Abstract: The present disclosure relates to the use of an amino acid dehydrogenase in combination with a cofactor regenerating system comprising a ketoreductase. In particular embodiments, the process can be used to prepare L-tert-leucine using a leucine dehydrogenase.

Abstract: The present invention relates to compositions comprising: a polypeptide having cellulolytic enhancing activity and a dioxy compound. The present invention also relates to methods of using the compositions.

Abstract: The disclosure relates to engineered enone reductase polypeptides having improved properties, polynucleotides encoding the engineered polypeptides, related vectors, host cells, and methods for making the engineered enone reductase polypeptides. The disclosure also provides methods of using the engineered enone reductase polypeptides for chemical transformations.

Abstract: A method of measuring the degradation of intact proteins includes a step of providing a protein substrate having one or more free or exposed carboxyl groups and then reductively attaching 7-amino-4-methylcoumarin (AMC) to the protein substrate with a reducing agent. The protein substrate is contacted in a test solution with one or more proteolytic enzymes that degrade the protein substrate. The amount of AMC attached to the protein substrate is then determined by monitoring the fluorescence of free 7-amino-4-methylcoumarin that is formed during degradation of the protein substrate to protein fragments.

Abstract: The present invention provides an enzymatic process for the preparation of (S)-5-(4-Fluoro-phenyl)-5-hydroxy-1morpholin-4-yl-pentan-1-one by the reduction of 1-(4-Fluoro-phenyl)-5-morpholin-4-yl-pentane-1,5-dione by using a suitable enzyme or by the resolution of (R,S)-5-(4-Fluoro-phenyl)-5-hydroxy-1morpholin-4-yl-pentan-1-one by using an enzyme. The present invention also provides process for the preparation of Ezetimibe comprising the steps of a) protecting the compound (S)-5-(4-Fluoro-phenyl)-5-hydroxy-1morpholin-4-yl-pentan-1-one with hydroxy protecting group b) hydrolyzing the obtained compound c) condensing with a chiral auxiliary d) reacting with an protected imine compound e) converting to alkyl ester f) cyclizing and g) deprotecting to obtain Ezetimibe.

Abstract: The present disclosure relates to non-naturally occurring polypeptides useful for preparing Ezetimibe, polynucleotides encoding the polypeptides, and methods of using the polypeptides.

Abstract: Carbon-containing materials, such as biomass (e.g., plant biomass, animal biomass, and municipal waste biomass) or coal are processed to produce useful products, such as fuels, carboxylic acids and equivalents thereof (e.g., esters and salts). For example, systems are described that can use feedstock materials, such as cellulosic and/or lignocellulosic materials and/or starchy materials, to produce ethanol, butanol or organic acids (e.g., acetic or lactic acid), salts of organic acids or mixtures thereof. If desired, organic acids can be converted into alcohols, such as by first converting the acid, salt or mixtures of the acid and its salt to an ester, and then hydrogenating the formed ester. Acetogens or homoacetogens which are capable of utilizing a syngas from a thermochemical conversion of coal or biomass can be utilized to produce the desired product.

Abstract: Genes SWA2 and GAM1 from the yeast, Schwanniomyces occidentalis, encoding ?-amylase and glucoamylase, respectively, were cloned and expressed in H. polymorpha. The expression was achieved by integration of the SWA2 and GAM1 genes into the chromosome of H. polymorpha under operably linked to a strong constitutive promoter of the H. polymorpha-glyceraldehyde-3-phosphate dehydrogenase gene (HpGAP. Resulting transformants acquired the ability to grow on a minimal medium containing soluble starch as a sole carbon source and can produce Ethanol at high-temperature fermentation from starch up to 10 g/L. A XYN2 gene encoding endoxylanase was obtained from the fungus Trichoderma resee, and a xlnD gene coding for ?-xylosidase was obtained from the fungus Aspergillus niger. Co-expression of these genes was also achieved by integration into the H. polymorpha chromosome under control of the HpGAP promoter.

Abstract: The present disclosure provides engineered transaminase polypeptides for the production of amines, polynucleotides encoding the engineered transaminases, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases to prepare compounds useful in the production of active pharmaceutical agents.

