294 results about "Isoelectric point" patented technology

Provided herein are bispecific antibodies having modifications that enable greater developability and manufacturability. In certain instances, such bispecific antibodies comprise common light chain bispecific antibodies that bind CD38 and CD19, having reduced isoelectric focusing, improved hydrophobic interaction chromatography retention, and effective targeting of cells expressing CD19 and CD38. Also provided are methods of reducing an experimental isoelectric point of bispecific antibodies that bind CD19 and CD38.

The present invention discloses an injectable human collagen soft tissue filling material and a preparation method thereof, belonging to the technical field of biomedical materials. The injectable human collagen soft tissue filling material comprises pretreated recombinant human collagen and an osmotic pressure regulator, and the injectable human collagen soft tissue filling material is in an isotonic state; the pretreatment of the recombinant human collagen is processed by isoelectric precipitation and centrifugal separation process; the preparation method thereof comprises filtering and sterilizing the raw materials, pretreatment, and homogenizing the pretreated recombinant human collagen and the osmotic pressure regulator. The injectable human collagen soft tissue filling material of the present invention is mainly human collagen, has a large molecular weight and a triple helix structure, and has a uniform particle size distribution, which can play a filling and supporting effect; the preparation process thereof is simple and convenient, without special processing technology, and will not introduce toxic and harmful residual substances, so that the product performance is stable.

The invention discloses a calcium carbonate scale inhibitor for oil and gas field injection and production and a preparation method thereof, and belongs to the technical field of scale inhibitors. The raw materials adopted by the invention comprise maleic anhydride, sodium hypophosphite, 2-acrylamide-2-methylpropanesulfonic acid and methacryloylethyl sulfobetaine, wherein the molar ratio of the maleic anhydride to the sodium hypophosphite to the 2-acrylamide-2-methylpropanesulfonic acid to the methacryloylethyl sulfobetaine is (100-300): (100-300): (5-15): (50-150). The scale inhibitor provided by the invention is used in the injection-production process of oil and gas fields, a sulfo betaine monomer is introduced into the scale inhibitor, the monomer has positive ions and negative ions, the positive ions and the negative ions have the same isoelectric point and do not influence the whole charge performance, and meanwhile, a sulfonic acid strong polar group is introduced into the negative ions, so that the temperature resistance and salt resistance of the scale inhibitor are improved; the cationic charges can improve the dispersing capacity of the scale inhibitor, so that the scale inhibition effect of the scale inhibitor is improved, the scale inhibitor provided by the invention has a relatively good scale inhibition effect on CaCO3, and the scale inhibition rate can reach 90% or above.

The invention relates generally to compositions and methods for purifying the desired species from a mixture of desired heterodimer and contaminating homodimer immunoglobulin variants by modifying the isoelectric point(s) of the individual chains.

The invention belongs to the technical field of biology, and particularly relates to antibacterial peptide based on large yellow croaker CXCL8 protein and application of the antibacterial peptide. The preparation method comprises the following steps: by taking a large yellow croaker CXCL8 protein as a template, intercepting a linear polypeptide of 13 amino acids, and carrying out carboxyl terminal amidation modification, so as to obtain the antibacterial peptide AVV13N, and the amino acid sequence of the antibacterial peptide AVV13N is Ala-Arg-Trp-Val-Arg-Arg-Val-Leu-Lys-Lys-Met-Val-NH2; the antibacterial peptide AVK13N is obtained by interchanging lysine at the 11th site and valine at the 13th site in an amino acid sequence of the antibacterial peptide AVV13N, and the amino acid sequence of the antibacterial peptide AVK13N is Ala-Arg-Trp-Val-Arg-Arg-Val-Leu-Lys-Lys-Val-Met-Lys-NH2. The molecular weights of the antibacterial peptides AVV13N and AVK13N are both 1669.12 Da, the isoelectric points of the antibacterial peptides AVV13N and AVK13N are both 12.44, and the antibacterial peptides AVV13N and AVK13N are both alkaline polypeptides. The antibacterial peptides AVV13N and AVK13N have broad-spectrum bactericidal activity and can be used for specifically killing gram-positive bacteria and gram-negative bacteria. In addition, the antibacterial peptides AVV13N and AVK13N have relatively weak hemolytic activity, relatively low cytotoxicity and good temperature stability, pH value stability and salt ion stability. The antibacterial peptides AVV13N and AVK13N provided by the invention can replace antibiotics and are applied to prevention and treatment of bacterial diseases.

