2450 results about "Bioengineerings" patented technology

The AI-enhanced cellular modeling and simulation platform is a computational system designed to enhance biomedical research and development and personalized medicine and wellness. This platform integrates simulation modeling, machine learning and artificial intelligence, multi-omics data, and sophisticated data fusion and decision-support techniques to create comprehensive models of cellular systems and processes across multiple scales. It enables researchers and clinicians to simulate complex biological interactions, predict disease progression, and design or optimize treatment strategies or medical devices with improved accuracy and efficacy. The system's architecture allows for integration of various components, including real-time data processing, federated learning, and quantum computing enhancements. From personalized drug discovery and cancer therapies to synthetic biology and epidemiological analysis, this platform offers powerful tools for understanding and manipulating cellular systems and bioengineered systems. By bridging the gap between molecular-level interactions between cells and materials and organism-wide effects, it enables significant advancements in healthcare and biological sciences.

The invention provides a method for improving synthesis of nucleic acid under a non-diagnostic constant-temperature condition, a kit and application, and relates to the technical field of bioengineering. Provided are: a nucleic acid having an F2 region capable of annealing with F2c in an F region on the same chain at the 3'end, and an R2c region capable of annealing with R2 in an R region on the same chain at the 5 'end; taking the nucleic acid as a template, taking the 3'end of the F1c region annealed with the F1 region as a synthesis starting point, and synthesizing a complementary nucleic acid chain of the nucleic acid; and performing complementary chain synthesis through a polymerase catalytic chain displacement type synthesis reaction so as to replace the complementary nucleic acid chain synthesized in the previous step. The method has the main advantage that a new combination of short-chain primers can be obtained through simple transformation to trigger rapid amplification of gene fragments by applying a single-enzyme constant-temperature system to short-chain nucleic acid fragments.

The invention relates to a fluorescent protein selection marker staygold-levEr gene as well as a construction method and application thereof, and belongs to the technical field of biological engineering. The invention provides a fluorescent protein selection marker staygold-levEr gene for screening an L-valine production strain and a construction method of a gene fragment, compared with other similar gene selection markers, the selection marker provided by the invention has the advantages that the fluorescence intensity is positively correlated with the concentration of L-valine, and the screening marker has the advantages that the screening marker can be used for screening the L-valine production strain; according to the screening marker, the screening efficiency of the L-valine high-yield strain can be obviously improved, the screening time and cost can be saved, the screening efficiency can be improved, and the screening marker has a wide application prospect.

The invention relates to a high-activity recombinant XVII type collagen as well as a rapid preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the high-activity recombinant XVII type collagen is as shown in SEQ ID NO. 1, and the nucleotide sequence of the high-activity recombinant XVII type collagen is as shown in SEQ ID NO. 2. The invention also provides a preparation method and application of the recombinant XVII type collagen. The high-activity recombinant XVII type collagen has good biological activity, has good effects of promoting cell adhesion, cell proliferation and cell migration, and can be compounded with other proteins to form raw materials of tissue engineering products, cosmetics, health care products or medicines. The high-activity recombinant XVII type collagen gene is integrated to different positions of a yeast genome through three different vectors, and the copy number of a target gene is increased, so that the expression quantity of the recombinant XVII type collagen is remarkably increased, and the yield of the high-activity recombinant XVII type collagen is effectively increased.

The invention relates to a high-yield lipase strain and application thereof, and belongs to the technical field of bioengineering. According to the invention, grease-rich samples from different sources are subjected to enrichment treatment, a strain with lipase activity reaching 80.8 + / -1.8 U / mL is obtained through neutral red grease plate screening, the strain is identified as Burkholderia cepacia OCRI-Lip100 through sequencing and sequence comparison, the Burkholderia cepacia OCRI-Lip100 is named as Burkholderia cepacia OCRI-Lip100, and the Burkholderia cepacia OCRI-Lip100 is preserved in China Center for Type Culture Collection on July 3, 2024 with a preservation number of CCTCC M20241369. Lipase obtained by fermentation of the strain is sequenced, enzymatic properties, catalytic activity and substrate preference of the lipase are studied, the optimum catalytic temperature is 60 DEG C, the specific enzyme activity is higher than that of commercial lipase, the catalytic activity is further improved to 116 + / -0.5 U / mL when a C14 substrate is catalyzed, and triglyceride can be hydrolyzed into diglyceride. The strain provided by the invention and the lipase produced by the strain enrich the resource library of the existing lipase, and provide a basis for improving the industrial application of the lipase and realizing the high utilization rate of resources.

