35 results about "Zeranol" patented technology

Zearalanol compounds are described and demonstrated or predicted to have utility as Heat Shock Protein 90 (HSP90) inhibiting agents in the treatment and prevention of various disorders. Methods of synthesis and use of such compounds are also described and claimed.

The invention provides a hybridoma cell strain 2D3, a monoclonal antibody to zearalenone secreted by the hybridoma cell strain 2D3 and application of the monoclonal antibody. The hybridoma cell strain 2D3 is preserved in China Center for Type Culture Collection with an accession number of CCTCC No. C201328 and can be used for preparation of a high-titer monoclonal antibody to zearalenone. According to detection results of enzyme linked immunosorbent assay (ELISA), the titer of the monoclonal antibody to zearalenone prepared through purification of mouse ascites can reach 1.5 * 10<5>. The monoclonal antibody to zearalenone has high sensitivity, half maximal inhibitory concentration IC50 of 20 pg/mL to zearalenone and cross reactivity of 4.9%, 3.3% and 3.2% with beta-zearalanel, alpha-zearalanel and beta-zeranol, respectively. The monoclonal antibody to zearalenone can be used for determination of the content of zearalenone.

The invention discloses an acinetobacter strain and application thereof to degradation of zearalenone. The acinetobacter strain disclosed by the invention is Acinetobacter sp. SM04, and is preserved in the China General Microbiological Culture Collection Center on December 5th, 2011, and the preservation number is CGMCC No. 5524. The Acinetobacter sp. SM04 disclosed by the invention has stronger degradation capability towards mycotoxins ZEN, can degrade more than 98% of zearalenone into low-estrogenic-activity product within 36 hours, cannot produce high-estrogenic-activity analogues such as zearalenone and zeranol, and has real detoxification capability. The acinetobacter strain can be applied to the treatment of corn grains, corn alcohol residues or other mycotoxin contaminated feed, so that safe food and animal feed are obtained, and further, a zearalenone degradation strain which has low cost and high efficiency and avoids secondary pollution is provided for the environment-friendly processing and treatment of the grains and feed.

The invention discloses a zearalenone (ZEN) toxin degrading enzyme for acinetobacter and a coding gene and applications of the ZEN toxin degrading enzyme. The amino acid sequence of the ZEN toxin degrading enzyme for the acinetobacter is shown by SEQ ID NO.6. The sequence of the coding gene of the ZEN toxin degrading enzyme for the acinetobacter is shown by SEQ ID NO.5. The ZEN toxin degrading enzyme for the acinetobacter performs stronger degrading capacity on mycotoxin ZEN, is capable of degrading at least 90 percent of ZEN into a low-estrogen active product in 12h without generating high-estrogen active analogues, such as ZEN, zeranol and the like, and has a real detoxification effect. According to the invention, the coding sequence of the ZEN toxin degrading enzyme for acinetobacter sp.SM04 is determined, i.e. a Prx gene, and thereby, a foundation is laid for researching the active site of the enzyme and changing the Prx enzyme activity through site-specific mutagenesis in the future.

The invention relates to a method for degradation of deoxynivalenol (DON), wherein bacterial powder of bacillus licheniformis is adopted to degrade the DON in mildewy grains. With the method of the present invention, the DON in the mildewy grains can be effectively degraded, and the application values of the mildewy grains are restored. According to the present invention, with detecting the effect of the DON degrading by the bacterial powder of the bacillus licheniformis under an in vitro simulation environment of the animal gastrointestinal tract, the optimal degradation conditions for the DON by the bacterial powder of the bacillus licheniformis are explored, and the method provides a solid foundation for further development of the bacterial powder of the bacillus licheniformis into thebiological antidote, wherein the biological antidote is provided for the degradation of zeranol in grains and corns.

A method for purifying alpha-zearalol and/or beta-zearalol and/or zearalone and/or alpha-zearalenol by the special immunoaffinity chromatographic column carrying immunoaffinity adsorbent is disclosed. Said adsorbent is composed of solid carrier and its coupled alpha-zearalol monoclonal antibody. It features that the chromatography is used to measure the contents of alpha-zearalol and its metabolites, having high correctness.

The invention discloses a method for detecting veterinary drug residues in fish meat, which comprises the following steps: (1) preparing a sample solution: taking and homogenizing fish meat, adding an acetonitrile aqueous solution containing formic acid, standing for 5-25 minutes, adding homogeneous protons, performing vortex oscillation for 20-40 minutes, centrifuging for 3-7 minutes, taking supernate, enabling the supernate to pass through a reversed-phase solid-phase extraction column, collecting effluent, blow-drying the effluent by N2 gas, adding an initial mobile phase, dissolving and filtering to obtain a test solution; and (2) detecting by adopting an ultra-high performance liquid chromatography-mass spectrometer. According to the method, through a specific sample pretreatment method and an instrument analysis method, veterinary drug residues cover mainstream veterinary drug types such as hormone and macrolide antibiotics and zeranol compounds, and the detection sample range is increased to bulk consumer fish species with complex matrixes such as turbots, mandarin fishes, snakeheaded fishes and grass carps; and the method is simple and rapid, low in cost, high in accuracy and good in stability.

The present invention relates to a method for hydrolyzing zearalenone and derivatives thereof. The zearalenone or derivatives thereof is used as a substrate, the substrate is hydrolyzed by using a zearalenone degrading enzyme and an amino acid sequence of the zearalenone degrading enzyme is shown in SEQ ID NO:1 or SEQ ID NO:2. The zearalenone degrading enzyme has high enzyme activity, good temperature and pH tolerance, etc., can be widely used in enzymatic hydrolysis of the zearalenone and several derivatives thereof, has a wide range of substrates, and has relatively high activity against zearalenone, alpha-zeranol and beta-zeranol, the amino acid sequence shown in the SEQ ID NO:2 is obtained by mutating the 158th T of the amino acid sequence shown in the SEQ ID NO:1 to H, and enzyme activity of the substrate alpha-zeranol is increased by 40% after the mutation.

