can be placed in one or more of the fixed bed reactors, disposed above the enzyme in the reactor, or it can be in a pre-treatment system which can comprise one or more reactors.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: A process is provided for producing target concentrations of peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity under conditions where control of reaction pH by selection of buffer concentration and concentration of perhydrolase and reactants produces a targeted concentration of peroxycarboxylic acids. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided, as are corresponding methods of use.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritime acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: The present invention relates to compositions and methods for treating and preventing cocaine addiction. In particular, the present invention provides mutated cocaine esterase proteins for use in treating and preventing cocaine addiction.

Abstract: Compositions and methods for reducing the level of nornicotine and N?-nitrosonornicotine (NNN) in tobacco plants and plant parts thereof are provided. The compositions comprise isolated polynucleotides and polypeptides for a root-specific nicotine demethylases, CYP82E10, and variants thereof, that are involved in the metabolic conversion of nicotine to nornicotine in these plants. Compositions of the invention also include tobacco plants, or plant parts thereof, comprising a mutation in a gene encoding a CYP82E10 nicotine demethylase, wherein the mutation results in reduced expression or function of the CYP82E10 nicotine demethylase. Seed of these tobacco plants, or progeny thereof, and tobacco products prepared from the tobacco plants of the invention, or from plant parts or progeny thereof, are also provided. Methods for reducing the level of nornicotine, or reducing the rate of conversion of nicotine to nornicotine, in a tobacco plant, or plant part thereof are also provided.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: A method and system for the enzymatic treatment of a lipid containing feedstock comprises contacting the feedstock with a processing aid, then causing the feedstock to pass at a substantially constant flow rate through a treatment system comprising a plurality of enzyme-containing fixed bed reactors connected to one another in series. The fixed bed reactors can be individually serviceable, the flow rate of the feedstock remaining substantially constant through the system when one of the fixed bed reactors is taken off line for servicing. In the most preferred embodiment, the processing aid is a substantially moisture-free silica. The processing aid can be placed in one or more of the fixed bed reactors, disposed above the enzyme in the reactor, or it can be in a pre-treatment system which can comprise one or more reactors.

Abstract: Novel genes that code for a family of feruloyl esterases that break down ferulic acid crosslinks between polysaccharide chains and between polysaccharides and lignins in plant cell walls are described herein as well as a method of rapid gene discovery.

Abstract: The present disclosure relates to chemically modified carbonic anhydrase polypeptides and soluble compositions, homogenous liquid formulations comprising them. The chemically modified carbonic anhydrase polypeptides have improved properties relative to the same carbonic anhydrase polypeptide that is not chemically modified including the improved properties of increased activity and/or stability in the presence of amine compounds, ammonia, or carbonate ion. The present disclosure also provides methods of preparing the chemically modified polypeptides and methods of using the chemically modified polypeptides for accelerating the absorption of carbon dioxide from a gas stream into a solution as well as for the release of the absorbed carbon dioxide for further treatment and/or sequestering.

Abstract: The present disclosure relates to ?-class carbonic anhydrase polypeptides having improved properties including increased thermostability and/or stability in the presence of amine compounds, ammonia, or carbonate ion. The present disclosure also provides formulations and uses of the polypeptides for accelerating the absorption of carbon dioxide from a gas stream into a solution as well as for the release of the absorbed carbon dioxide for further treatment and/or sequestering. Also provided are polynucleotides encoding the carbonic anhydrase polypeptides and host cells capable of expressing them.

Abstract: The present invention relates to a method for the preparation of 4-hyroxy-L-proline or compositions with a high content of this aminoacid and the use thereof as agrochemical in the agronomical field and/or as a synthesis intermediate of chemical compounds.

Abstract: The invention provides a use of platelet activating factor acetylhydrolase (PAF-AH) activity as a biomarker for severe or fatal anaphylaxis in a subject. The level of PAF-AH activity inversely correlates with the susceptibility to severe or fatal anaphylaxis. The use comprises assaying PAF-AH activity in a sample from the subject and comparing the measured activity to a reference value, wherein a lower level of measured PAF-AH activity relative to said reference level of PAF-AH activity indicates a presence of or susceptibility to severe or fatal anaphylaxis in the subject. A method for treating or preventing severe or fatal anaphylaxis in a subject is also provided. The method comprises increasing serum platelet activating factor acetylhydrolase (PAF-AH) concentration in the subject by administering to the subject, PAF-AH and/or a PAF receptor antagonist. A composition for treating severe or fatal anaphylaxis is also provided.

