47 results about "Amine oxidase" patented technology

The present invention relates to novel compounds which are capable of inhibiting semicarbazide-sensitive amine oxidase and myeloperoxidase. These compounds are useful for the treatment of a variety of inflammatory indications, e.g., autoimmune diseases, respiratory disease, fibrosis, vasculitis, neurological diseases or disorders, and the complications resulting from infectious disease, obesity, diabetes / metabolic syndrome and / or cardiovascular disease in human subjects as well as in pets and livestock. In addition, the present invention relates to pharmaceutical compositions containing these compounds, as well as various uses thereof.

The present invention relates to novel compounds which are capable of inhibiting certain amine oxidase enzymes. These compounds are useful for treatment of a variety of indications, e.g., fibrosis, cancer and / or angiogenesis in human subjects as well as in pets and livestock. In addition, the present invention relates to pharmaceutical compositions containing these compounds, as well as various uses thereof.

The invention provides preparation and application of a novel MAO-B inhibitor containing a tetrahydronaphthalene-1-amine structure, and belongs to the field of medicine. The derivative is a compound as shown in a formula I, or a pharmaceutically acceptable salt thereof, or a stereoisomer thereof. The compound disclosed by the invention can be used for inhibiting MAO (monoamine oxidase), and particularly can be used for selectively inhibiting MAO-B; the compound can be used for treating Parkinson's disease, Alzheimer's disease, emotional disorder and other diseases, and has a good application prospect.

The invention relates to the technical field of bioengineering, in particular to a process for continuously producing nicotine based on immobilized enzyme. The immobilized microbial agent comprises a composite carrier, an engineering strain and an immobilized auxiliary agent, in the process for continuously producing nicotine based on immobilized enzyme, amine oxidase of an engineering strain is subjected to site-specific modification, so that spatial structure deformation when the amine oxidase is combined with a carrier is reduced, and a three-dimensional network structure of hydroxyethyl chitosan-guar gum composite microspheres in the composite carrier is matched to provide an adaptive microenvironment; the activity loss of enzyme molecules caused by steric hindrance or structural change is reduced; in the immobilization auxiliary agent, gallic acid and an enzyme molecule sulfydryl form a coordinate bond to maintain an active center conformation, glutaraldehyde and polyethyleneimine enhance the binding stability through a crosslinking effect and charge regulation, and the maintaining effect of enzyme activity during continuous production is improved, so that the enzyme activity loss in the immobilization process is reduced, and the immobilization efficiency is improved. The stability of the enzyme in long-term continuous reaction is enhanced.

The invention provides mutant monoamine oxidase and application thereof in synthesis of chiral amine compounds. Specifically, the invention provides monoamine oxidase or a mutant thereof capable of efficiently catalyzing a desymmetric oxidation reaction of 3-azabicyclo [3.3. 0] octane. The monoamine oxidase or the mutant of the monoamine oxidase can be used for efficiently catalyzing 3-azabicyclo [3.3. 0] octane to be subjected to desymmetric oxidation to form (3S, 7R)-3-azabicyclo [3.3. 0] octyl-2-ene, so that the monoamine oxidase or the mutant of the monoamine oxidase can be used for producing chiral amines such as telaprevir intermediates or other chiral amine precursors.

The application discloses a preparation process of rice wine fermentation and relates to the technical field of rice wine preparation, and comprises the following steps: S1, a circulating fermentation activator is prepared; S2, the circulating fermentation activator is introduced into a digestion treatment procedure, a porous carrier is loaded with non-amine-producing competitive lactic acid bacteria biofilm and covalently immobilized amine oxidase; S3, according to the risk level of a coupling risk value, a corresponding digestion strengthening procedure is triggered; and S4, the circulating fermentation activator treated by the digestion treatment procedure is added back to a new batch of fermentation substrate. The application prepares the circulating fermentation activator by directional complex enzymolysis treatment of the distiller's grains generated after rice wine fermentation, and the non-amine-producing competitive lactic acid bacteria biofilm and the covalently immobilized amine oxidase are loaded on the porous carrier, so that the biological amine in the circulating system is subjected to directional digestion, and the problems of excessive accumulation of biological amine and deterioration of rice wine flavor caused by direct reuse of the distiller's grains in the prior art are solved.

