36 results about "Cinnamyl-alcohol dehydrogenase" patented technology

A method for producing an L-amino acid is described, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan, or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of a wild-type alcohol dehydrogenase encoded by the adhE gene or a mutant alcohol dehydrogenase which is resistant to aerobic inactivation.

The present invention relates to recombinant microorganisms comprising biosynthetic pathways and methods of using said recombinant microorganisms to produce various beneficial metabolites. In various aspects of the invention, the recombinant microorganisms may further comprise one or more modifications resulting in the reduction or elimination of 3 keto-acid (e.g., acetolactate and 2-aceto-2-hydroxybutyrate) and/or aldehyde-derived by-products. In various embodiments described herein, the recombinant microorganisms may be microorganisms of the Saccharomyces clade, Crabtree-negative yeast microorganisms, Crabtree-positive yeast microorganisms, post-WGD (whole genome duplication) yeast microorganisms, pre-WGD (whole genome duplication) yeast microorganisms, and non-fermenting yeast microorganisms.

The invention discloses an alcohol dehydrogenase, a gene thereof, a recombinant expression vector and a recombinant expression transformant respectively containing the gene, a recombinase of the alcohol dehydrogenase, and an application of the alcohol dehydrogenase in asymmetric reduction synthesis of chiral diaryl secondary alcohol as a catalyst, and belongs to the technical field of bioengineering. The alcohol dehydrogenase is from Kluyveromyces sp. CCTCCM2011385, has a carbonyl group reduction function, and also has a hydroxy group oxidation function. Extra addition of glucose dehydrogenase and other enzymes used for cofactor circulation is not needed when the alcohol dehydrogenase is used in the reduction of diaryl ketone into the chiral diaryl secondary alcohol as a biocatalyst, and the alcohol dehydrogenase has the advantages of high catalysis efficiency, mild reaction conditions, easy product recovery and low cost, so the alcohol dehydrogenase has very good application and exploitation prospect in the production of antihistamine medicines.

The present invention relates to a multi-stage process for producing substituted, optically active alcohols, comprising an enzyme-catalyzed synthesis step, in particular a synthesis step which is catalyzed by an alcohol dehydrogenase. The inventive method is particularly suitable for producing phenylephrine, i.e. 3-[(1R)-1-hydroxy-2-methylamino-ethyl]-phenol.

The present invention provides for a transgenic non-human animal whose cells contain a recombinant DNA sequence comprising a nerve tissue specific promoter operatively linked to a DNA sequence which encodes amyloid-beta peptide alcohol dehydrogenase (ABAD), and exhibits at least one phenotype from the group consisting of: overexpression of ABAD, elevated levels of basal ATP; protection from metabolic or ischemic stress.

The invention provides an alcohol dehydrogenase with high catalytic activity, strong enantiotropic selectivity and good substrate tolerance, and provides an enzymatic synthesis method of employing the alcohol dehydrogenase to catalyze and synthesize (s)-3-substituted amido-1-(thiophenyl-2-yl)-1- propanol and furthermore Duloxetine. The invention also provides a nucleic acid sequence for encoding the alcohol dehydrogenase, a recombinant expression vector including the nucleic acid sequence, and a recombinant expression transformant, and a preparation method of the alcohol dehydrogenase, and uses of the alcohol dehydrogenase in catalyzing asymmetric reduction of carbonyl substrates. The invention has advantages that the product concentration is high, the optical purity of the product is high, the reaction condition is mild and environment-friendly, the operation is convenient and is easy to industrialize, and an extra expensive coenzyme NADP<+>/NAD<+> is not necessary.

The invention concerns the use of duplex oligonucleotides about 25 to 30 base pairs to introduce site specific genetic alterations in plant cells. The oligonucleotides can be delivered by mechanical (biolistic) systems or by electrpoporation of plant protoplasts. Thereafter plants having the genetic alteration can be generated from the altered cells. In specific embodiments the invention concerns alteration in the gene that encode acid invertase, UDP-glucose pyrophosphorylase, polyphenol oxidase, O-methyl transferase, cinnamyl alcohol dehydrogenase, ACC synthase and ACC oxidase or etr-1 or a homolog of etr-1, and plants having isolated point mutations in such genes.

Loblolly pine (Pinus taeda L.) is the most important commercial tree species in the USA harvested for pulp and solid wood products. Increasing the efficiency of chemical pulping may be achieved through the manipulation of genes involved in the lignin biosynthetic pathway. A null allele of cinnamyl alcohol dehydrogenase (CAD) has been discovered in the loblolly pine clone 7-56 which displays altered lignin composition. During identification of single nucleotide polymorphisms (SNPs) in the cad gene, a two-base pair adenosine insertion located in exon five and unique to clone 7-56 was discovered. The sequence mutation causes a frame-shift predicted to result in premature termination of the protein. For routine detection of the mutation, a diagnostic assay was developed utilising Template-directed Dye-terminator Incorporation and Fluorescence Polarization detection (FP-TDI).

The invention discloses an alcohol dehydrogenase embedded gelatin-silica hybrid gel and a preparation method thereof. According to invention, the grain diameter of the alcohol dehydrogenase embedded gelatin-silica hybrid gel is 3-4mm, and a silica coating is coated on a gelatin core. The preparation method comprises the following steps of: preparing a mixed solution of gelatin and alcohol dehydrogenase; preparing a mixed solution of sodium silicate and a glutaraldehyde solution precursor; adding the mixed solution of gelatin and alcohol dehydrogenase into deionized water at a temperature of 0-4 DEG C droplet by droplet to generate alcohol dehydrogenase embedded gelatin gel particles; stirring and incubating to obtain the alcohol dehydrogenase embedded gelatin-silica hybrid gel. The preparation method has the advantages that the preparation condition is mild, the preparation process is simple and feasible, and the alcohol dehydrogenase embedded gelatin-silica hybrid gel has a strong fixing capability; compared with gelatin gel, the hybrid gel has a lower leakage rate of immobilized alcohol dehydrogenase, and lower swelling degree and better recycling stability.

