25 results about "Carboxylesterase" patented technology

The present invention relates to fusarium toxin cleavage polypeptide variants of a fusarium toxin carboxylesterase having SEQ ID No.1, 46 wherein said polypeptide variants each have an amino acid sequence shortened by 47 amino acids at the N-terminus and said amino acid sequence has a sequence identity of at least 70%, preferably 80%, particularly preferably 100%, to the amino acid sequence segments 48-540 of SEQ ID No.46, i.e. SEQ ID No.1; and isolated polynucleotides encoding the polypeptide variants; and an additive for cleaving fusarium toxins comprising at least one polypeptide variant and optionally at least one adjuvant; the invention also relates to the use of said polypeptide variants or additives for hydrolytically cleaving at least one fusarium toxin, and to a method for hydrolytically cleaving at least one fusarium toxin.

The invention belongs to the technical field of genetic engineering, and discloses application of an anchoring protein INP-N in a PET degrading enzyme system displayed on the surface. According to the invention, after efficient anchoring protein INP-N is screened, FAST-PETase is mediated by the efficient anchoring protein INP-N to construct recombinant escherichia coli of which the surface displays PET degrading enzyme. Furthermore, hydrophobin HFBII is introduced into the surface display system, so that the relative enzyme activity of the PET degrading enzyme is improved by 1.1 times or more. Meanwhile, FAST-PETase and carboxylesterase Est30KL are synchronously expressed, so that the proportion of TPA in a degradation product can reach 95% or above. In addition, the PET degrading enzyme surface display system provided by the invention is excellent in cycle performance, more than 65% of activity can still be retained when PET is cyclically degraded for the third time, and the application cost can be greatly reduced. The method can be applied to the fields of degradation of PET products, preparation of PET degradation agents or BHET degradation agents and the like.

The invention provides a method for improving the molecular weight of polyhydroxyalkanoates (polyhydroxyalkanoates, called PHA for short) synthesized by microorganisms, and relates to a method for improving the molecular weight of the polyhydroxyalkanoates (polyhydroxyalkanoates, called PHA for short). By knocking out or knocking down endogenous (intracellular) carboxylesterase, lipase, esterase, thioesterase and PHA degrading enzyme genes of bacteria for synthesizing PHA, the molecular weight of various synthesized PHA is obviously improved. The method has universality for improving the molecular weight of various PHAs synthesized by different species of bacteria, the mechanical property of the PHA can be improved by improving the molecular weight of the PHA, and new performance is provided for expanding the application of the PHA.

The invention relates to an application of carboxylesterase TfdI in degradation of phenoxy carboxylic acid herbicides. The invention provides application of rhodococcus pyridinivorans Y6 in degrading phenoxy carboxylic acid herbicides, a novel phenoxy carboxylic acid herbicide degrading enzyme TfdI is cloned from the rhodococcus pyridinivorans Y6, the rhodococcus pyridinivorans Y6 has excellent catalytic action on phenoxy carboxylic acid herbicides, the degradation rate on 2, 4-D isooctyl ester with the concentration of 100 mg / L within 1 h is 100%, and the degradation effect is stable. The excellent degrading enzyme provided by the invention has good application potential in bioremediation of the environment polluted by the phenoxy carboxylic acid herbicide, a new scheme is provided for solving the problem of residual pollution of the 2, 4-D isooctyl ester herbicide in agricultural production, and meanwhile, a herbicide degradation gene resource library is enriched.

Methods of treating a metabolic disorder in a subject are provided. Aspects of the method include enhancing extracellular Carboxylesterase 2 (CES2) activity in the subject in order to treat the subject for the metabolic disorder. Also provided are compositions for use in practicing the methods.