Abstract: The storage stability of a serine hydrolase acting on ester bonds in a formulation without a protease can be improved by incorporating a serine protease inhibitor.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: A recombinant antibody vector for producing a single chain recombinant antibody comprises: (a) a contiguous nucleotide sequence: (i) that comprises a restriction endonuclease site that encodes an amino acid sequence of an immunoglobulin variable region; and (ii) that encodes an immunoglobulin constant region amino acid sequence in the same reading frame as (i), wherein another nucleotide sequence encoding (iii) an immunoglobulin variable region amino acid sequence, is insertable into the restriction endonuclease site in the same reading frame as (ii); and (b) one or more regulatory nucleotide sequences operably linked or connected to said nucleotide sequence, wherein the amino acid sequence in (i) comprises amino acids conserved in different immunoglobulin variable regions. The restriction endonuclease site may be a SacI site which encodes the conserved amino acids glutamate and leucine. In frame insertion of the nucleotide sequence of (iii) is facilitated by ligase independent cloning.

Abstract: A reaction medium for enzyme-catalyzed reactions is provided, comprising an oil-in-water emulsion including water, an emulsifier, an oil phase and at least one interfacially active enzyme, where the emulsion is produced by the phase inversion temperature process and has a droplet size of 50 to 400 nm. A method for the enzyme-catalyzed esterification, transesterification or hydrolysis of fatty acid alkyl esters and/or triglycerides is also provided where the oil-in-water emulsion is used as the reaction medium.

Abstract: A fusion protein that includes a polypeptide binding specifically to a constant region of an antibody and a stabilization protein linked to a terminus of the polypeptide, a polynucleotide encoding the fusion protein, a cell including the polynucleotide, a method of preparing the fusion protein, and a method of isolating an antibody by using the fusion protein.

Abstract: The invention relates to novel mutants of ?PLE, to vehicles containing the same and to their use in the production of enantiomer-enriched alcohols, carboxylic acids and esters.

Abstract: The invention relates to a Talaromyces transformant comprising one or more recombinant gene, capable of producing cellulase in the absence of cellulase inducer in a glucose medium, having a cellulase activity of 2 WSU/ml or more, in 16 times or more diluted supernatant or broth.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: The present invention encompasses albumin fusion proteins. Nucleic acid molecules encoding the albumin fusion proteins of the invention are also encompassed by the invention, as are vectors containing these nucleic acids, host cells transformed with these nucleic acids vectors, and methods of making the albumin fusion proteins of the invention and using these nucleic acids, vectors, and/or host cells. Additionally the present invention encompasses pharmaceutical compositions comprising albumin fusion proteins and methods of treating, preventing, or ameliorating diseases, disorders or conditions using albumin fusion proteins of the invention.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: The present invention is related to a fungal serine protease enzyme, which said enzyme has serine protease activity and comprises an amino acid sequence of Malbranchea ALKO4122 mature protease as defined in SEQ ID NO:18 or an amino acid sequence having at least 66% identity to the amino acid sequence of SEQ ID NO:18. Also disclosed is an isolated nucleic acid molecule, comprising a polynucleotide sequence which encodes a fungal serine protease enzyme, nucleic acid sequences encoding said protease, a host cell and a process of producing a polypeptide having serine protease activity. Said protease is useful as an enzyme preparation applicable in detergent compositions and for treating fibers, wool, hair, leather, or silk, for treating food or feed, or for any applications involving modification, degradation or removal of proteinaceous material.

Abstract: Isolated nucleic acids encoding polypeptides that exhibit butyrylcholinesterase (BChE) enzyme activity are disclosed, along with molecular criteria for preparing such nucleic acids, including codon optimization. Methods of preparing modified and/or truncated BChE molecules having selected properties, especially selective formation of monomers, are also described. Vectors and cells containing and/or expressing the nucleic acids are also disclosed.

Abstract: Promoter regions associated with the Yarrowia lipolytica esterase/lipase (EL1) gene are disclosed and have been found to be particularly effective for the expression of heterologous genes in yeast. These promoter regions will be useful for driving high-level expression of genes involved in the production of omega-3 and omega-6 fatty acids.

