903 results about "Biocatalysis" patented technology

The invention discloses a glycosyl transferase UGT76G1 mutant and a method for catalytically synthesizing rebaudioside M by using the glycosyl transferase UGT76G1 mutant, and relates to the technical field of biological catalytic synthesis. The glycosyl transferase UGT76G1 mutant is any one of the following components (A)-(C): (A) a protein obtained by performing any one or more of the following mutations on the basis of an amino acid sequence as shown in SEQ ID NO.1: the 89th amino acid is mutated into H from M; the 380th amino acid is mutated from L to M; the 411th amino acid is mutated from A to Y; (B) a protein which has 95% or 98% or more of identity with the amino acid sequence defined by (A) and has the same function as the amino acid sequence defined by (A); and (C) a fusion protein obtained by connecting a tag to the terminal of the protein defined in (A) or (B). The glycosyl transferase UGT76G1 mutant disclosed by the invention is obtained by mutating and screening glycosyl transferase UGT76G1, has higher catalytic activity, and can be used for efficiently synthesizing rebaudioside M by taking rebaudioside D and UDPG as substrates.

The invention discloses a method for efficiently synthesizing epiinositol by using a heat-resistant myo-inositol dehydrogenase mutant cascade system, and belongs to the field of biocatalysis engineering. Whole cells for expressing a scyllo-inositol dehydrogenase mutant and a heat-resistant scyllo-inositol dehydrogenase mutant are utilized to catalyze the scyllo-inositol to synthesize the epiinositol in a two-step cascade manner, and different from reported scyllo-inositol and D-chiral inositol synthesis methods, in the process of synthesizing the epiinositol by taking the scyllo-inositol as a substrate, the C4 position of the scyllo-inositol is dehydrogenated firstly, then the C4 position of the scyllo-inositol is dehydrogenated, and the C4 position of the D-chiral inositol According to the present invention, the structure of the substrate and the structure of the product are symmetric, and the enzyme is difficult to specifically recognize during the catalysis process, such that the synthesis of the different chiral compounds of the inositol is the important problem in the biological catalysis field. The invention provides a brand-new way for biocatalytically synthesizing the epiinositol, the yield of the epiinositol is increased to 1.89 g / L through enzyme modification, the conversion rate is 52.6%, and the yield and the conversion rate are the highest level reported publicly at present.

The invention belongs to the field of bioengineering, and particularly discloses a tryptophan synthetase mutant with improved enzymatic activity and application of the tryptophan synthetase mutant in production of L-cysteine. Compared with wild tryptophan synthetase from escherichia coli, the amino acid sequence of the tryptophan synthetase mutant has the advantages that a beta catalytic subunit has T69A, S143A, R219E and F280H site combined mutation. Researches show that the enzyme activity of the mutant is increased by 2.4 times compared with that of a wild type through enzyme activity determination and analysis of inducible expression and purification. The beneficial tryptophan synthetase mutant provided by the invention can efficiently biocatalyze L-serine and sodium hydrosulfide to synthesize L-cysteine, and has a better industrial application prospect.

The invention discloses a thermostable conjugated polyketoreductase mutant, which is obtained by performing single-point mutation or multi-point combined mutation on the 25th site, the 92th site, the 214th site or the 256th site of an amino acid sequence as shown in SEQ ID NO.1. The invention further discloses a preparation method of the thermostable conjugated polyketoreductase mutant. The initial enzyme activity of the mutant is high, and the residual enzyme activity is gt after incubation at 50 DEG C; the Tm value can be increased by more than 9 DEG C compared with that of an original strain, the 50 DEG C half-life period t1 / 2 is increased by more than 377.8 times, and the thermal stability is obviously improved. The invention also provides a coding gene, a recombinant vector containing the coding gene and a co-expression engineering bacterium. The thermostable conjugated polyketoreductase mutant, glucose dehydrogenase and L-pantolactone dehydrogenase are used for constructing a three-enzyme co-expression engineering bacterium as a biocatalyst, racemization pantolactone is catalyzed to synthesize DPL, for a 1M substrate, the yield of the DPL reaches 97.5% within 36 hours, KPL hydrolysis is avoided, the reaction time is shorter, the product concentration is higher, and the thermostable conjugated polyketoreductase mutant has great market application value.

