33 results about "Lipase b" patented technology

The invention discloses a method for splitting and preparing optically pure 1-(1-naphthyl)ethylamine by an immobilized enzyme method. Selective esterification of ‑1‑(1‑naphthyl)ethylamine followed by separation of (R)‑1‑(1‑naphthyl)ethylamine from (S)‑1‑(1‑naphthyl)ethylamine , to obtain (S)‑1‑(1‑naphthyl) ethylamine, and finally (R)‑1‑(1‑naphthyl) ethylamine ester hydrolysis to obtain (R)‑1‑(1‑naphthyl) Ethylamine. The catalyst used for selective esterification is the cross-linked Candida antarctica lipase B aggregate, which first dissolves Candida antarctica lipase B in water to obtain an enzyme solution, and then uses a precipitant to precipitate the enzyme protein from the enzyme solution Come out, then add a bifunctional cross-linking agent for cross-linking, and finally dry it. The cross-linked enzyme aggregate of the invention has high reutilization rate and strong operation stability in pure organic solvent.

The invention relates to candida Antarctica lipase B gene and applications thereof in yeast display. Coded protein of improved candida Antarctica B and wild type candida Antarctica lipase protein havethe same function on the amino acid level; the heat resistance capacity of the enzyme is 50-80 DEG C, and the half-lift is 3-24 hours; a nucleotide sequence is hybridized with SEQ.ID.NO2 from 1st to978th of nucleotide under the moderate precise condition; and a preservation number of colon bacillus DH5Alpha / Puc57-CALB (Escherichia coliDH5Alpha / pUC57-CALB) which carries the plasmids is CCTCC M 209081. The candida Antarctica lipase B gene is transferred into pichia pastoris host bacteria so as to realize the high-efficient display expression of the candida Antarctica lipase B in pichia pastoris; and the provided pichia pastoris bacteria can effectively display candida Antarctica lipase B, can be widely applied to the synthesis of ethyl caproate, has different melting points and does not contain triglyceride of various fatty acids, a plurality of structured lipids, and the like.

A method for preparing methyl-p-benzoquinone catalyzed by lipase is characterized in that butylamine is reacted with methyl-p-benzoquinone catalyzed by immobilized Candida antarctica lipase B to prepare 2-methyl-5-butane Amine p-benzoquinone. The enzyme-catalyzed method used in the present invention prepares 2-methyl-5-butylamino-p-benzoquinone. Due to the high degree of steric selectivity of the enzyme, it can avoid the poor selectivity of the chemical synthesis process and the difficulty of product separation, and is an environmentally friendly and efficient synthetic method. .

The invention discloses a 3, 4-dihydropyrimidine-2(1H)-ketone and derivatives thereof and synthesis method and application thereof. The method comprises the following steps: taking biocatalyst Candida antarctica lipase B as a catalyst and taking vinyl acetate and isopropanol as raw materials to generate acetaldehyde in situ, and adding beta-dicarbonyl compound, urea and water to react with the in-situ generated acetaldehyde to manufacture 3, 4-dihydropyrimidine-2(1H)-ketone and derivatives thereof. By use of the method disclosed by the invention, the biocatalyst Candida antarctica lipase B is used as the catalyst, the vinyl acetate and isopropanol are used as the raw material to generate the acetaldehyde in situ; the in-situ generated cetaldehyde is simultaneously reacted with the beta-dicarbonyl compound, urea and water; the reaction method is simple and environment-friendly; the reaction efficiency is high, and the byproduct is less; the method is an environment-friendly, sustainable, simple and effective method for synthesizing 3, 4-dihydropyrimidine-2(1H)-ketone and derivatives thereof.

The invention discloses a method for producing Candida antarctica lipase B and the specific DNA molecule used therefor. The nucleotide sequence of the specific DNA molecule is shown in SEQ ID NO:3. Experiments have shown that the recombinant plasmid pET30a‑CALB prokaryotically expresses CALB inclusion bodies, and then undergoes renaturation to obtain high-purity (over 95%) and high-activity CALB protein; the enzyme activity of CALB protein obtained from 1L of culture medium is about 21252U, and the specific activity About 253U / mg; much higher than the specific activity of the CALB protein prepared in the existing literature. It can be seen that the present invention significantly improves the output of CALB, and the production process is simple, and the completion can be applied to actual production. The invention has important application value.

The invention discloses a method for using Candida antarctica lipase B to produce a ticagrelor chiral medicine intermediate, and belongs to the technical filed of enzyme engineering. The Candida antarctica lipase B (called CALB for short) is used for converting racemic ticagrelor with the structural formula represented by formula (a) to a single configuration intermediate of a formula (b). In the formula (a) and (b), R is CnH2n+1CO or CnH2n-1CO (n is 2-6), and R' is Cbz or Boc. The configuration of the product (b) obtained through splitting the racemic medicine intermediate by the CALB is (1S,4R). The method using the CALB to split the above substrate has a high catalysis efficiency, and the purity of the product of the formula (b) obtained in the invention is high.

The invention discloses a process method for immobilizing lipase B from candida antarctica fermented supernatant fluid. According to the method, the immobilized candida antarctica lipase B is prepared by using a cheaper vector, adopting a water-phase immobilization mode and cooperating with a post-treatment process, therefore, the enzyme activity recovery rate under water-phase adsorption is increased, the cost and the using effect are balanced, and the important significance on industrial application of the CALB is achieved.