The present invention relates to a recombinant human diamine oxidase (DAO) with reduced glycosaminoglycan binding affinity, said DAO comprising at least one amino acid modification in the glycosaminoglycan (GAG)-binding domain. The present invention further relates to the use of DAO in the treatment of conditions associated with excess histamine, particularly in the treatment of chronic allergic diseases, more particularly in the treatment of anaphylaxis, anaphylactic shock, chronic urticaria, acute urticaria, asthma, hay fever, allergic rhinitis, allergic conjunctivitis, histamine poisoning, headache, atopic dermatitis, inflammatory diseases, mastocytosis, mast cell activation syndrome (MCAS), pre-eclampsia, hyperemesis gravidarum, preterm labor, peptic ulcer, acid reflux, pruritus, and sepsis.

The present invention provides recombinant Escherichia coli for producing glutarate, a construction method and use thereof. A double-plasmid recombinant bacterium is constructed through molecular biological means for co-expressing an aldehyde synthase (AAS) gene, an amine oxidase Mao (gene) and an aldehyde dehydrogenase (Glox) gene. The constructed expression plasmids are introduced into the Escherichia coli to reconstruct to obtain recombinant cells. A recombination strain for efficiently producing glutarate is obtained through amicillin resistance and kanamycin resistance combined plate screening. Efficient production of the glutarate is achieved by optimizing concentration of a substrate, cell concentration and a transformation temperature. L-lysine with a concentration of 30 g / L may be transformed into 19.65 g of glutarate through reactions for 30 h under transformation conditions that the cell concentration is 30 g / L, the pH value is 8 and 6 mM of NAD+ is additionally added, wherein a transformation rate may be 65.3%.

The invention provides a monoamine oxidase mutant, recombinant yarrowia lipolytica and application of the monoamine oxidase mutant and the recombinant yarrowia lipolytica. Monoamine oxidase is subjected to site-directed mutagenesis modification by searching a key catalytic pocket, so that the catalytic efficiency of monoamine oxidase is improved, and biosynthesis of bovine heart alkali is increased; finally, the Phe208Ala mutant is obtained, and the capacity of synthesizing bovine heart alkali by utilizing a genetic engineering strain constructed by the mutant is obviously improved; an MAO-A wild type and a MAO-A mutant are respectively expressed and designed in engineering bacteria, the ability of the mutant for catalyzing dopamine to generate bovine heart alkali in yarrowia lipolytica is compared, and the result shows that the monoamine oxidase mutant can significantly improve the yield of the yarrowia lipolytica bovine heart alkali, the yield is significantly improved by 40.05% compared with an original strain, and the monoamine oxidase mutant has a good application prospect. The method has better performance, can significantly improve the yield of biosynthesized phylline, is more suitable for industrial application in the future development process, and can significantly reduce the production cost and improve the production efficiency.

The present invention discloses a Lactobacillus plantarum expressing a signal molecule AI-2 and its application, and belongs to the field of microbial technology. The present invention is to provide a new lactic acid bacteria that can produce diamine oxidase in high yield and has a strong degradation ability for putrescine, cadaverine and histamine in air-dried sausages, Lactobacillus plantarum expressing the quorum sensing signal molecule AI-2. The present invention discloses a Lactobacillus plantarum expressing the signal molecule AI-2, and the Lactobacillus plantarum is named Lactobacillus plantarum SH7, with a preservation number of CGMCC NO.28113, and is deposited in the China General Microbiological Collection Center on August 7, 2023. Lactobacillus plantarum SH7 has significant amine-reducing properties, and the extracellular diamine oxidase activity is 615.24U / g protein, which can be used as a starter to reduce the content of biogenic amines in the production of fermented meat products.

This invention relates to the field of food labeling technology, and more particularly to a smart label assembly and its preparation method. A smart label assembly includes: a substrate layer, a color-developing layer, and a protective layer; the color-developing layer is fixed to the surface of the substrate layer, and the protective layer covers the surface of the color-developing layer; the color-developing layer includes: an amine oxidase-type color-developing area and a glucose oxidase-type color-developing area. When livestock and poultry meat spoils and produces volatile amines and glucose degradation products, these two types of substances are catalyzed by amine oxidase and glucose oxidase, respectively, to produce ammonia and hydrogen peroxide, which then react with indicators on the label to produce color changes. The two types of labels are used together for mutual verification, forming a rapid detection method for livestock and poultry meat spoilage using smart labels, which can directly determine the quality of livestock and poultry meat. This label is simple to prepare, low in cost, and suitable for fresh livestock and poultry meat packaging, allowing monitoring from the freshness stage.