The invention provides a high-stability recombinant XVII type collagen as well as a construction method and application thereof, and belongs to the technical field of bioengineering. According to the invention, an amino acid sequence of natural human (XVII) type collagen is selected as a basic unit and repeated for multiple times to obtain recombinant (XVII) type collagen; in the design process of the recombinant XVII type collagen, an unstable GXY triad is avoided, potential matrix metalloproteinase restriction enzyme cutting sites and glycosylation sites are abandoned, a KGD active sequence is reserved, and the probability of containing sites which are easy to degrade can be reduced; a sequence fragment of the recombinant XVII type collagen is derived from a full-length sequence of a natural collagen gene, has excellent solubility, biological activity and high stability, and can be kept stable in a high-temperature storage environment and under the condition of avoiding alkalinity; the product can be used as a raw material in the production process of medicines, medical equipment, biological materials or cosmetics, and has good practicability.

The invention discloses a radish bolting and flowering gene RsSUF4 regulated by m6A demethylase and application of the radish bolting and flowering gene RsSUF4, relates to the technical field of bioengineering, and is technically characterized in that the gene is RsSUF4. The functions of the demethylase RsALKBH10B and the flowering inhibition gene RsSUF4 in the flowering process are analyzed in a targeted manner, and a specific association mechanism between m6A modification and radish flowering regulation and control is defined.

The invention relates to the technical field of bioengineering, and discloses a mutant of Burkholderia lipase as well as a recombinant expression vector and application of the mutant, the mutant comprises P131S, T132A, T251A, T251S, P131A, P131Q, T132G, Q88S and P113A single processes; and a Q88S double process and a P113A double process; and a multi-site mutation combination: a combination I: Q88S, P113A, T132G and L287S, and a combination II: Q88S, P113A, T132G and L287S; a combination II: Q88S, P113A, P131S and L287S; and a combination III: Q88S, P113A, P131S and T251A. Based on experiments, the invention finds that each mutant can not only improve the protein yield, but also improve the enzyme activity by 57% at most; ePA enrichment experiments find that the EPA content of the mutant can be increased by 33% at most, and the mutant has excellent EPA purification and enrichment effects.

The invention discloses a formate dehydrogenase mutant and application thereof in catalytic synthesis of D-mannitol, and belongs to the technical field of bioengineering. According to the formate dehydrogenase mutant provided by the invention, the 18th-site glutamic acid of wild-type formate dehydrogenase with an amino acid sequence shown as SEQ ID NO.2 is mutated into proline, the 57th-site asparagine is mutated into glutamic acid, the 70th-site histidine is mutated into tryptophan, the 235th-site serine is mutated into threonine, and the 316th-site valine is mutated into threonine, so that the formate dehydrogenase mutant is high in enzyme activity and catalytic activity; the coenzyme circulation efficiency during the production of D-mannitol can be obviously improved, so that the yield of D-mannitol can be effectively improved. When the genetically engineered bacterium co-expressed by the formate dehydrogenase mutant and the mannitol dehydrogenase mutant is used for catalyzing 150 g / L fructose to produce D-mannitol, the yield of D-mannitol within 15 h can reach 140 g / L or above.