Abstract: The present disclosure relates to an enzyme derived from Candida bombicola that is capable of lactonizing or polymerizing carbohydrate-containing compounds, lipids, fatty acids, hydroxylated fatty acids, alcohols, dicarboxylic acids or mixtures thereof. Hence, host cells comprising the latter enzyme can be used, via the formation of intra- or inter-molecular ester-bounds, to produce, for example, lactonized sophorolipids or polymers of acidic sophorolipids. On the other hand, host cells having lost their capability to produce a functional enzyme disclosed herein can be used to produce 100% acidic sophorolipids.

Abstract: The present disclosure relates to biocatalysts and its uses for the efficient preparation of eslicarbazepine, eslicarbazepine acetate, and analogs thereof.

Abstract: The present disclosure relates to polypeptides having transaminase activity, polynucleotides encoding the polypeptides, and methods of using the polypeptides.

Abstract: Chromogenic or fluorescent carbapenems according to formula I, wherein Ar is a mono or disubstituted carbocyclic aromatic group or an optionally mono or disubstituted heterocyclic aromatic group, are useful compounds for the detection of bacterial carbapenemase.

Abstract: The invention relates to an enzyme that comprises or includes a sequence according to SEQ. ID No. 1 or SEQ. ID No. 2, to a method for the production thereof, and to the use thereof as a catalyst in the oxidative cleavage of vinyl aromatics.

Abstract: The present invention relates to a novel amino acid dehydrogenase, DNA encoding the enzyme, and a transformant having the DNA introduced therein. The present invention also relates to a process for producing an L-amino acid, 2-oxo acid or D-amino acid, which includes allowing the amino acid dehydrogenase or a microorganism or transformant capable of producing the enzyme to act on a substrate compound. The amino acid dehydrogenase has good reactivity even with an amino acid or a 2-oxo acid each having a bulky side chain such as an aromatic-ring-containing group, which acids are poorly reactive with conventional amino acid dehydrogenases. The amino acid dehydrogenase enables the inexpensive and highly efficient production of a useful optically active amino acid.

Abstract: In a process for the enantioselective enzymatic reduction of a hydroxy ketone of general formula I wherein R1?C1-C6 alkyl and R2?—Cl, —CN, —OH, —H or C1-C6 alkyl, into a chiral diol of general formula II wherein R1 and R2 have the same meaning as in formula I, the hydroxy ketone is reduced with an oxidoreductase in the presence of NADH or NADPH as a cofactor, wherein a) the hydroxy ketone is provided in the reaction at a concentration of ?50 g/l, b) the oxidized cofactor NAD or NADP having formed is regenerated continuously by oxidation of a secondary alcohol of general formula RXRYCHOH, wherein RX, RY independently represent hydrogen, branched or unbranched C1-C8-alkyl and Ctotal?3, and c) the reduction of the hydroxy ketone and the oxidation of the secondary alcohol are catalyzed by the same oxidoreductase.

Abstract: The invention relates to enzymatic methods for hydroxylation in position 2 or 3 of substituted or unsubstituted, linear or branched aliphatic hydrocarbons.

Abstract: The present invention provides a nucleic acid molecule comprising: (a) a nucleotide sequence as shown in SEQ ID No. 1; or (b) a nucleotide sequence which is the complement of SEQ ID No. 1; or (c) a nucleotide sequence which is degenerate with SEQ ID No. 1; or (d) a nucleotide sequence having at least 85% sequence identity (preferably at least 87%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity) with SEQ ID No. 1; or (e) a part of any one of (a) to (d), wherein said nucleic acid molecule encodes or is a complementary to a nucleic acid molecule encoding one or more polypeptides, or comprises or is complementary to a nucleic acid molecule comprising one or more genetic elements, having functional activity in the synthesis of a polyketide-based or macrolactam molecule.

Abstract: The present invention relates to a method for purifying target protein which contains electron transfer protein, from a protein solution containing the target protein, by means of liquid chromatography. The liquid chromatography is performed as follows: First, the protein solution is introduced into a column which is filled with a packing agent, thereby causing the packing agent to bond to the target protein. Then, impurities are removed, and then the target protein is eluted from the packing agent in an eluent which contains a hydroxy-cholate. An example of the target protein is glucose dehydrogenase which contains a protein having glucose dehydrogenation activity. The liquid chromatography is performed as a combination of hydrophobic chromatography and anion exchange chromatography.

Abstract: Escherichia. coli mutants which can be used for the synthesis of D-amino acids, and to such a process. The mutants are distinguished by deficiencies in particular enzymes which break down D-amino acids and include those which produce D-amino acids via the carbamoylase/hydantoinase route.