This application relates to the field of air purification technology, specifically to a biomedical-based odor-removing and antibacterial air freshener, mainly composed of the following raw materials in parts by weight: 2.5-5.5 parts modified lysozyme microcapsules, 2.5-4.5 parts modified quaternary ammonium salt-β-cyclodextrin inclusion complex, 1.5-2.5 parts plasma amine oxidase, 2.0-3.5 parts compound plant extract, 0.2-0.3 parts citric acid, 0.5-0.6 parts lactic acid, and the balance being food-grade deionized water; the air freshener has a pH value of 6.0-8.5. The mist particle size is 10-50μm; the air freshener does not contain fragrances, alcohol, pigments, preservatives, chlorine disinfectants, hypochlorous acid, drugs, hormones and other irritating ingredients. All raw materials and modified carriers are food-grade and edible. Through a triple deodorization system of plasma amine oxidase, β-cyclodextrin and compound plant extracts, the ammonia removal rate is ≥95%, the odor suppression time is ≥100h, the product has a skin irritation level of 0, and the acute oral toxicity LD50 is >5000mg / kg, achieving a balance between mild and non-irritating properties and highly effective sterilization.

The present invention relates to novel bioprobes which are capable of binding to certain amine oxidase enzymes. These bioprobes are useful in methods of detecting and determining the concentration of certain amine oxidase enzymes in a sample as well as in methods for the quantitative assessment of inhibition of certain amine oxidases.

The present invention provides a series of monoamine oxidases (PMAON) with high catalytic activity and strong chiral selectivity, which are derived from Penicillium, as well as a method for stereoselectively preparing 6,6-dimethyl-3-azabicyclo[3.1.0]hexene compounds using the enzyme. The present invention also provides genes encoding the series of monoamine oxidases, recombinant expression vectors containing the series of genes, recombinant expression transformants and methods for preparing the same.

The invention discloses preparation and application of alcohol-resistant amine oxidase LYYOBN2 capable of degrading biogenic amine, and belongs to the technical field of molecular biology. The invention provides the amine oxidase from bacillus, and the expression of the amine oxidase in escherichia coli is realized. According to the application of the prepared amine oxidase to degradation of the biogenic amine, the enzyme is added into fermented food, the biogenic amine can be effectively degraded in an environment containing ethanol or NaCl, an enzyme library for degrading the biogenic amine can be expanded, and the safety of the fermented food is further improved.

The invention provides a production method of p-hydroxyacetophenone, which comprises the following steps of: co-expressing phenylalanine amino mutase, L-aspartic acid-beta-decarboxylase, monoamine oxidase and catalase in escherichia coli, converting L-tyrosine into (R)-3-amino-3-(4-hydroxyphenyl) propionic acid through TAM (Transcriptional Amplification Molecule), and converting the (R)-3-amino-3-(4-hydroxyphenyl) propionic acid into (R)-3-amino-3-(4-hydroxyphenyl) propionic acid. According to the method, (R)-3-amino-3-(4-hydroxyphenyl) propionic acid is converted into (R)-4-(1-aminoethyl) phenol through ADC, (R)-4-(1-aminoethyl) phenol is converted into p-hydroxyacetophenone through AOD, and generated hydrogen peroxide is removed through CAT. According to the method, the reaction process is simple, no coenzyme needs to be added, the selected enzyme has the advantages of being high in activity, high in optical specificity and the like, and the p-hydroxyacetophenone is produced through conversion of the recombinant bacterium, so that the method is high in production efficiency, environmentally friendly, low in cost and good in industrial application prospect.

The present invention relates to the field of biosynthesis technology, and particularly to a method for preparing S-nicotine. The present invention creatively uses amine oxidase to oxidize 1-methylpyrrolidine into the corresponding imine, and then under the catalysis of nicotine synthase, condenses and decarboxylates the imine with nicotinic acid to obtain the final product S-nicotine. This method can obtain chirally specific S-nicotine through two-step reactions in a single reaction system, with a short synthesis route, high yield, mild reaction conditions and easy large-scale production; at the same time, the raw materials are widely sourced, inexpensive, with low production costs, environmentally friendly, significantly reducing the production cost of nicotine while also making it more in line with the requirements of today's green industrial production.