The invention belongs to the technical field of bioengineering, and particularly relates to recombinant III-type humanized collagen as well as a coding gene and application thereof. According to the invention, a novel III-type humanized collagen sequence is designed by adopting an advanced AI technology and molecular dynamics simulation, so that the recombinant III-type humanized collagen product is ensured to have high stability and degradation resistance. According to the invention, the screened new III-type humanized collagen sequence is transferred to the pichia pastoris strain for recombinant expression, and the prepared recombinant III-type humanized collagen has the advantages of strong stability, high expression quantity and good hydrophilicity, and meanwhile, the recombinant III-type humanized collagen also has obvious effects of promoting cell proliferation and cell adhesion.

The invention discloses an arginine decarboxylase diaA enzyme mutant and application thereof in preparation of butanediamine, and belongs to the field of bioengineering. According to the invention, rational charge overturning transformation is simultaneously carried out on a pentamer meridian oligomeric interface and a dimer latitudinal oligomeric interface, so that stable assembly and efficient catalysis of the decamer under the condition of neutral to alkaline pH (7.0-9.0) are realized. Wherein positive charges are introduced into a meridian interface to weaken electrostatic repulsion, and negative charges are introduced into a latitudinal interface to enhance dimer compactness and substrate transfer efficiency. The specific enzyme activity of the representative double mutant AdiAD110K / H736E at pH 8.0 is about 35 times that of a wild type, and the representative double mutant AdiAD110K / H736E keeps a complete decamer state in a pH range of 7.0-9.0. The yield of butanediamine is up to 145.9 g / L under the whole-cell catalysis of the mutant.

The invention provides a fluorescent protein selection marker staygold-ygjHr gene and application thereof, and belongs to the technical field of biological engineering. The preparation method comprises the following steps: replacing codons of L-valine in nucleotide sequences of a fluorescent protein gene Staygold and a gene ygjH by using a rare codon GTC to respectively obtain a fluorescent protein gene Staygoldr after codon replacement and a gene ygjHr after codon replacement, and connecting the two segments of genes after codon replacement by using a flexible protein peptide to obtain the fluorescent protein selection marker Staygold-ygjHr gene. Experiments prove that the gene can obviously improve the screening efficiency of L-valine high-yield strains.

The invention discloses an anti-degradation recombinant collagen as well as a preparation method and application thereof, and belongs to the technical field of collagen and bioengineering. According to the invention, full-length or partial genes of natural collagen in a human body are selected for certain optimization combination, a collagen amino acid sequence with strong stability and high biological activity is designed, and the amino acid sequence is completely consistent with a sequence of a corresponding region of the natural collagen in theory, and has relatively low immunogenicity; and the collagen has typical biological functions of human body collagen. The recombinant collagen prepared by the invention has excellent stability, biological activity and safety.

The invention belongs to the field of bioengineering, and particularly discloses a glutamate oxidase mutant with improved enzymatic activity. According to the invention, site-specific mutagenesis and saturation mutation are carried out on glutamate oxidase coding genes derived from streptomyces mobaraensis, wherein mutations are C536R, P532R, Q378D, V548E and G236D. After the mutant obtained by the invention is induced and purified, the specific enzyme activity of the optimal glutamate oxidase mutant is 1.69 U / mg and is improved by about 30% compared with that of wild bacteria, which shows that the 378-site amino acid residue has great influence on the catalytic action and stability of the enzyme. In addition, the invention also discloses a construction method of the glutamate oxidase mutant with improved enzymatic activity and application of the glutamate oxidase mutant in production of amino acid derivatives such as alpha-ketoglutaric acid. Therefore, the beneficial mutant provided by the invention can lay a good foundation for industrial fermentation production of alpha-ketoglutaric acid and other products.

The invention discloses a rational copolymerization strategy for improving the stability of an oligomeric structure of acid-induced high-order oligomeric decarboxylase AdiA in a neutral to alkaline environment and application of the rational copolymerization strategy, and belongs to the field of bioengineering. According to the strategy, rational charge overturning transformation is carried out on a pentamer radial oligomeric interface and a dimer weft-wise oligomeric interface at the same time, and stable assembly and efficient catalysis of a decamer under the condition that the pH value is from 7.0 to 9.0 from neutral to alkaline are achieved. Wherein positive charges are introduced into a meridian interface to weaken electrostatic repulsion, and negative charges are introduced into a latitudinal interface to enhance dimer compactness and substrate transfer efficiency. The specific enzyme activity of the representative double mutant AdiAD471K / E467K / H736E is 45.5 times that of a wild type when the pH value is 8.0, and the representative double mutant AdiAD471K / E467K / H736E keeps a complete decamer state when the pH value is 7.0-9.0. The yield of butanediamine is up to 156.5 g / L by using the mutant to catalyze whole cells.