The invention relates generally to compositions and methods for purifying the desired species from a mixture of desired heterodimer and contaminating homodimer immunoglobulin variants by modifying the isoelectric point(s) of the individual chains.

The invention relates to a mussel bionic adhesive material based on oligopeptide modified polyglutamic acid, and a preparation method and application thereof, and belongs to the field of bionic bio-based materials. The preparation method comprises the following steps: firstly, synthesizing tyrosine-containing oligopeptide through protease catalysis, and modifying the oligopeptide onto a polyglutamic acid skeleton to obtain a bionic polymer precursor; meanwhile, polyglutamic acid is modified by cysteine groups, so that a bionic high polymer material with reducibility is synthesized, and a required reducibility reaction environment is provided. The preparation method comprises the following steps: uniformly mixing the polyglutamic acid and the precursor, activating tyrosine in the precursor in a reducing environment by using tyrosinase, converting the tyrosine into dopa to finally obtain a bionic adhesive material solution, and adjusting the pH value of the solution to be close to an isoelectric point of the polyglutamic acid to realize self-assembly to form the adhesive. The adhesive prepared by the preparation method disclosed by the invention shows excellent adhesion performance and also shows good biocompatibility.

The invention discloses synthesized XVII type humanized collagen as well as a preparation method and application thereof, and particularly relates to the technical field of genetic engineering. The amino acid sequence of the recombinant XVII type collagen is as shown in SEQ ID NO. 1. According to the invention, key functional domains (five high-hydrophilicity and high-stability peptide fragments such as 641-685 and the like) in a human XVII type collagen alpha1 chain are retained, and non-functional regions are removed. The 100% human source sequence coverage rate is adopted, the immunogenicity risk of animal source collagen is completely avoided, and the biocompatibility is excellent. The functional peptide fragment is repeated twice to form a stable structure of 210 amino acids, so that the functional activity of the protein is enhanced. The theoretical isoelectric point (pI = 6.07) is close to the pH value (7.4) of human tissue fluid, the dissolvability is excellent, and the applicability is high.

The invention provides peony polypeptide for reducing uric acid as well as a preparation method and application thereof, and belongs to the technical field of biology. The preparation method comprises the following steps: soaking and cleaning peony seed meal with ethanol, centrifuging at 3000-500r for 30-50min, taking a first precipitate, drying the first precipitate, adding water, adjusting the pH value to 9-10, carrying out alkali extraction at 45-55 DEG C for 70-80min, taking supernate, adjusting the pH value to an isoelectric point, and taking a second precipitate; the second precipitate is subjected to enzymolysis for 2-8 h under the conditions that the temperature is 20-80 DEG C, the pH is 5-9, and the protease addition amount is 1500-9000 U / g, and the peony polypeptide capable of reducing uric acid is obtained. The compound has inhibitory activity on xanthine oxidase, and the active components of the compound have stability and functionality by adopting ultrafiltration grading and simulated digestion model exploration.

The invention discloses recombinant humanized XVII type and recombinant humanized I type collagen sequences as well as a synthesis method and application thereof, the recombinant humanized collagen comprises one or more functional sequences in cell integrin binding sites such as R / KGD, GER / K, GVMGFP and DGEA, the molecular weight is 6-14 kDa, and the recombinant humanized collagen simultaneously surrounds an isoelectric point, has hydrophilicity and hydrophobicity, and can be used for preparing the recombinant humanized collagen. Reasonable design is carried out on information such as an antigen epitope, GXY sequence stability, protease degradation sites and the like, so that the recombinant humanized collagen has relatively good stability and also has biological activity of promoting cell proliferation and resisting wrinkles and tightening.

A qualitative or quantitative test method to detect a substance to be detected contained in a specimen, the test method including a preparation step of preparing a test sample from the specimen, and a test step of testing at least part of the test sample with a reagent to detect each of a first substance to be detected and a second substance to be detected, in which the first substance to be detected has an isoelectric point of 10.0 or more, and in any one or both of the preparation step and the test step, the first substance to be detected is brought into contact with any one or both of a glass-made member and a nitrocellulose-made member in the presence of a cationic substance. In this test method, two or more substances to be detected including a substance having an isoelectric point of 10.0 or more can be detected with high sensitivity using the same specimen while suppressing a decrease in measurement sensitivity.