The invention relates to the technical field of biological catalysis, and discloses an L379A mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: leucine of the 379th amino acid sequence is mutated into alanine; the enzyme can be applied to RA in-vitro conversion preparation of RI with higher utilization value, the conversion rate is higher than 50%, and the enzyme activity is remarkably improved by 7 times compared with the original enzyme catalytic conversion enzyme activity. The UGT76G1 mutant disclosed by the invention has the advantages that (1) the blank is filled, and a special enzyme catalyst capable of realizing efficient in-vitro synthesis of rebaudioside I (RI) is provided for the first time; 2) efficiency jump: the catalytic conversion rate is greatly increased from original about 7% to more than 50% (increase gt; and 3) stability and reliability: in the cross-scale reaction of 10mL to 5L, the catalyst has stable catalytic performance, shows excellent industrial application potential, and is suitable for popularization and application.

The invention discloses a carbonyl reductase mutant as well as a preparation method and application thereof, and belongs to the technical field of enzyme engineering. According to the invention, on the basis of carbonyl reductase BcKRED from Bacillus cereus, a series of dominant mutants are obtained through a method of directed evolution in the field of enzyme engineering. The carbonyl reductase dominant mutant obtained by the invention has high catalytic activity, thermal stability and chiral selectivity reversed with wild-type carbonyl reductase. A green and efficient way is provided for industrial production of chiral alcohol by taking carbonyl reductase as a biocatalyst, and the method has a wide application prospect.

The invention belongs to the field of biological catalysis, and discloses a high-activity PET hydrolase mutant and application thereof. The mutant of the thermophilic PET hydrolase provided by the invention is as shown in 1), 2) or 3): 1) a protein corresponding to an amino acid sequence SEQ ID NO.4; 2) a protein corresponding to the amino acid sequence of SEQ ID NO.6; and 3) a protein corresponding to the amino acid sequence of SEQ ID NO.8. Experiments prove that the modified mutant shows higher catalytic efficiency on PET hydrolysis and can keep activity for a long time at the optimal temperature for PET depolymerization. The activity of the mutant protein BhrM3 for catalyzing PET hydrolysis is improved by 1.82 times compared with that of a wild type and is 1.22 times that of efficient PET hydrolase LCC-ICCG, and the protein melting temperature reaches 92.9 DEG C.

Glycosyltransferase UGT76G1 and UGT91C1 mutants and a method for catalytic synthesis of rebaudioside A, D, and M by using same, pertaining to the technical field of biocatalytic synthesis. The glycosyltransferase UGT76G1 mutant can effectively synthesize rebaudioside A using stevioside STV as a substrate. The glycosyltransferase UGT91C1 mutant is obtained by mutation screening of wild-type glycosyltransferase UGT91C1, has higher enzyme activity and catalytic rate, and can effectively synthesize rebaudioside D using rebaudioside A as a substrate. The glycosyltransferase UGT76G1 mutant can also be obtained by mutation and subsequent screening of glycosyltransferase UGT76G1, has higher catalytic activity, and can effectively synthesize rebaudioside M using rebaudioside D and UDPG as substrates.

The invention discloses a biological catalytic synthesis method of norambrox ether, which comprises the following steps: step 1, starting from trans-nerolidol, carrying out carroll rearrangement reaction to synthesize farnesyl acetone; 2, in the presence of a cofactor, converting farnesyl acetone into high farnesol acetate under catalysis of Bayer-Villiger monooxygenase; step 3, catalyzing the deacetylation of the high-farnesol acetate by using esterase to obtain EE-high-farnesol; and step 4, carrying out enzymatic conversion on farnesol by using the squalene hopaene cyclase mutant to obtain norambrox ether. The transformation process is safe and non-toxic, Bayer-Villiger monooxygenase which is new with a key enzyme, natural co-expressed esterase, alcohol dehydrogenase and squalene and hopaene cyclase mutants matched with the system are used for synergistic transformation, so that not only is the coenzyme for oxidation reaction promoted to be recycled, but also the conversion efficiency is improved; conversion from farnesyl acetone to norambrox ether can be efficiently and specifically catalyzed, and a final product can be directly obtained from a reaction system without separation and purification of an intermediate.