The application discloses an esterase whole cell catalyst and preparation and application thereof, the esterase whole cell catalyst can express a carboxylic acid esterase mutant disclosed in the application, the carboxylic acid esterase mutant is subjected to the following mutations on the amino acid sequence shown in SEQ ID NO. 1: the glycine at the 236th position is replaced by valine, the arginine at the 417th position is replaced by phenylalanine, and the threonine at the 545th position is replaced by alanine. The application effectively solves the problems of low catalytic activity of a warming catalyst for resolving methyl chrysanthemate and poor product tolerance in the prior art. The esterase whole cell catalyst of the application significantly improves the activity of selectively resolving methyl chrysanthemate to prepare dextro-trans chrysanthemic acid, and the optical purity can reach more than 99%. Moreover, the carboxylic acid esterase mutant disclosed in the application can be expressed in a soluble form in cell supernatant, can be produced in a large scale through microbial fermentation, has mild reaction conditions, and is simple to operate, and is more suitable for industrial production.

The application discloses a carboxylic esterase lyophilization protective agent, a preparation method and application thereof, and belongs to the technical field of bioengineering. The carboxylic esterase lyophilization protective agent is a single-component polyvinylpyrrolidone; wherein, the polyvinylpyrrolidone has a viscosity-average molecular weight Mv of 10000-15000000; a K value of 17-90; when used for lyophilization protection of carboxylic esterase, the carboxylic esterase lyophilized powder can effectively improve the stability of the carboxylic esterase lyophilized powder at normal temperature, prevent the purity and activity of the carboxylic esterase lyophilized powder from decreasing, and the lyophilized powder cake is complete, easy to be powdered, the enzyme powder resuspension is clear and transparent, the enzyme activity recovery rate is high, and the carboxylic esterase is convenient for being applied to different application scenarios.

This invention discloses a carboxylesterase-activated mitochondrial-targeting fluorescent probe with photodynamic therapy properties, its preparation method, and its uses. The structure of the mitochondrial-targeting fluorescent probe is shown below. The mitochondrial-targeting fluorescent probe CML of this invention can specifically respond to different concentrations of carboxylesterases (CEs), with a detection limit as low as 0.30 U / L. Simultaneously, this probe can specifically target mitochondria, and through structural optimization (replacing the methyl group on the indole salt with a butyl group), its mitochondrial anchoring ability is significantly superior to that of methyl-substituted derivatives. Cytotoxicity experiments confirmed that the probe has good biocompatibility; confocal fluorescence imaging experiments showed that this probe can effectively monitor the fluorescence changes of endogenous and exogenous CEs in HepG2 cells. Most importantly, after being specifically activated by carboxylesterases, the probe can efficiently generate reactive oxygen species under light conditions, thereby exerting a photodynamic therapeutic effect on cancer cells.

The application relates to a synthesis method of a compound of formula I, a genetically engineered bacterium for synthesizing terpenes and application of the genetically engineered bacterium, relates to the field of biosynthesis, and a synthesis method of terpenes, and comprises the following method: a compound of formula II is sequentially subjected to the action of cytochrome oxidase, carboxylic acid esterase and cyclase to generate the terpene compound shown in formula I. The application solves the problem of multiple synthesis steps of the compound shown in formula I. The application solves the problem of low enzyme rate of each step through gene optimization.

The invention provides a biosynthesis method of an esdoxaban tosylate chiral intermediate. According to the preparation method, 3-cyclohexene-1-carboxylic acid methyl ester is taken as a starting raw material, and a target intermediate is finally obtained through carboxylesterase resolution, hydrolysis, hydroxylation, dehydrogenation oxidation, transamination reaction, amidation and Boc2O reaction in sequence. According to the method, high-selectivity carboxylesterase is used for realizing chiral resolution; p450 oxidase with excellent regioselectivity and stereoselectivity is utilized to realize specific hydroxylation of a C-H bond under a mild condition, and a traditional process depending on a highly toxic chemical oxidant is overturned; then, clean oxidation is realized through alcohol dehydrogenase, and a way is laid for subsequent reaction; most importantly, the transaminase is adopted to directly construct the chiral amine, so that the use of a high-risk reagent sodium azide is thoroughly avoided, and major potential safety hazards are eliminated from the source; and finally, green amidation is realized by virtue of lipase, and an acyl chloride method for generating corrosive wastewater is replaced.