A kit for detecting zeranol in foods is disclosed. The kit includes an enzyme-linked immuno sorbent assay plate, a zeranol standard substance, a zeranol antibody working fluid, a zeranol enzyme-labeled secondary antibody working fluid, a substrate A solution, a substrate B solution, a stopping solution, a concentrated diluent and a concentrated washing liquid. Specific antibody competition between the zeranol in a sample and an antigen immobilized on the enzyme-linked immuno sorbent assay plate is utilized, the enzyme-labeled secondary antibody is added and reacted with the antibody, color developing occurs through an enzymatic color developing agent, and the zeranol content of the sample is determined according to the color developing shade. If the zeranol content of the sample is low, color is dark, and otherwise, color is light. A detecting method utilizing the kit is simple and convenient to operate, detection is sensitive, accurate and rapid and the kit is suitable for rapid detection of a large-scale of samples.

The invention discloses an immunoaffinity stir bar for adsorbing raxofelast acid lactone compound, and a preparation method and an application thereof. The immunoaffinity stir bar for adsorbing raxofelast acid lactone compound is composed of solid phase carrier and zeranol murine monoclonal antibody coupled with the same, wherein the ratio of the coupling length of the solid phase carrier and coupled zeranol murine monoclonal antibody to the weight thereof is 1 cm: 2 mg. Through combining with a chromatography, an extracting method can effectively separate and condense the ingredients to be detected in a sample, the raxofelast acid lactone compound detection is facilitated, the disadvantages of less information amount, low quantification precision, low physico-chemical method selectivity and the like due to using the simplex immunoassay to directly detect the sample are overcome, and the analysis mechanism complementarity between the immunological technique and conventional physical and chemical technology is reflected.

The invention discloses a method for purifyingalpha-gibberella zeae alcohol and the private immunity affinity chromatography thereof. The filling material of the chromatography are alpha-gibberella zeae alcohol and immunity affinity adsorbent which comprises solid carrier and the coupled alpha-gibberella zeae alcohol monoclonal antibody; thealpha-gibberella zeae alcohol monoclonal antibody is made by the coupling object of the alpha-gibberella zeae alcohol and carrier protein as immunogen; The invention has the advantages of having more information and accurate definite quantity.

The invention discloses a composite immunization affinity column for purifying beta-zeranol and chloramphenicol, a preparation method and an application thereof. By employing 4% of cylindrical agarose gel as a solid phase carrier, the agarose gel and a prepared beta-zeranol antibody and a chloramphenicol antibody purchased on market are coupled to form an immunoadsorbent, and the immunoadsorbent is filled in the column to prepare the immunization affinity column. When a sample containing beta-zeranol and chloramphenicol passes through the immunization affinity column, beta-zeranol and chloramphenicol can be specifically adsorbed by the immunoadsorbent, other impurities flows out of the immunization affinity column, then methanol is used for eluting beta-zeranol and chloramphenicol from the column, so that the sample can be better purified. An immunoaffinity column purifying-liquid chromatography is established to detect beta-zeranol and chloramphenicol, so that detection is fast, accurate and safe.

The invention discloses a preparation method of zeranol monoclonal antibody and a monoclonal antibody prepared by using the same and application of the monoclonal antibody. The method comprises the following steps: preparation of antigen, determination of animal immunity and potency, preparation and fusion of splenocyte and myeloma cells of immune mice, screening of hybridoma cells, subcloning ofthe hybridoma cells, and preparation of a monoclonal antibody. The preparation method disclosed by the invention is simple and effective, overcomes the problems of high price of ZER standard products,less holoantigen synthesis methods, complicated steps or use of highly toxic chemical, tributylamine, and the like; by adopting ZEN standard products as raw material to prepare a ZER monoclonal antibody, the cost is low, the holoantigen synthesis method is simple, and the synthesis efficiency is high. According to the invention, the ZER monoclonal antibody is prepared, which is high in potency, has good combining capacity with ZER, has no cross reaction with other toxin such as aflatoxin, and can be used for establishing immunological detection methods such as ELISA.

The invention discloses application of silymarin in relieving of the reproductive toxicity of zeranol in animal corn. The silymarin is added into feed at the addition amount of 100 to 500mg/kg. By means of the silymarin, a reproductive toxicity effect caused by ZEN can be effectively relieved.

The invention relates to a preparation method of a zeranol complete antigen. The preparation method is characterized by comprising the following steps: weighing 2mg of ZER (zeranol), dissolving the ZER in 3mL of acetone, adding excessive K2CO3 (10mg) and 1[mu]L of ethyl 4-bromobutyrate, and performing refluxing for 24h at 60 DEG C; and carrying out a reaction by using a developing solvent namely 9.5mL of chloroform and 0.5mL of methanol, performing standing in the absence of light at a room temperature for 2 days after reaction, performing suction filtration to remove a deposit, and drying filtrate by rotary evaporation. The zeranol complete antigen prepared by the method provided by the invention is high in sensitivity, and a cross reaction between the zeranol complete antigen and other mycotoxins is less than 0.5%, which shows that the zeranol complete antigen is relatively strong in antiserum specificity; moreover, the preparation process is simple, industrial production can be achieved and the practicability is strong.