The invention belongs to the technical field of protein engineering modification, and particularly relates to a method for improving thermal stability of amine oxidase ACAO and a mutant. Compared with a wild type enzyme, the temperature tolerance of the mutant enzyme in a certain temperature range is superior to that of the wild type enzyme, and the thermal stability is remarkably improved. Through molecular modification on a wild type, the thermal stability of amine oxidase ACAO mutant enzyme is remarkably improved. The enzyme is mainly applied to the industries of food production, livestock feed processing and the like so as to reduce the harm of fumonisins to the health of animals and human beings. The thermal stability improved amine oxidase ACAO mutant obtained by the invention is beneficial to improving the production efficiency of continuous production of enzyme in actual industrial application, has good industrial application prospects, and lays a foundation for further research on the structure of amine oxidase.

The invention discloses preparation and application of salt-tolerant amine oxidase KCYOBN sourced from bacillus subtilis and capable of degrading biogenic amine, and belongs to the technical field of molecular biology. The invention provides the amine oxidase from bacillus subtilis, and the expression of the amine oxidase in escherichia coli is realized. The invention also provides an application of the amine oxidase in degradation of biogenic amines, the amine oxidase is added into fermented food, the biogenic amines can be effectively degraded, an enzyme library for degrading the biogenic amines can be expanded, and the safety of the fermented food is further improved.

The invention provides a diamine oxidase detection probe and a kit. The diamine oxidase detection probe with the chemical structure as shown in the formula (I) can perform fluorescence color development and has an absorption peak value within the range of 592-602nm, and the absorption peak value is close to 596nm. And the diamine oxidase can oxidize the diamine oxidase detection probe as shown in the formula (I), so that light absorption within the range of 592-602nm disappears. The diamine oxidase detection probe with the chemical structure as shown in the formula (I) is stable in structure and beneficial to storage. The diamine oxidase detection probe with the chemical structure shown in the formula (I) can be applied to diamine oxidase detection. And a detection method is provided for taking the serum diamine oxidase (DAO) level as an early diagnosis index of intestinal mucosal injury.

The present invention provides preparation of a semicarbazide-sensitive amine oxidase inhibitor and use thereof. In particular, disclosed in the present invention are a compound as represented by formula I, or a stereoisomer or a racemate or a pharmaceutically acceptable salt of the compound. Also disclosed in the present invention is that the compound can inhibit semicarbazide-sensitive amine oxidase.

The invention discloses a preparation method for reducing biogenic amine in red intestines by using lactobacillus plantarum diamine oxidase. The preparation method comprises the following steps: culturing lactobacillus plantarum SH7, extracting and purifying the diamine oxidase and applying the diamine oxidase to the red intestines. High-activity enzyme powder is obtained through ammonium sulfate salting-out and anion exchange chromatography and added into the sausage raw material, biogenic amine is effectively degraded, the safety of the sausage is improved, and the product quality is not affected. The method is simple in process and suitable for industrial production, and provides a new way for biogenic amine control of fermented meat products.

This invention relates to a method and application of nicotine conversion based on a co-immobilized multi-enzyme cascade system. The method includes the following steps: adding a co-immobilized multi-enzyme catalyst to a reaction system containing nicotine; the co-immobilized multi-enzyme catalyst includes nicotine dehydrogenase carrying an AviTag tag, pseudooxynicotine amine oxidase, 3-succinyl hemialdehyde pyridine dehydrogenase – SpyCatcher, and aldehyde-ketone reductase – SpyTag; in NADP... + The reaction was carried out in a buffer solution in the presence of a sacrificial substrate; after the reaction, the reaction solution was separated and purified to obtain the product 3-succinylpyridine. This invention significantly reduces NADP. + The coenzyme dosage was adjusted, and the co-immobilized multi-enzyme catalyst exhibited excellent pH and thermal stability as well as recyclability, achieving efficient and targeted conversion of nicotine. This provides a new technical approach for the resource utilization of nicotine from tobacco waste and the green preparation of 3-succinylpyridine.

This invention provides a novel MAO-B inhibitor containing a tetrahydronaphthalene-1-amine structure, its preparation and uses, belonging to the pharmaceutical field. The derivative is a compound represented by Formula I, a pharmaceutically acceptable salt thereof, or a stereoisomer thereof. The compound of this invention can be used to inhibit monoamine oxidase (MAO), particularly selectively inhibiting MAO-B; it has promising applications in the treatment of Parkinson's disease, Alzheimer's disease, mood disorders, and other diseases.