The invention relates to the technical field of biological catalysis, and discloses an M88V mutant enzyme for preparing rebaudioside I. The M88V mutant enzyme is obtained by the following mutations generated by UGT76G1: M88V: methionine of the 88th amino acid sequence of UGT76G1 is mutated into valine. Aiming at the technical bottlenecks of low RI yield and poor selectivity in the existing RA biotransformation process, an efficient solution is provided for the UGT76G1 mutant developed by the invention. The mutant can specifically catalyze conversion from RA to RI, and the conversion rate of a target product is remarkably increased to 65% or above from general less than 7%. The excellent catalytic performance of the catalyst is verified in milliliter-level to upgraded reaction systems, the key problems of conversion efficiency and process amplification are solved, and a foundation is laid for large-scale green manufacturing of a high-added-value product RI.

The invention discloses a p-nitrophenyl ethyl esterase mutant with high enantioselectivity as well as a construction method and application of the p-nitrophenyl ethyl esterase mutant. The p-nitrophenyl ethyl esterase mutant is obtained by mutating an amino acid sequence of wild p-nitrophenyl ethyl esterase pnbA as shown in SEQ ID NO.1 according to one or a combination of more of the following modes: leucine at the 273rd site is mutated into aspartic acid, phenylalanine at the 314th site is mutated into histidine, and leucine at the 362nd site is mutated into arginine. The mutant pnbA-L273D / F314H / L362R provided by the invention shows optimal catalytic performance (E = 47.16) for racemization-acetic acid pinyl hydrate, the enantiomeric excess value of the mutant is 95.13%, the conversion rate of 1S, 5R-acetic acid pinyl hydrate is 90.42%, the enantioselectivity of the mutant is obviously higher than that of a wild type, and the mutant has great application potential in biological catalytic synthesis of monocyclic monoterpenoid chiral alcohols.

The invention discloses a 3-ketosteroid-delta1-dehydrogenase mutant and application thereof in synthesis of prednisone acetate, the mutant with high catalytic activity on cortisone acetate is obtained through screening, and a methanol-water phase (Tris-HCl buffer solution) system is adopted to increase the solubility of a substrate so as to improve the biological catalytic efficiency. In a single water phase system (Tris-HCl buffer solution) without methanol, the conversion efficiency is only 64.8% for 60g / L of cortisone acetate, and under the condition that other conditions are the same, the conversion rate in the Tris-HCl buffer solution system with methanol is increased to 92.1%, and the conversion rate is increased by 1.42 times.

The invention discloses a preparation method for synthesizing coal-based carbon quantum dots through microbial catalysis, which comprises the following specific preparation steps: (1) pretreating coal, specifically comprising crushing and sterilizing treatment; (2) combining the pretreated coal sample with selected microorganisms or biological factors, and carrying out fermentation treatment on the coal; (3) after fermentation is completed, dialyzing the coal fermentation liquid to prepare a carbon quantum dot solution; (4) separating and purifying the dialyzed carbon quantum dot solution to remove impurities; and (5) carrying out quick freeze-drying on the separated and purified carbon quantum dot solution to obtain the carbon quantum dots with fluorescent properties. According to the method, microorganisms serve as a core, an aerobic or anaerobic fermentation process is combined, coal resources are fully utilized, and efficient preparation of the coal-based carbon quantum dots is achieved. The method not only has good environmental protection property, but also can provide a new technology for industrial production of the carbon quantum dots, and has important significance for efficient conversion and green chemical synthesis of coal.

The invention discloses a metal supported activated carbon catalyst for efficiently preparing aquacide dichloride and application of the metal supported activated carbon catalyst. The catalyst is prepared by taking activated carbon as a carrier, loading Lewis acid active components such as aluminum ions, zinc ions, iron ions, copper ions and the like through an impregnation method, and carrying out vacuum pyrolysis activation treatment at 300-600 DEG C. The catalyst synergistically catalyzes a nucleophilic substitution reaction of a pyridine derivative and alkyl halide in an aprotic polar solvent such as acetonitrile or nitrobenzene, and synthesis of diquat dichloride can be realized under the conditions that the temperature is 100-180 DEG C and the pressure is 1-3 MPa. In a reaction system, the mass ratio of the pyridine derivative to the catalyst to the solvent is 1: (0.01-0.05): (5-8), and real-time monitoring and regulation are performed through an online infrared spectrum, a liquid chromatograph and a gas chromatograph-mass spectrometer. The purity of the product is more than 99% after the product is subjected to filtration, recrystallization with an ethanol-water mixed solvent and vacuum drying. The catalyst provided by the invention has the characteristics of high activity, strong stability and recoverability, obviously improves the atom economy of the reaction, simplifies the production process, reduces the energy consumption and pollution, and is suitable for large-scale industrial production.

