28 results about "Amine oxidase" patented technology

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 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.

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 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 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 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.

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.

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 present invention relates to novel compounds which are capable of inhibiting semicarbazide-sensitive amine oxidase (SSAO / VAP-1) and monoamine oxidase B (MAO-B). These compounds are useful for treatment of a variety of neuromuscular diseases, such as muscular dystrophies, and neuroinflammatory diseases, including both peripheral and central disorders 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 discloses a substituted coumarin-eugenol derivative as well as a preparation method and application thereof. The derivative is prepared by connecting a coumarin mother nucleus and eugenol through a flexible chain by virtue of a two-step nucleophilic substitution reaction. The derivative disclosed by the invention is novel in structure, can simultaneously and effectively inhibit monoamine oxidase-B and acetylcholin esterase and inhibit A beta protein aggregation, has excellent oxidation resistance and metal ion chelation capability, and realizes a multi-target synergistic effect. In-vitro and in-vivo experiments show that the compound has a remarkable improvement effect on a plurality of pathological links such as Alzheimer's disease, and is low in neurotoxicity and high in safety. Meanwhile, the preparation method has the advantages of easily available raw materials and simple steps, is suitable for industrial production, and has a wide application prospect in the aspect of preparing the anti-neurodegenerative disease medicine.

Disclosed are a genetically engineered bacterium catalyzing the production of a quinoline compound, and a use thereof. The genetically engineered bacterium expresses monoamine oxidase and an enzyme capable of catalyzing alcohol oxidation, the enzyme capable of catalyzing alcohol oxidation being selected from alcohol oxidase or alcohol dehydrogenase. It has been unexpectedly discovered that monoamine oxidase coupled to alcohol dehydrogenase or alcohol oxidase can catalyze the preparation of quinoline from amino alcohol substrates, which fills the gap that current biocatalysis methods cannot synthesize amino alcohol substrates into quinoline compounds.

The invention relates to a preparation method and application of a monoamine oxidase treating fluid. The preparation method comprises the following steps: step 1, preparing a buffer solution; step 2, preparing an enzyme inclusion solution; and step 3, sequentially adding 0.25 g / L-0. 5 g / L of flavin adenine dinucleotide and 0.25 g / L-0. 5 g / L of a hydrophilic nonionic surfactant into the continuously stirred enzyme inclusion solution in an environment of 4 + / -1 DEG C, continuously stirring for 30 minutes, filtering, transferring into a dark brown glass bottle, and storing at 2-8 DEG C, thereby obtaining the product. The method disclosed by the invention has the beneficial effects that 1, the problem of too fast enzyme activity loss in the preparation process of the MAO quality control product is solved, and the enzyme activity loss is reduced from original 40% to below 10%; 2, the problem of short preservation period after the MAO quality control product is redissolved is solved, the preservation stability at 2-8 DEG C after the MAO quality control product is redissolved is improved to 7 days from the original 7 hours, and the frozen preservation at-20 DEG C is improved to 30 days from 10 days; and 3, the risk of too high production cost or patent infringement of reagent enterprises caused by MAO raw materials prepared by adopting patented technologies such as gene modification is avoided.

The invention relates to the technical field of molecular detection, in particular to a preparation method of a 5-hydroxytryptamine antibody reagent, and the 5-hydroxytryptamine antibody reagent comprises the following basic components: serum, a 5-hydroxytryptamine receptor diluent, concentrated sulfuric acid, concentrated nitric acid, monoamine oxidase, glyoxylic acid and a developing solution. The basic components for forming the color developing solution are sulfuric acid, nitric acid, glyoxylic acid and ultrapure water, and the mass ratio of the sulfuric acid to the nitric acid to the glyoxylic acid is 30%; 25% of nitric acid; 25% of glyoxylic acid; and 20% of ultrapure water. The reagent has agility, can complete detection in a short time, is suitable for large-scale screening and has convenience, the reagent can observe a result without complex operation of four steps: 1, sampling, 2, centrifuging, 3, mixing of the reagent and a specimen, and 4, standing for 1-15 minutes to obtain the result, the reagent is single, and the operation is simpler and more accurate due to the fact that only a single reagent is provided; and the accuracy of double combination of shaping and quantification is higher.

This application relates to a collagen hydrogel, its preparation method, and use. The preparation method includes the steps of (1) catalyzing the oxidative deamination of collagen using amine oxidase to generate unsaturated aldehyde functional groups, thereby generating intramolecular or intermolecular crosslinks and completing primary crosslinking, and (2) subjecting the primary crosslinked product to secondary crosslinking under the catalysis of a carboxyl activator to obtain the collagen hydrogel. The collagen hydrogel prepared by this method is a pure collagen hydrogel that exhibits a fast setting rate, good biocompatibility (excellent biomimetics), tunable mechanical strength, tunable structural size, good stability, and a wide range of applications.

The present invention provides a nanocomposite catalyst, and the preparation process of the nanocomposite catalyst is as follows: first, peroxidase nanomimetic enzyme is subjected to aldehyde modification to obtain CHO-nanozyme, and then the CHO-nanozyme is coupled with a protease and a ketoamine oxidase to obtain a nanocomposite catalyst. The present invention also provides a one-step method for determining glycated albumin, comprising the following steps: adding the aforementioned nanocomposite catalyst to a glycated albumin test solution, then adding a TMB solution to react for a period of time, observing the results, and the color of the solution after the reaction turns blue, indicating the presence of glycated albumin, and the blue color deepens as the concentration of glycated albumin in the glycated albumin test solution increases. The present invention uses a composite catalyst that integrates the triple functions of protease, ketoamine oxidase, and peroxidase, and detects glycated albumin in a one-step cascade reaction, which can simplify the operation and improve the detection efficiency and accuracy.

The invention discloses an amine oxidase mutant and application thereof in synthesis of chiral compounds, and relates to the field of biology. The amine oxidase mutant provided by the invention has mutation at any one or more sites of the 47 site, the 182 site, the 183 site, the 275 site, the 282 site and the 335 site of a wild type amino acid sequence, has relatively high catalytic activity on (S)-3-aminobutanol and relatively good stereoselectivity, can selectively oxidize (S)-3-aminobutanol under the condition that (R)-3-aminobutanol is not influenced, and has good application prospects. When the 4-hydroxy-2-butanone is applied to catalysis of (R)-3-aminobutanol feed liquid containing (S)-3-aminobutanol, the R-type ee value in the feed liquid can be effectively increased, additional refining and purifying steps are not needed, and the cost is remarkably reduced.

The present application relates to a collagen hydrogel, a preparation method therefor, and the use thereof. The preparation method comprises the following steps: (1) by using an amine oxidase, catalyzing collagen to undergo oxidative deamination to generate unsaturated aldehyde functional groups, and performing intramolecular or intermolecular crosslinking, so as to complete primary crosslinking; and (2) subjecting the primary cross-linked product to secondary crosslinking under the catalysis of a carboxyl activator so as to obtain the collagen hydrogel. In the present application, the collagen hydrogel prepared by the method is a pure collagen hydrogel, and has a high curing speed, good biocompatibility (excellent bionic properties), adjustable mechanical strength, adjustable structural size, good stability, and a wide range of application.

The present invention relates to functional foods and dietary supplements comprising a specific diamine oxidase (DAO) enzyme derived from the yeast Yarrowia lipolytica PO1f, uses of said enzyme and respective methods for the production of biogenic amine-depleted products, and said enzyme for use in medicine, in particular for use in the prevention or treatment of a condition or disease that is associated with increased levels of biogenic amines.

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