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 P450 mutant and application thereof in synthesis of calcifediol, and belongs to the technical field of bioengineering. According to the present invention, the P450 enzyme mutant enzyme is constructed, and the single plasmid three-enzyme co-expression system of the redox partner and the cofactor cycle enzyme is constructed, such that the sufficient electron transport chain is provided for the P450 enzyme, and the calcifediol can be efficiently synthesized under the mild condition by using the vitamin D3 as the substrate; the conversion rate of calcifediol can reach 63.1%, and the conversion rate of the reaction is greatly improved. By adopting the method disclosed by the invention, the catalytic efficiency of the catalyst is improved, and the reaction cost is reduced.

The invention belongs to the technical field of bioengineering, and particularly relates to recombinant III-type humanized collagen and application thereof. Area fragments with good hydrophilicity in a human III-type collagen alpha chain are selected and sequentially connected to serve as expression protein, the amino acid sequence is 100% identical to that of a corresponding part of natural human III-type collagen, and immunological rejection cannot be generated when the human III-type collagen is applied to a human body. According to the invention, the screened new III-type humanized collagen sequence is transferred into pichia pastoris for recombinant expression, the prepared recombinant III-type humanized collagen has the advantages of strong stability, high expression quantity and good hydrophilicity, and meanwhile, the recombinant III-type humanized collagen also has obvious effects of promoting cell proliferation and cell adhesion.

The present invention belongs to the technical field of bioengineering. Provided are an IscB mutein and the use thereof. Compared to the wild-type IscB protein, the IscB mutein comprises arginine at at least one of the following amino acid positions: position 84, position 96, position 102, position 111, position 159, position 368 and position 386; preferably, the IscB mutein further comprises arginine at position 401 and position 456. The relatively strong interaction between the IscB mutein and a double-stranded DNA target improves the editing activity for mammalian cell lines, which can greatly enhance the application potential of the IscB mutein as a new-generation underlying tool for gene editing, and promote the use of the IscB mutein in the aspects of precision medicine, animal model construction and crop breeding.

The invention discloses humanized III-type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. According to the method, firstly, on the basis of an original humanized III-type collagen gene, cell adhesion activity is taken as an evaluation index, a better cell adhesion sequence is screened out and spliced and integrated with the original collagen gene, and brand-new humanized III-type collagen is obtained. And constructing a recombinant expression vector of the humanized III type collagen containing the adhesion sequence by taking the probiotic EcN as a host cell, and introducing the recombinant expression vector into the EcN to obtain a strain of functional recombinant probiotic. Compared with a traditional escherichia coli engineering bacterium BL21 (DE3), the recombinant probiotics have good cell adhesion activity while efficiently expressing the humanized type III collagen, the bacterial endotoxin content of the recombinant humanized type III collagen obtained through purification meets the industrial standard, and the recombinant probiotics have good application prospects. The purification cost caused by industrial removal of endotoxin can be avoided, so that the production cost is reduced, and the method has a good application prospect.