The present application relates to the technical field of biocatalysis and biosynthesis, and specifically discloses a natural blue pigment and a biosynthesis method therefor. The present application uses metabolically engineered bacteria to express indigoidine synthetase and phosphopantetheinyl transferase, to catalyze glutamine and N-acetylglutamine to biosynthesize a natural blue pigment N-acetylindigoidine, and deduces its molecular structure by means of mass spectrometry, nuclear magnetic resonance and other methods. The present application achieves catalytic synthesis of N-acetylindigoidine from glutamine and N-acetylglutamine in Escherichia coli, Corynebacterium glutamicum, Saccharomyces cerevisiae and Streptomyces. Compared with indigoidine, N-acetylindigoidine has a maximum absorption wavelength of 584 nm, possesses better color brightness, and has more stable coloration that is not easily faded, with a very broad application range and industrial production application prospects.

The invention relates to the technical field of biological catalysis, and discloses an M88A mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: M88A: methionine of the 88th amino acid sequence of UGT76G1 is mutated into alanine; the key conversion rate of RI is greatly increased from 7% to 85% (increased by more than 12 times), and the utilization rate and economical efficiency of raw materials are remarkably improved; the method can be perfectly reproduced under any test scale (10mL, 100mL and 5L), the conversion rate is always anchored to be more than 85%, and incomparable stability and amplification potential are shown.

The present application relates to the technical field of biocatalysis and biosynthesis, and specifically discloses a blue pigment and a biosynthesis method thereof. In the present application, an indigoidine synthetase and a 4′-phosphopantetheinyl transferase are expressed by a metabolically engineered strain to catalyze the biosynthesis of the blue pigment N-acetyl-indigoidine from glutamine and N-acetylglutamine, and a molecular structure of the blue pigment is inferred by mass spectrometry, nuclear magnetic resonance spectroscopy, etc. The present application achieves the catalytic synthesis of N-acetyl-indigoidine from glutamine and N-acetylglutamine in Escherichia coli (E. coli), Corynebacterium glutamicum (C. glutamicum), Saccharomyces cerevisiae (S. cerevisiae), and Streptomyces. Compared with indigoidine, N-acetyl-indigoidine has a maximum absorption wavelength of 584 nm, and a stable color having high brightness that is not easy to fade. Thus, the blue pigment shows an extensive application range and a promising industrial production prospect.

The invention discloses a method for preparing immobilized lipase Janus particles by an emulsion template one-step method based on a zymoprotein directional adsorption strategy and application of the immobilized lipase Janus particles in a Pickering emulsion catalytic system. The natural hydrophilicity of lipase protein is utilized to drive the lipase protein to form directional adsorption on the surfaces of hydrophobic particles, and the Janus particles with hydrophilic and hydrophobic characteristics are constructed. Firstly, an organic phase containing hydrophobic particles and a water phase containing lipase are oscillated to form an emulsion, so that the lipase in the water phase is accurately adsorbed on the single side of the surface of the particles, and directional connection of zymoprotein and a hydrophobic matrix is realized. Afterwards, the Janus particles are used for constructing a Pickering emulsion system, and a microreactor is built, so that the catalytic efficiency of lipase in hydrolysis, ester synthesis and transesterification reaction is improved. The method is easy to operate, efficient and stable enzyme immobilization can be achieved, the obtained immobilized lipase Janus particles are remarkably superior to free enzyme in biological catalytic activity and cyclic utilization performance, and the application value of lipase in industrial large-scale production is remarkably improved.

The invention belongs to the technical field of catalytic materials, and particularly relates to high-entropy alloy nanoparticles used as a biocatalyst and application of the high-entropy alloy nanoparticles. The PtFeCuCoNi high-entropy alloy nano-particles with pH adaptability are developed through a one-step solvothermal synthesis method, it is found that the PtFeCuCoNi high-entropy alloy nano-particles can serve as potent oxidase, can generate reactive oxygen species (ROS) and effectively kill bacteria such as MRSA under the acidic condition, and can play the functions of superoxide dismutase and catalase under the neutral condition, so that the PtFeCuCoNi high-entropy alloy nano-particles with the pH adaptability can be used for effectively killing bacteria such as MRSA. Active oxygen in cells is efficiently removed, oxidative stress is relieved, and the cell protection effect is achieved.