This invention discloses an alkaloid, its preparation method, and its application in the preparation of human carboxylesterase 2 inhibitors. The residue of Paeonia lactiflora after ultrasonic extraction was extracted with 95% ethanol and then with ethyl acetate to obtain ethyl acetate extract CS-5. Separation was performed by silica gel column chromatography, using a gradient elution with petroleum ether-acetone mixed solvent and dichloromethane-methanol mixed solvent to obtain six eluent fractions, named A-F. Compound D was separated by silica gel column chromatography, Sephadex LH-20 column chromatography, and semi-preparative HPLC to obtain compound I-2. Compound F was separated by Sephadex LH-20 column chromatography and semi-preparative HPLC to obtain compounds I-1 and I-3. Compound I-1 was separated by a chiral HPLC column to obtain enantiomers I-(+)-1 and I-(–)-1. The four alkaloids of this invention have a pH range of 13.65–14.16. m At concentrations of M, it can significantly inhibit the activity of human carboxylesterase 2. Therefore, it can be applied to the preparation of attenuated and protective agents for anticancer drugs such as irinotecan.

The invention belongs to the technical field of medicinal chemistry, and discloses a human carboxylesterase 2A (hCES2A) self-activated covalent inhibitor as well as a preparation method and application thereof. The inhibitor is a novel benzamide-O-carbamate derivative (I) with a structure as shown in a formula (I) and pharmaceutically acceptable salts thereof, and the compound can powerfully and highly selectively inactivate the activity of human intestinal tract hCES2A. Further, the oral bioavailability of the oral prodrug is improved or the intestinal toxicity caused by the carboxylesterase 2A activated prodrug (such as irinotecan) is relieved. The IC50 value of the compound for inhibiting human carboxylesterase 2A can reach a nanomole level and is dose-dependent and time-dependent. The compound provided by the invention also has good safety, and has the advantages of simple preparation process, high yield and the like, which indicates that the compound has good application prospects.

The present disclosure provides engineered carboxylesterase enzymes having improved activity in catalyzing cyclization of short polypeptides, as compared to a naturally occurring wild-type carboxylesterase enzyme. These variants catalyze the cyclization of linear tetrapeptides with high regioselectivity. Also provided are polynucleotides and expression vectors encoding the carboxylesterase enzymes and methods of using the carboxylesterase enzymes to generate cyclic tetrapeptides containing non-canonical amino acids.

The invention belongs to the technical field of artificial mimic enzymes, and discloses a carboxylesterase simulant with phthalate degradation activity as well as a preparation method and application of the carboxylesterase simulant. The stimulant is Zn (II) (at) IMD PDA: beta-CD, and the structure of the stimulant takes beta-cyclodextrin as a skeleton, is bridged with an imidazole group through 1, 3-propane diamine, and is coordinated with Zn (II) ions to form a catalytic center. According to the design, a hydrophobic cavity of beta-cyclodextrin and a Zn (II)-imidazole active center are integrated into a whole, so that efficient recognition and catalytic hydrolysis of phthalate pollutants are realized. According to the preparation method, beta-cyclodextrin is taken as an initial raw material, one-pot three-step continuous reaction synthesis is carried out, the process is simple and convenient, the condition is mild, the cost is low, and the use of precious metals and tedious separation and purification steps are avoided. The simulant shows high-efficiency degradation capacity to various phthalic acid esters (such as DEHP, DBP and the like) under mild conditions, the degradation rate to the DEHP within 72 hours can reach 81.4%, and the activity of the simulant is still kept to be 98% or above after the simulant is recycled for 5 times.