The invention discloses a cinnamyl alcohol dehydrogenase of wheat and an encoding gene and application thereof; the cinnamyl alcohol dehydrogenase is the protein of the following a) or b): a) the protein composed of the amino acid sequences represented by the sequences 2 in the sequence table; b) the protein derived from a) and related to the cinnamyl alcohol dehydrogenase function by substituting and/or deleting and/or adding one or more amine acid in the amino acid sequences represented by the sequences 2 in the sequence table. The invention further provides the encoding gene of the cinnamyl alcohol dehydrogenase, and application of the encoding gene in culturing lodging-resistant plants. The encoding gene is introduced in the plants; and the transformed plant hosts can be wheat. The protein in the invention utilizes coniferyl aldehyde as base materials and has enzyme activities of 94.49 nmol/sec/mg, showing that the protein can control the lignin synthesis of the wheat. Northern hybridization is carried out on the Ta-CADI genes of the stems of easily-lodging and lodging-resistant wheat, which shows that the Ta-CADI genes not only control the lignin synthesis of the wheat, but also are closely related to the lodging-resistant characteristics of the stems of the wheat.

This invention relates to an isolated nucleic acid fragment encoding a lignin biosynthetic enzyme. The invention also relates to the construction of a chimeric gene encoding all or a portion of the lignin biosynthetic enzyme, in sense or antisense orientation, wherein expression of the chimeric gene results in production of altered levels of the lignin biosynthetic enzyme in a transformed host cell.

The invention provides a preparation method of ADH (alcohol dehydrogenase) and GDH (glucose dehydrogenase) co-crosslinked enzyme aggregates. Specifically, a supernatant obtained after high-density fermentation and wall-breaking centrifugation is taken as a crude enzyme liquid, ADH and GDH in the crude enzyme liquid are subjected to glutaraldehyde cross-linking for preparation of the co-crosslinkedenzyme aggregates, and enzyme activity recovery of the co-crosslinked enzyme aggregates is increased to 82% by adding Tween 80.

The invention discloses alcohol dehydrogenase. The nucleotide sequence of the alcohol dehydrogenase is shown in SEQ ID NO.1. The amino acid sequence of the alcohol dehydrogenase is shown in SEQ ID NO.2. The invention further discloses application of the alcohol dehydrogenase in a reaction for synthesizing alcohol with aldehyde as a substrate. The novel recombinant alcohol dehydrogenase has efficient soluble expression capability in an escherichia coli expression system, and the conversion rate of the recombinant alcohol dehydrogenase for synthesizing the alcohol in an aldehyde reducing reaction system is 90% or so.

The invention relates to a method for improving quality of cotton fibers by overexpressing GhCAD6 gene, belonging to the technical field of biology. The method comprises the following steps: constructing a plant overexpression vector pCAMINBIA-2300-GhCAD6 from styrone dehydrogenase gene GhCAD6 in cotton fibers, transforming the vector into agrobacterium LB4404 by agrobacterium mediation, and integrating into cotton to obtain the trans-styrone dehydrogenase gene cotton plant. The field and molecular detection analysis detects that the lignin content in cotton fibers obviously increases in different development periods, the fibrocyte wall thickness obviously decreases in the cotton secondary wall rapid deposition stage, and the ripe cotton fiber surface becomes more compact and smooth. The method can maximally enhance the length of the cotton fibers by 16.935%, enhance the specific strength by 25.10% and enhance the fiber yield by 3.80%, thereby greatly improving the quality of the cotton fibers.

The invention relates to the technical field of dehydrogenase mutants, in particular to a novosphingobium short-chain alcohol dehydrogenase mutant and an application thereof. The novosphingobium short-chain alcohol dehydrogenase mutant adopts the amino acid sequence of novosphingobium short-chain alcohol dehydrogenase NA-ADH as a template. The short-chain alcohol dehydrogenase mutant of a marine origin is obtained by site-directed mutagenesis. The mutuant is transferred into an expression strain BL21 (DE3) to obtain thalli containing the recombinant short-chain alcohol dehydrogenase after recombination by an expression vector, and then beta-hydroxytetradecanoate is used as a substrate to prepare (R)-beta-hydroxytetradecanoate by bio-enzyme catalysis, the chiral ee value of the obtained (R)-beta-hydroxytetradecanoate can reach above 99, and the substrate conversion rate is above 95%. The preparation conditions are mild, and the process way is simple.

The invention discloses a method for increasing thermal stability of polymer protein and alcohol dehydrogenase with increased thermal stability, which belong to the technical field of enzyme engineering. The method for increasing the thermal stability of polymer protein is characterized in that a covalent bond mode is introduced into a contact interface of terminal N of polymer protein with adjacent N terminals (in a scope of 8 angstrom) and an internal subunit, and the subunits of polymer protein are linked to form a cyclized integral body. The sequences of alcohol dehydrogenase with increased thermal stability are respectively SEQ ID NO.2, SEQ ID NO.3 or SEQ ID NO.4, compared with a wild type, a T5015 value of the alcohol dehydrogenase can be respectively increased by 5.5 DEG C, 6.0 DEGC and 18 DEG C. The method avoids the problems of large screening work amount and tedious processes in the prior art, and site-specific mutagenesis has pertinency by a strategy introduced through a disulfide bond between interfaces.