The invention discloses a recombinant plasmid, a recombinant strain and a method for synthesizing rebaudioside M by a one-step method, and belongs to the technical field of biological catalytic synthesis. The recombinant plasmid contains a coding gene of a glycosyl transferase UGT91C1 mutant, a coding gene of a glycosyl transferase UGT76G1 mutant and a coding gene of sucrose synthase. The mutant of the glycosyl transferase UGT91C1 is 2-12E, and the coding gene sequence of the glycosyl transferase UGT91C1 is as shown in SEQ ID NO. 1; the glycosyl transferase UGT76G1 mutant is 101H10, and the coding gene sequence of the glycosyl transferase UGT76G1 mutant is as shown in SEQ ID NO. 2; the sequence of the coding gene of the sucrose synthase is as shown in SEQ ID NO. 3. The rebaudioside M is synthesized by using a three-enzyme co-expression recombinant strain containing the plasmid through a one-step method, so that the loss of fermentation materials can be reduced, the utilization efficiency of equipment is improved, the energy consumption is reduced, and the large-scale production of the rebaudioside M is facilitated.

The invention discloses a method for efficiently synthesizing epiinositol by catalyzing muscle inositol through double-enzyme cascade, and belongs to the field of biological catalysis engineering. According to the invention, scyllo-inositol dehydrogenase is mutated to obtain a beneficial mutant C261R, and the beneficial mutant C261R is coupled with heat-resistant myo-inositol dehydrogenase to efficiently catalyze and synthesize the epiinositol, and belongs to the field of biological catalysis engineering. The new way for synthesizing the epiinositol is completely different from reported synthesis methods of scyllo-inositol and D-chiro-inositol, and comprises the following steps of: firstly dehydrogenating the C4 position of the muscle inositol to form an intermediate product ketone, and then hydrogenating to realize chiral inversion of hydrogen at the C4 position, so as to obtain the final product epiinositol. The invention provides a brand new way for biocatalytically synthesizing the epiinositol, the yield of the obtained epiinositol is 1.39 g / L, the conversion rate is 38.7%, the yield and the conversion rate are the highest level which is publically reported at present, the biosynthesis process is simple to operate, low in cost, green and environment-friendly, and a solid research foundation is laid for industrial production of the epiinositol.

The invention relates to a method for converting lignocellulosic biomass by contacting pretreated lignocellulosic biomass with at least one biocatalyst (3) in an aqueous phase in a first reactor (1) containing a reaction medium, the reaction medium comprises the pretreated lignocellulosic biomass (2) and the biocatalyst in an aqueous phase, the process comprises: (a) a first liquefaction step without removing all or part of the reaction medium from the reactor by adding the pretreated lignocellulosic biomass and at least one biocatalyst to the reactor, followed by (b) a second continuous liquefaction step, wherein a portion of the reaction medium is continuously withdrawn from the first reactor, at least one biocatalyst is added, and pretreated lignocellulosic biomass is continuously added.

The invention discloses a method for biosynthesizing epigallocatechin gallate glucoside, and belongs to the technical field of biocatalytic synthesis. According to the method, a sucrose phosphorylase mutant is adopted as a catalyst, the sucrose phosphorylase mutant is subjected to single-point mutation or combined mutation on the basis of an amino acid sequence SEQ ID NO.1, and the enzyme activity of the sucrose phosphorylase is improved through mutation; the mutant is utilized to realize efficient catalytic synthesis of epigallocatechin gallate glucoside, and in the whole catalytic process, the synthesis method is mild in condition, simple to operate, short in reaction time and high in catalytic efficiency, and has a good application prospect.

The invention discloses a phase transfer catalyst of metal ion complexing crown ether for efficiently preparing aquacide dichloride and application of the phase transfer catalyst. The catalyst is prepared by taking crown ethers as 18-crown-6 and dicyclohexyl-18-crown-6 ether and complex ions as lewis acid active components such as potassium ions, lithium ions, cobalt ions, copper ions and the like through a direct chemical method. The catalyst synergistically catalyzes a nucleophilic substitution reaction of a pyridine derivative and alkyl halide in an aprotic polar solvent such as acetonitrile or nitrobenzene, and synthesis of diquat dichloride can be realized under the conditions of 60-140 DEG C, normal pressure and no oxygen. The mass ratio of the pyridine derivative to the catalyst to the solvent in a reaction system is 1: (0.001-0.05): (5-8), and real-time monitoring and regulation are performed through an online infrared spectrum, a liquid chromatograph and a gas chromatograph-mass spectrometer. The purity of the product is more than 99% after the product is subjected to filtration, recrystallization with an ethanol-water mixed solvent and vacuum drying. The catalyst provided by the invention has the characteristics of high activity, strong stability and recoverability, obviously improves the atom economy of the reaction, simplifies the production process, reduces the energy consumption and pollution, and is suitable for large-scale industrial production.