The application discloses a lysosome-targeting near-infrared fluorescent probe and a preparation method and application thereof in carboxylesterase detection, wherein the structure of the lysosome-targeting near-infrared fluorescent probe is shown in the following formula: The lysosome-targeting near-infrared fluorescent probe of the application shows a rapid response (response time is 40 seconds) to carboxylesterase (CE) in an in-vitro experiment. Cell toxicity test shows that the probe has low biological toxicity, and confocal fluorescence microscopic imaging experiment shows that the fluorescent probe has good light stability in HeLa cells and can effectively target lysosomes (localization coefficient is 0.86), and is suitable for CE near-infrared region fluorescence imaging and detection in lysosomes of living cells.

The application discloses a stable whitening oral composition based on bio-enzyme catalysis, and belongs to the technical field of oral care products. The stable whitening oral composition based on bio-enzyme catalysis is characterized in that the components in the formula mainly include a humectant, a polyethylene glycol, a peroxide, an abrasive, an acyl donor, a carboxyl esterase, a sweetener, a fragrance, an anionic surfactant, a fluoride, a compound emulsifier, a thickening agent, a phosphate and an amphoteric surfactant. The compound emulsifier is composed of sucrose palmitate and sucrose stearate. The paste of the composition has high centrifugal stability, high and low temperature storage stability and excellent extrusion performance. The carboxyl esterase has high catalytic activity, and can realize high-efficiency whitening effect under the condition of low-concentration hydrogen peroxide.

The present application relates to a nucleic acid molecule comprising a first nucleic acid sequence comprising at least a portion of a 5′ untranslated region (5′ UTR) of a carboxylesterase gene and a second nucleic acid sequence encoding a protein of interest, where the second nucleic acid sequence is heterologous to and operatively coupled to the first nucleic acid sequence. Also disclosed are methods of expressing a protein of interest in a target cell, methods of treating subject for cardiac ischemia or hepatic ischemia, and methods of identifying a nucleic acid sequence capable of selectively enhancing translation of a heterologous protein of interest in a target cell.

The invention discloses a liver / mitochondria dual-targeting carboxylesterase fluorescent probe as well as a preparation method and application thereof, and belongs to the technical field of medicines. The probe is a compound LDM-CA, has the liver and mitochondria dual-targeting characteristic, and shows high selectivity, sensitivity and strong binding affinity to CEs. In-vitro cell experiments show that the LDM-CA has excellent mitochondrial targeting ability in the HCC cells and specific fluorescence opening response to CEs in the cells, and can clearly distinguish the HCC cells from normal liver cells or non-liver cancer cells. In-vivo imaging of a mouse model shows that no matter in-tumor injection or intravenous injection, the LDM-CA can effectively visualize the HCC tumor and draw the edge of the tumor, has the prospect of serving as a powerful molecular tool for early HCC diagnosis and image-guided surgery, and also provides a valuable means for studying the action of mitochondrial CEs activity in HCC pathogenesis at the subcellular level.

The application discloses a stable whitening oral composition based on bio-enzyme catalysis, and belongs to the technical field of oral care products. The stable whitening oral composition based on bio-enzyme catalysis is characterized in that the components in the formula mainly include a humectant, a polyethylene glycol, a peroxide, an abrasive, an acyl donor, a carboxyl esterase, a sweetener, a fragrance, an anionic surfactant, a fluoride, a compound emulsifier, a thickening agent, a phosphate and an amphoteric surfactant. The compound emulsifier is composed of sucrose palmitate and sucrose stearate. The paste of the composition has high centrifugal stability, high and low temperature storage stability and excellent extrusion performance. The carboxyl esterase has high catalytic activity, and can realize high-efficiency whitening effect under the condition of low-concentration hydrogen peroxide.

The present disclosure relates to an efficient and scalable enzymatic process for synthesizing macrocyclic peptides of Formula 1': or salt, hydrate, and / or solvate thereof. The process utilizes engineered ATP-dependent ligase and carboxylesterase enzymes to provide a compound of Formula 1' in large scale while maintaining desired regiochemistry, reduced by-product formation and high yields.