The invention provides a method for purifying a semeglutide precursor, and belongs to the technical field of polypeptide preparation.The method comprises the steps that a precursor crude sample solution obtained after enzyme digestion in the synthesis process is treated through isoelectric point precipitation, precipitation is taken and suspended again, then hydrophobic chromatography purification is conducted, and the purified semeglutide precursor is obtained. Meanwhile, the hydrophobic chromatography process is easy for linear amplification and low in production cost, and the feasibility of amplified production is greatly improved; besides, most of impurities such as enzymes and pigments can be removed after pretreatment by an isoelectric precipitation process, and after hydrophobic chromatography purification, the purity of the semeglutide precursor is greatly improved and can reach 95% or above, the hydrophobic purification yield is greater than 80%, product related impurities generated by enzyme digestion are effectively removed, and the product quality is improved. The purified precursor can be directly used for subsequent modification and other process steps.

The invention relates to tetanus subtoxin and a preparation method thereof. The preparation method specifically comprises the following steps: providing or constructing a tetanus toxin Hc fragment mutant TeNT-Hc strain; inoculating the TeNT-Hc strain into a seed culture medium according to an inoculum size of 0.1%-0.5%, and carrying out shake culture until the OD600 value reaches 0.8-1.5 to obtain a first-stage seed culture solution; further increasing the number of strains on the basis of the first-stage seeds to obtain a second-stage seed culture solution; performing fermentation; re-suspending, crushing and centrifuging the bacteria, collecting supernate, carrying out Ni column affinity chromatography on the supernate, washing impurities and eluting, and collecting eluent; and carrying out second-step purification on the eluent through isoelectric precipitation or Q anion exchange or SP ion exchange, and collecting the supernate or the eluent to obtain the tetanus subtoxin. The purity of 95% or above is achieved through two-step purification, and meanwhile the expression quantity of the target protein is increased.

The invention provides a fluorine-doped Fe-N-C composite material as well as a preparation method, application and regeneration thereof, and belongs to the technical field of water pollution. The preparation method comprises the following steps: firstly, mixing an iron precursor, zinc salt, an organic ligand and an organic solvent to synthesize a Fe-doped metal organic framework Fe (at) ZIF-8 material, and then carbonizing the Fe-doped metal organic framework Fe (at) ZIF-8 material into a Fe-N-C material; and then Fe-N-C and a fluorine source are mixed and subjected to secondary carbonization, and the fluorine-doped Fe-N-C composite material is obtained. Fluorine atoms are introduced into the Fe-N-C material and generate axial coordination with Fe in the center of FeN4, the fluorine element with high electronegativity can effectively improve the isoelectric point of the Fe-N-C material, the reaction activity of the material is enhanced, Fe leaching of the material in the reaction process is inhibited, and the stability of the material is improved. In addition, the prepared fluorine-doped Fe-N-C composite material can continue to be recycled through fluorine doping regeneration, and high reduction activity and stability are kept.

The invention belongs to the technical field of biomedical engineering, and particularly relates to a polypeptide preparation method for preparing a GLP-1 analogue through tandem expression. According to the method, a coding gene sequence of the GLP-1 analogue is repeatedly connected in series for a plurality of times, and then expression preparation is carried out on the basis of a genetic engineering technology. The inventor optimizes a series-connected polypeptide structure by adding a section of key peptide sequence. The key peptide serving as a leading peptide can greatly improve the expression quantity of the strain in the fermentation expression process; as a linked peptide, the key peptide sequence can effectively improve the recognition capability of enzyme digestion sites on one hand and can adjust the overall isoelectric point of the sequence on the other hand, so that the solubility, enzyme digestion yield and purity of a target product can be improved. Preliminary experiment results show that the expression quantity of the polypeptide prepared through expression is extremely high, the enzyme digestion efficiency is good, the good enzyme digestion efficiency can be achieved under the condition that the enzyme dosage is low, and the yield and purity of the final GLP-1 analogue are high.

The invention provides an apolipoprotein B detection kit and a use method thereof, the apolipoprotein B detection kit comprises a reagent R1 and a reagent R2, the reagent R1 comprises the following components: 40-80 mmol / L of an HEPES buffer solution, and 1-5 g / L of polyethylene glycol 6000; naCl is 5 g / L to 9 g / L; the preservative is 1g / L to 5g / L, and the surfactant is 1g / L to 5g / L; the pH value of the reagent R1 is 7.0 to 7.5; the pH value is 7.0-7.5 in the reagent R1, so that the pH value is below the isoelectric point of apolipoprotein B, and after the apolipoprotein B and the reagent R1 are mixed, protein in a detection sample can present weak negative charge property; accordingly, hyaluronic acid is added into the reagent R2, the hyaluronic acid and the anti-human APOB antibody in the reagent can form an integrated substance with weak covalent bond combination, and the hyaluronic acid has positive charges, so that apolipoprotein B can be rapidly combined with the anti-human APOB antibody through the attraction of the charges, the problem of long-time incubation is avoided, and the detection accuracy is improved. The detection time is shortened and the accuracy of the detection result is ensured.