The invention is applicable to the technical field of bioengineering, and provides a coding gene for enhancing iron deficiency stress tolerance of plants and application. According to the soybean GmMYB14 transcription factor disclosed by the invention, the problem that the growth of soybeans is limited in an iron-deficient environment, particularly calcareous soil and soda saline alkali soil, is solved by excavating and applying the encoding gene (the nucleotide sequence is shown as SEQ ID No.1) of the soybean GmMYB14 transcription factor. Experiments prove that after the gene is over-expressed in arabidopsis thaliana and soybean, the tolerance of plants to iron deficiency stress can be remarkably enhanced. The invention provides a key gene resource for molecular breeding: the GmMYB14 effectively promotes the absorption and utilization of plants on iron by regulating and controlling the metabolic pathway of phenylpropane, not only can improve the planting adaptability of soybeans in low-iron soil, but also can improve the yield and quality of the soybeans, provides powerful technical support for enlarging the planting area of the soybeans in iron-deficient soil regions, and has a wide application prospect. The method is of great significance in relieving insufficient soybean productivity in China and improving the self-sufficiency rate.

The invention belongs to the technical field of bioengineering and artificial intelligence crossing, and particularly discloses a microbial fermentation experiment intelligent design method and system based on a large language model (LLM). According to the invention, a historical database can be automatically retrieved and an experiment resource state can be inquired according to an experiment purpose input by a user intention, an experiment scheme is generated through large language model reasoning, and a task structure which can be identified by an experiment system is synchronized to a digital system so as to support confirmation, optimization and execution of tasks.

The invention discloses a method for regulating the transport activity of a strain to 1-aminocyclopropane-1-carboxylic acid, and relates to the technical field of bioengineering. The method for regulating and controlling the transport activity of the strain to 1-aminocyclopropane-1-carboxylic acid and / or methionine analogues and the tolerance of the strain to the 1-aminocyclopropane-1-carboxylic acid and / or methionine analogues, disclosed by the invention, comprises the step of transferring a LeuE gene into escherichia coli to obtain an escherichia coli recombinant strain with corresponding functions. The invention discloses the application of the LeuE protein and the LeuE gene in regulating and controlling the transport activity of escherichia coli to the 1-aminocyclopropane-1-carboxylic acid and / or methionine analogue and the tolerance of escherichia coli to the 1-aminocyclopropane-1-carboxylic acid and / or methionine analogue for the first time. The invention discloses that LeuE is an optimal candidate gene for constructing ACC synthetic bacteria for the first time, and the substrate specific transport of the LeuE meets the aim of enhancing the ACC tolerance of cells without influencing precursor supply.

The invention belongs to the technical field of bioengineering, and particularly discloses a chimeric enzyme for degrading PET (Polyethylene Terephthalate) as well as a related biological material and application of the chimeric enzyme. The chimeric enzyme for degrading PET provided by the invention is obtained by replacing at least one fragment in an amino acid sequence as shown in SEQ ID No.1-12 on the basis of IsPETase. Compared with IsPETase, the chimeric enzyme for degrading PET provided by the invention has the advantages that the thermal melting temperature is increased by 4.8-31.7 DEG C, the concentration of a degradation product TPA after PET degradation is increased by 1.5-44.5 times, while the application conditions of PET degradation are widened, the PET degradation efficiency can be greatly improved, the recycling rate of the degradation product TPA with high added value is increased, and the chimeric enzyme has important economic value and environmental benefit. The method can be used in the fields of PET degradation, PET degradation agent preparation or PET degradation product preparation and the like.

The invention relates to a CHO-S cell strain capable of stably expressing H5N1 hemagglutinin protein and a construction method of the CHO-S cell strain, and belongs to the field of bioengineering.H5N1 hemagglutinin protein expression plasmids are obtained in an in-vitro synthesis and seamless cloning mode, 293T cells are transfected through the H5N1 hemagglutinin protein expression plasmids, and it is proved that the H5N1 hemagglutinin protein is expressed; the CHO-S cell strain capable of stably expressing the H5N1 hemagglutinin protein is obtained by transfecting CHO-S cells by using the H5N1 hemagglutinin protein expression plasmids and carrying out multiple rounds of cloning and screening, so that a basis is provided for obtaining H5N1 recombinant protein influenza vaccines.