The invention discloses serratia marcescens and application of the serratia marcescens in improvement of host pesticide tolerance. The serratia marcescens is a serratia marcescens LB3 strain, the strain is preserved in the Guangdong Microbial Culture Collection Center on June 19, 2025, and the preservation number is GDMCC No: 66557. The serratia marcescens LB3 strain disclosed by the invention has the advantages that the preservation number is CGMCC No: 66557; the LB3 strain can effectively degrade the lambda-cyhalothrin, the activity of glutathione S-transferase, carboxylesterase and cytochrome P450 in a host can be improved by ingestion of the strain, the tolerance of the host to the lambda-cyhalothrin is improved, and the survival rate of the host under the stress of the lambda-cyhalothrin is improved. Based on the strain, the tolerance of natural enemy insects to the lambda-cyhalothrin can be improved, the influence of the lambda-cyhalothrin on the natural enemy insects is reduced, and effective prevention and control of pests are promoted.

The application discloses a kind of mitochondria-targeted near-infrared fluorescent probe and its preparation method and application in carboxylesterase detection, wherein the structure of the mitochondria-targeted near-infrared fluorescent probe is as follows: The near-infrared fluorescent probe SYH-SF of the application shows good selectivity and high sensitivity (detection limit is as low as 0.027 U / L) to carboxylesterase, and has good mitochondria-targeting ability (positioning coefficient Pr=0.92). Cell toxicity test shows that the probe has good biocompatibility, and confocal fluorescence microscopic imaging experiment shows that the probe has good light stability for HepG2 cells, can effectively detect carboxylesterase in mitochondria of living cells, and is suitable for confocal fluorescence imaging of intracellular endogenous carboxylesterase, evaluation of anticancer drug efficacy and differentiation between normal cells and cancer cells.

The present invention provides engineered carboxyesterase enzymes having improved properties as compared to a naturally occurring wild-type carboxyesterase enzymes, as well as polynucleotides encoding the engineered carboxyesterase enzymes, host cells capable of expressing the engineered carboxyesterase enzymes, and methods of using the engineered carboxyesterase enzymes in hydrolysis reactions.

The application discloses a fluorescent dye responding to carboxylic esterase, and a preparation method and application thereof, relates to the technical field of fluorescent dyes, and the preparation method comprises the following steps: mixing 2, 3, 3-trimethyl-3H-indole and 3-iodine propionic acid and dissolving them in toluene, then performing a reaction under a protective atmosphere at 110-130 DEG C to prepare compound 1; mixing compound 1 and 3, 4-dihydroxy-3-cyclobutene-1, 2-diketone, dissolving them in a mixed solution of n-butanol, toluene and pyridine, then performing a reaction under a protective atmosphere at 110-130 DEG C to prepare compound 2; mixing compound 2 and m-benzene dimethanol, then performing a cross-linking reaction after adding a cross-linking agent to prepare the fluorescent dye. The fluorescent dye disclosed by the application can be not influenced by external temperature and pH, can be combined with carboxylic esterase more highly, realizes high specificity and high sensitivity response to carboxylic esterase, and has potential application prospects in biological imaging.

The application provides a bioluminescent probe for detecting carboxylesterase 2 in vivo, and a preparation method and application thereof, and belongs to the technical field of biological detection.The bioluminescent probe is a compound shown in formula CBP, or a salt thereof, or a stereoisomer thereof.The bioluminescent probe for detecting carboxylesterase 2 in vivo provided by the application has good biocompatibility, a fast reaction speed with carboxylesterase 2, strong selectivity, almost no response to other interfering ions, high detection sensitivity, good responsiveness, low detection limit, a linear relationship between the bioluminescent intensity and carboxylesterase 2 in a certain concentration range, and stable bioluminescent signals, and can be used for qualitative and quantitative detection of carboxylesterase 2, and has a wide application prospect.