The invention provides an extracellular vesicle marker separation-free detection method based on nanoparticle enhancement, and belongs to the technical field of detection methods, the method comprises the following steps: preparing gold nanoparticles with the surface modified with a first antibody, the first antibody being used for specific recognition of an extracellular vesicle surface marker; determining the particle size distribution of the gold nanoparticles by adopting a dynamic light scattering method, and determining the surface potentials and surface isoelectric points of the gold nanoparticles by adopting a potentiostat; adopting a transmission electron microscope to characterize the morphology of the screened gold nanoparticles; co-modifying polyethylene glycol molecules on the surfaces of the gold nanoparticles to form an anti-interference layer; mixing the gold nanoparticles with uniform morphology with a sample to be detected; adding a second antibody into the mixed system; distinguishing signals of the binding-state second antibody and the free-state second antibody through fluorescence lifetime analysis; preparing an extracellular vesicle standard substance, and obtaining a standard curve and a system response curve; the optimal detection condition is determined by solving the detection system optimization equation set, and separation-free detection is carried out.

An anti-rabies virus neutralizing antibody and preparation and a use thereof. Provided is an anti-rabies virus neutralizing antibody, comprising a heavy chain variable region SEQ ID NO. 1-SEQ ID NO. 3, a light chain variable region SEQ ID NO. 4-SEQ ID NO. 5, and GAS. The anti-rabies virus neutralizing antibody has good neutralizing activity; a high isoelectric point provides advantages in the stability of antibody formulations; a high Tm value indicates good thermal stability; strong affinity with recombinant rabies virus glycoproteins shows promise for the mass production of rabies virus neutralizing antibodies, providing technical support for the preparation of low-cost, safe, and effective rabies passive immune formulations.

The invention discloses cellulose nanocrystal Pickering emulsion gel with stable protein hydrophobic modification and a preparation method of the cellulose nanocrystal Pickering emulsion gel, oil-in-water type emulsion gel is prepared and formed under the shearing action based on cellulose nanocrystals (CNCs) coated with protein or protein sodium salt with an isoelectric point in a range of 4-6, so that a stable gel network structure is formed; by adjusting conditions of different protein coating proportions, particle concentrations and internal phase proportions, the emulsion gel can obtain different processability, and the emulsion gel based on different performance differences has good application flexibility in 3D printing. The main materials are safe in source and have good biocompatibility and biodegradability, the modification method is green and safe, and the prepared emulsion gel can be used as a food 3D printing base material or a nutrient substance loading material.

The invention relates to the field of biological medicine preparation, and particularly provides liraglutide precursor peptide tandem recombinant fusion protein, polynucleotide, recombinant expression plasmid, engineered host cell and a method for preparing target polypeptide. The recombinant fusion protein is fusion peptide-target polypeptide-(linker peptide-target polypeptide) n from the N terminal to the C terminal, n is a positive integer from 4 to 6, the fusion peptide is SEQ ID NO.1, the target polypeptide is liraglutide precursor peptide, the linker peptide comprises a spacer peptide and a protease restriction enzyme cutting site, the spacer peptide is SEQ ID NO.2, the isoelectric point of the recombinant fusion protein is 4.6-4.7, and the average hydrophilic value is-0.780--0.765. The proportion of the target polypeptide in the recombinant fusion protein is high, use of solvents under extreme conditions is avoided in the production process, the enzyme digestion efficiency is high, and the product purity and yield are high.

The invention relates to a method for separating out and condensing specific protein in liquid for dyeing and detection. The liquids include but are not limited to human samples, human blood, saliva, urine and the like. The liquid is diluted and its pH is raised or lowered to form a mixed liquid. Placing the mixed solution in an electrostatic field, moving the specific protein in the mixed solution to one side of the mixed solution, accurately dropwise adding an acidic or alkaline solution, adjusting the pH value of the mixed solution, enabling the pH value of the mixed solution to reach the isoelectric point of the specific protein, and enabling the specific protein to be separated out and precipitated on one side of the mixed solution. In addition, according to the sequence of the pH values from large to small or from small to large, the isoelectric points of all the specific proteins can be traversed in the process, and all the specific proteins can be separated out and precipitated in the same area of the mixed solution.