Abstract: A process is provided for producing peroxycarboxylic acids from carboxylic acid esters. More specifically, carboxylic acid esters are reacted with an inorganic peroxide, such as hydrogen peroxide, in the presence of an enzyme catalyst having perhydrolysis activity. The present perhydrolase catalysts are classified as members of the carbohydrate esterase family 7 (CE-7) based on the conserved structural features. Further, disinfectant formulations comprising the peracids produced by the processes described herein are provided.

Abstract: The present disclosure relates to a method for producing heterologous protein including: (c) providing a host cell comprising a 2 ?m-family plasmid, the plasmid comprising a gene encoding a protein comprising the sequence of a chaperone protein and a gene encoding a heterologous protein; (d) culturing the host cell in a culture medium under conditions that allow the expression of the gene encoding the chaperone protein and the gene encoding a heterologous protein; (e) purifying the thus expressed heterologous protein from the cultured host cell or the culture medium.

Abstract: A process for preparing urethane-containing (meth)acrylic esters (U) by reacting a urethane-containing alcohol (A) with a (meth)acrylic ester of a saturated alcohol (G) in the presence of at least one polymerization inhibitor (P) with an enzyme (E) as a catalyst in a reactor, wherein the (meth)acrylic ester of a saturated alcohol (G) and the urethane-containing alcohol (A) are passed continuously through at least one fixed bed reactor filled with an immobilized enzyme (E) as a catalyst.

Abstract: The invention relates to a process for production of an enzyme product having a plurality of enzyme activities obtained by fermentation of an Aspergillus strain.

Abstract: The present invention relates to a process for preparing a compound comprising an ?,? amide linkage between a cysteine moiety and a glutamic acid moiety, such as ?-glutamylcysteine or a ?-glutamylcysteine derivative, the process comprising providing a cysteine derivative, a ?-glutamyl donor and an enzyme capable of transferring the ?-glutamyl group to said cysteine derivative in a reaction environment promoting transfer of the ?-glutamyl group to said cysteine derivative. The invention also relates to compounds comprising an ?,? amide linkage between a cysteine moiety and a glutamic acid moiety, such as ?-glutamylcysteine or a ?-glutamylcysteine derivative, when obtained by processes of the invention, and uses thereof.

Abstract: The present invention relates to a method for preparing a variant lipolytic enzyme comprising expressing in a host organism a nucleotide sequence which has at least 90% identity with a nucleotide sequence encoding a fungal lipolytic enzyme and comprises at least one modification at a position which corresponds in the encoded amino acid sequence to a) the introduction of at least one glycosylation site in the amino acid sequence compared with the original fungal lipolytic enzyme; b) the introduction of at least one amino acid at a surface position and at a location in an external loop distal to the active site of the enzyme which is more hydrophilic; or c) a substitution or insertion at one or more of positions disclosed herein or a deletion at one or more positions disclosed herein. The invention also relates to polypeptide produced by the method and to novel nucleic acids.

Abstract: The present invention relates to LipA and its variant that binds to the glucosyl- and acyl chain- region of its glycoside substrate in plant cell walls useful for biofuel production, wherein presence of a hydrophobic pocket confers extensive hydrophobic interaction of the acyl chain with the rest of the tunnel residues.

Abstract: The invention relates to functional polypeptides secreted from Botryospaeria rhodina CBS 274.96.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in the ratio of peracetic acid formation to peracetic acid hydrolysis specific activities (PAAF/PAAH ratio). The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: Butyrylcholinesterase (BChE) polypeptide variants of the presently-disclosed subject matter have enhanced catalytic efficiency for (?)-cocaine, as compared to wild-type BChE. Pharmaceutical compositions of the presently-disclosed subject matter include a BChE polypeptide variant having an enhanced catalytic efficiency for (?)-cocaine. A method of the presently-disclosed subject matter for treating a cocaine-induced condition includes administering to an individual an effective amount of a BChE polypeptide variant, as disclosed herein, to lower blood cocaine concentration.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.

Abstract: An acetyl xylan esterase variant having perhydrolytic activity is provided for producing peroxycarboxylic acids from carboxylic acid esters and a source of peroxygen. More specifically, a Thermotoga maritima acetyl xylan esterase gene was modified using error-prone PCR and site-directed mutagenesis to create an enzyme catalyst characterized by an increase in specific activity. The variant acetyl xylan esterase may be used to produce peroxycarboxylic acids suitable for use in a variety of applications such as cleaning, disinfecting, sanitizing, bleaching, wood pulp processing, and paper pulp processing applications.