The present disclosure provides engineered transaminase polypeptides for the production of amines, polynucleotides encoding the engineered transaminases, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases to prepare compounds useful in the production of active pharmaceutical agents.

The invention relates to the technical field of biological catalysis, and discloses an L204A mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: L204A: leucine of the 204 amino acid sequence of UGT76G1 mutates into alanine; the high-efficiency in-vitro enzymatic preparation of the rebaudioside I (RI) is realized for the first time, the catalytic efficiency of the rebaudioside I (RI) is improved by more than 7 times (from about 7% to more than or equal to 50%) compared with that of an original enzyme, the high-efficiency performance can be stably maintained under different scales of 10mL to 5L, a solid foundation is laid for industrial application of the RI, and the preparation method is simple, controllable in process condition and suitable for popularization and application.

The invention relates to the technical field of enzyme engineering, in particular to an acylase mutant and a biosynthesis method of (R)-2-aminobutanol.The acylase mutant comprises at least one of mutation of the following sites relative to wild type acylase with the amino acid sequence being SEQ ID NO: 1: T106, A625 and S413. The acylase mutant disclosed by the invention is used for synthesizing (R)-2-aminobutanol through biological catalysis, and the reaction route is as follows: the catalytic efficiency of a product is remarkably improved by the mutant, and the ee value of a chiral product is improved; according to the synthesis method, the problem of chiral resolution in the prior art is solved, the production cost is reduced, and pollution is reduced.

The invention provides geranial dehydrogenase as well as a preparation method and application thereof, and relates to the technical field of biology, and the amino acid sequence of the geranial dehydrogenase is as shown in SEQ ID NO.1. Citral can be used as a substrate to catalytically synthesize the aromatic folic acid, and the conversion rate reaches 90%. The geranial dehydrogenase can be used for efficiently synthesizing the aromatic folic acid and can be used for biocatalytically converting the aromatic folic acid. Meanwhile, NAD < + > is used as a coenzyme to improve the enzymatic reaction efficiency, so that efficient catalytic synthesis of the aromatic folic acid is realized.

This invention relates to the field of biocatalysis technology, and more particularly to an aflatoxin oxidase, its preparation method, and its applications. This invention utilizes a self-designed artificial intelligence enzyme design workflow to de novo design a novel aflatoxin oxidase, DnD-AFO. Compared to the traditional wild-type AFO, DnD-AFO exhibits enhanced activity, better thermal stability (its activity is significantly superior to the wild-type after high-temperature granulation), and improved resistance to pepsin and acid. Furthermore, it further enhances the detoxification efficiency against aflatoxin, making it well-suited as a food or feed additive for applications in agriculture and food engineering, among other related industries, demonstrating significant commercial and added value.

The invention discloses a heme oxygenase mutant and application of the heme oxygenase mutant in preparation of bilirubin through multienzyme coupling, and belongs to the field of biological catalysis engineering. The forward mutant of the heme oxygenase is obtained through a directed evolution technology, and heme can be efficiently catalyzed to synthesize biliverdin; the bilirubin is synthesized by further introducing biliverdin reductase, coupling cytochrome P450 reductase and formate dehydrogenase, and coupling the two core enzymes with foreign assistant enzymes to construct recombinant escherichia coli to catalyze heme to synthesize bilirubin. In the system, NADPH does not need to be exogenously added, the reaction time is about 4 h, the yield of bilirubin reaches 2.10 g / L, accumulation of intermediate products is not observed in the catalysis process, and the highest yield and the shortest reaction time in bilirubin synthesis reported at home and abroad at present are achieved. Compared with the traditional pig bile extraction, the method disclosed by the invention breaks through the resource limitation, is simple to operate and high in yield, and realizes efficient and green synthesis of bilirubin.