A method of processing of electrocardiogram (“ECG”) signals from at least one ECG lead connected to a patient includes computing an average beat from a plurality of beats occurring during a predetermined averaging interval. An onset point, isoelectric point, and a J-point of the average beat is computed to establish an S-T segment of the average beat. The isoelectric point and the J-point of the average beat are used to determine an S-T segment for each beat of the averaging interval, and the average of the S-T segments of each beat is computed and averaged with the S-T segment of the average beat.

The present invention relates to the technical field of waste recovery, and provides a method for preparing a hemihydrate gypsum powder from phosphogypsum by means of an atmospheric salt solution process, and a hemihydrate gypsum powder. The method comprises: preparing a slurry from a mixed liquid of a salt and a crystal modifier and purified phosphogypsum, wherein the crystal modifier is a betaine compound with pH responsiveness; and adjusting the pH value of the slurry on the basis of the isoelectric point of the crystal modifier and the required length-diameter ratio of hemihydrate gypsum crystals, subjecting the slurry to a constant-temperature dynamic reaction, and filtering same, thereby obtaining a hemihydrate gypsum powder, wherein when the pH value of the slurry is greater than the isoelectric point of the crystal modifier, the length-diameter ratio of the hemihydrate gypsum crystals increases, and when the pH value of the slurry is less than the isoelectric point of the crystal modifier, the length-diameter ratio of the hemihydrate gypsum crystals decreases. By using the betaine compound as the crystal modifier, hemihydrate gypsum crystals with different length-diameter ratios can be obtained by adjusting the pH value of the slurry, and therefore the regulation and control of the crystal morphology of hemihydrate gypsum are achieved and exhibit a certain pattern.

The invention relates to the field of biological medicine preparation, and particularly provides canagliflozin precursor peptide tandem recombinant fusion protein, polynucleotide, recombinant expression plasmid, engineered host cell and a method for preparing target polypeptide. The recombinant fusion protein is a fusion peptide-target polypeptide-(linker peptide-target polypeptide) n from an N terminal to a C terminal, n is a positive integer of 4-6, the fusion peptide is SEQ ID NO.1 or SEQ ID NO.2, the target polypeptide is a canagliptin precursor peptide, the linker peptide comprises a spacer peptide and a protease restriction enzyme cutting site, the spacer peptide is SEQ ID NO.3, the isoelectric point of the recombinant fusion protein is 5.5-6.5, and the average hydrophilic value is-0.85--0.96. The invention creatively provides a method for preparing the canagliflozin precursor peptide by using a gene recombination technology, the proportion of the target polypeptide in the recombinant fusion protein is high, the use of a solvent under extreme conditions is avoided in the production process, the enzyme digestion efficiency is high, and the product purity and yield are high.

The invention provides a gel composition, a product containing the gel composition and application of the gel composition. The gel composition comprises gelatin; wherein in the gel composition, the content of the gelatin is 4-13%, and the content of the fat-soluble component is not less than 10% according to the mass percent; the mass ratio of the gelatin to the sugar alcohol is 0.12-0.4; the isoelectric point of the gelatin is I, the pH value of the diluted gel composition when the mass concentration is 1% is H, and the following relational expressions are met in the gel composition: 1lt; i to Hlt; 5.3). The gelatin and the sugar alcohol are introduced, the content and the proportion of the gelatin and the sugar alcohol in the gel composition are controlled, the pH value of the gel composition and the isoelectric point of the gelatin are regulated and controlled to keep a certain difference value, and the relationship among the surface viscosity, the cohesion and the affinity of the packing material in the gel composition is balanced; the gel composition can still keep the complete form after the packing material is removed, and meanwhile, the taste, hardness, formability and the like of the gel composition are not influenced.