A preparation method of immobilized amine oxidase relates to the technical field of amine oxidase, and comprises the following steps: S1, taking Fe3O4 nanoparticles, H3TATB and Tb (NO3) 3.5 H2O as raw materials, and carrying out solvothermal synthesis reaction in a mixed solvent of DMA, methanol and water to obtain a Fe3O4 (at) Tb-mesoMOF crystal; s2, the Fe3O4 (at) Tb-mesoMOF crystal prepared in the step S1 is immersed in an AOs solution containing an HEPES buffer solution for adsorption, and after full adsorption, AOs-Fe3O4 (at) Tb-mesoMOF is obtained; the invention further provides the immobilized amine oxidase and application thereof in biogenic amine degradation, the prepared immobilized amine oxidase is high in biogenic amine degradation catalysis efficiency, easy and convenient to operate and capable of being recycled, the problem that the biogenic amine content in fermented food is too high can be solved, and the production process and conditions do not need to be changed.

The present application relates to a kind of collagen hydrogel and its preparation method and application, the preparation method includes the following steps: (1) using amine oxidase catalytic collagen oxidation deamination generates unsaturated aldehyde group functional group, intramolecular or intermolecular crosslinking occurs, completes first crosslinking;(2) the product of first crosslinking occurs secondary crosslinking under the catalysis of carboxyl activating agent, obtains the collagen hydrogel.In the present application, the collagen hydrogel prepared by the method is pure collagen hydrogel, solidification speed is fast, biocompatibility is good (excellent bionics), mechanical strength is adjustable, structure size is adjustable, stability is good, and application range is wide.

The invention provides a construction method of a monoamine oxidase A (MAOA) gene site-directed mutagenesis mouse model. The construction method comprises the following steps: mutating a 1410th base T of a mouse monoamine oxidase A gene into a base C through a CRISPR / Cas gene editing technology, and optionally mutating a 1401st base C of the mouse monoamine oxidase A gene into a base A, the 1413th basic group A of the mouse monoamine oxidase A gene is mutated into a basic group C. The site-directed mutagenesis mouse shows unique physiological and pathological phenotypes, and can be used for researching biological function changes caused by single nucleotide polymorphism of the MAOA gene.

Provided in the present invention are preparation and use of a novel MAO-B inhibitor containing a tetralin-1-amine structure, which belong to the field of medicines. The derivative is a compound represented by formula I, or a pharmaceutically acceptable salt thereof, or a stereoisomer thereof. The compound of the present invention can be used for inhibiting monoamine oxidase (MAO), especially selectively inhibiting MAO-B. The compound can be used for treating diseases such as Parkinson's disease, Alzheimer's disease, and emotional disorders, and exhibits good application prospects.

This invention provides a monoamine oxidase mutant and a recombinant *Yarrowia lipolytica* strain, along with their applications. By identifying key catalytic pockets, site-directed mutagenesis was performed on the monoamine oxidase to improve its catalytic efficiency and increase the biosynthesis of calciferine. The Phe208Ala mutant was ultimately obtained, and the genetically engineered strain constructed using this mutant showed a significantly enhanced ability to synthesize calciferine. The wild-type MAO-A and the designed MAO-A mutant were expressed in the engineered strain, and their ability to catalyze the conversion of dopamine to calciferine in *Yarrowia lipolytica* was compared. The results showed that the monoamine oxidase mutant significantly increased the yield of calciferine in *Yarrowia lipolytica*, with a 40.05% increase compared to the starting strain. This improved performance significantly enhances the biosynthetic yield of calciferine and is more suitable for industrial applications in the future, potentially reducing production costs and increasing production efficiency.

The invention discloses a biogenic amine detection kit based on double-enzyme nanoparticles as well as a preparation method and application of the biogenic amine detection kit. The biogenic amine detection kit based on the double-enzyme nanoparticles comprises a biogenic amine recognition agent, a color developing agent and a solvent, the biogenic amine recognition agent is horse radish peroxidase / diamine oxidase-zinc phosphate nanoparticles, the color developing agent is dopamine, and the kit can specifically recognize histamine and diamine biogenic amine and can be used for detecting the content of histamine and diamine biogenic amine in a sample; when the biogenic amine detection kit is used for biogenic amine content detection, the cost is low, the operation is simple and rapid, the detection kit is environment-friendly, expensive detection equipment and professional technicians are not needed, the result can be obtained in the whole detection process within a short time, and the biogenic amine detection kit is suitable for rapid detection of biogenic amine in food.