The application discloses a vaccine and a preparation method thereof, and the preparation method comprises the following steps: mixing an acidic protein antigen solution containing a phosphate buffer solution with an aluminum adjuvant to make the molar ratio of phosphorus and aluminum below 0.9, so as to obtain an acidic protein vaccine; or mixing the aluminum adjuvant with a solution containing phosphate ions to make the molar ratio of phosphorus and aluminum above 0.2, and then mixing the aluminum adjuvant with an alkaline protein antigen solution containing a phosphate buffer solution, so as to obtain an alkaline protein vaccine; wherein the acidic protein antigen is any kind of protein antigen with a net negative charge; and the alkaline protein antigen is any kind of protein antigen with a net positive charge. According to the preparation method, the molar ratio of phosphorus and aluminum is adjusted to a specific range according to the net charge of the protein antigen, so that the isoelectric point of the aluminum adjuvant can be effectively changed, the charge carried by the aluminum adjuvant is opposite to the charge carried by the protein antigen, and then the aluminum adjuvant and the protein antigen are attracted to each other through electrostatic interaction. The vaccine antigen prepared by the method has high antigen adsorption rate and good stability, the preparation method is simple, and the method is suitable for industrial application.

The invention discloses a method for rapidly and efficiently extracting ovotransferrin in egg white, which comprises the following steps: (1) pre-treating egg white, namely treating egg white liquid through an ultrasonic composite high-voltage pulse electric field, so that the thick protein is thinned, the viscosity is further reduced, molecules are dispersed, the egg white liquid is prevented from being diluted by adding water in the subsequent process, and the production efficiency is favorably improved; (2) removal of ovomucin and ovalbumin: removing the ovomucin and ovalbumin by an isoelectric precipitation method combined with a PEG precipitation method; (3) preparation of ovotransferrin; (4) separating an ovotransferrin crude product; and (5) purifying the ovotransferrin crude product. According to the method disclosed by the invention, high-yield and high-purity ovotransferrin is rapidly and efficiently prepared, and the method is simple, relatively low in cost and suitable for large-scale industrialization.

The invention discloses a large-through-flow varistor and a preparation method thereof, and belongs to the technical field of varistors, the varistor is prepared from the following raw materials: 93 to 96 mol percent of modified ZnO, 1.2 to 1.6 mol percent of Bi2O3, 0.5 to 1.5 mol percent of Co3O4, 0.3 to 0.8 mol percent of Mn2O3, 1.0 to 3.0 mol percent of Sb2O3, 0.3 to 0.8 mol percent of NiO and 0.05 to 0.3 mol percent of Li2CO3; a silane coupling agent with a fluorinated quaternary ammonium salt structure is adopted to modify the surface of ZnO, and the quaternary ammonium salt structure improves the isoelectric point of ZnO, so that ZnO is positively charged at a relatively high pH value, the interaction with an anionic dispersant is enhanced, and the effect of the anionic dispersant on slurry is improved; f <-> introduced by the silane coupling agent is uniformly dispersed on the surface of ZnO, during subsequent sintering, Li < + > is used as a diffusion carrier, the migration rate of F <-> in crystal lattices can be improved through the synergistic effect of Li < + > and F <->, and the property of the ZnO varistor is enhanced by introducing Li < + > and F <->.

The invention discloses a method for detecting a charge variant of a monoclonal antibody. The method comprises the following steps: preparing a monoclonal antibody to be detected into a test solution; the test solution comprises a monoclonal antibody to be detected, a methylcellulose solution, urea, amino acid, an ampholyte carrier and an isoelectric point marker; detecting the test solution by adopting a full-column imaging capillary isoelectric focusing method, and determining the content percentage of the charge variant of the monoclonal antibody to be detected according to an isoelectric focusing map; wherein the isoelectric point of the amino acid is similar to the boundary isoelectric point of a main peak and an alkali peak in an isoelectric focusing map of the monoclonal antibody to be detected. According to the method, the separation degree between the main peak and the alkali peak of the to-be-detected sample can be remarkably improved. The sensitivity is good, the precision is high, and while the separation degree of a main peak and an alkali peak is improved in a targeted manner, the separation degree and proportion of an acid peak and the main peak, the isoelectric point of a sample and the like are basically not influenced.

The application discloses a biosynthesis method of blue copper peptide, comprising the following steps: synthesizing a recombinant protein according to an amino acid sequence shown in SEQ ID NO. 1, synthesizing a gene coding the recombinant protein, constructing a recombinant plasmid by using the gene, transferring the recombinant plasmid into a host bacterium, carrying out fermentation culture to induce protein expression, separating the protein, carrying out enzyme cutting and purification, and finally carrying out complexing with copper ions to obtain the blue copper peptide. Compared with the prior art, the biosynthesis method of the blue copper peptide has the advantages of low production cost, green environmental protection and high yield by optimizing the design of the fusion protein, and the yield of the final product can be significantly improved, and the fusion protein has better structure and isoelectric point characteristics.