The invention relates to the technical field of bioengineering, in particular to streptomyces noursei capable of producing multimycotin B and application of the streptomyces noursei. According to the invention, gene editing is carried out on the nysL gene and the nysGtf gene or a combination thereof in the streptomyces nosella, so that the yield of the polymycotin B in the streptomyces nosella is remarkably improved. According to the streptomyces noursei for producing the multi-fungal element B, the multi-fungal element B can be efficiently synthesized and accumulated by utilizing low-cost raw materials, the yield of the multi-fungal element B is remarkably increased, and the streptomyces noursei can be used for producing the multi-fungal element B or increasing the content ratio of the multi-fungal element B in prepared nystatin. According to the streptomyces noursei and the method for producing the multi-fungal element B by using the streptomyces noursei, provided by the invention, a strain resource and an effective method are provided for producing the multi-fungal element B and producing nysfungin with a high multi-fungal element B content ratio, and the streptomyces noursei has a relatively good application prospect.

The invention discloses preparation of a whey protein peptide mixture with immune and muscle-building effects, and relates to the technical field of food processing and bioengineering. The neutral protease is adopted and the pH is adjusted, so that the enzymolysis efficiency is effectively improved, and the enzymolysis time is greatly shortened; meanwhile, the whey protein peptide which is uniform in molecular weight distribution, free of peculiar smell and good in thermal stability is successfully prepared by accurately controlling enzymolysis conditions and combining microbial fermentation. The protein peptide can effectively improve thymus indexes and spleen indexes, enhance the proliferation capacity of splenic lymphocytes and the activity of NK cells, play an excellent immune regulation role and have a remarkable muscle building effect. The preparation process has the advantages of high efficiency, low cost, simplicity, convenience and the like, gives consideration to high quality and high functionality of the product, and has great application value.

The invention discloses a Sarcabomyces lipolytica strain for synthesizing (2S)-naringenin and application of the Sarcabomyces lipolytica strain, and belongs to the technical field of engineering and bioengineering. According to the invention, a key enzyme CHS is subjected to semi-rational transformation, so that the yield of the strain (2S)-naringenin expressing the mutant V196A / T132C is increased by 60%. According to the method, the modified CHS is further integrated into a yeast genome, conversion of p-coumaric acid to (2S)-naringenin is promoted by strengthening a shikimic acid pathway and enhancing supply of cofactors, so that the yield of the (2S)-naringenin reaches 776mg / L after the constructed strain is fermented in a 24-pore plate for 96 hours, and the yield of the constructed strain can reach 8.65 g / L after the strain is fermented in a 5L fermentation tank; the method lays a foundation for the subsequent biosynthesis of flavonoid compounds, and has potential value and significance for the development of synthetic biology.

The invention relates to the technical field of bioengineering, in particular to a recombinant VII type collagen for inhibiting scars as well as a preparation method and application of the recombinant VII type collagen. The amino acid sequence of the recombinant VII type collagen is as shown in SEQ ID NO. 1. The recombinant VII type collagen provided by the invention has a better cell adhesion function, so that the recombinant VII type collagen can be applied to the fields of preparation of tissue materials, wound dressings and the like. Meanwhile, the VII type collagen does not contain any tag or exogenous amino acid sequence, is a completely humanized sequence, and does not generate immune response. The VII type collagen has a good adhesion effect, the adhesion effect is better than that of other recombinant collagen, the adhesion effect is equivalent to that of a common cell adhesive in the market, scars can be reduced by inhibiting activation of a TGF-beta pathway, and the VII type collagen can be developed into skin care products and medical instruments for promoting traceless wound repair and has a wide application prospect.

The invention provides bacillus velezensis and application of the bacillus velezensis in co-production of 6-methyl-2-heptanone and 2, 4-di-tert-butylphenol, and belongs to the technical field of biological engineering. The bacillus velezensis is classified and named as bacillus velezensis LT-22, and is preserved in the China Center for Type Culture Collection (CCTCC), the preservation number is CCTCC NO: M2023779, and the preservation date is May 19, 2023. According to the bacillus velezensis, the 6-methyl-2-heptanone and the 2, 4-di-tert-butylphenol can be co-produced, and the concentrations of the synthesized 6-methyl-2-heptanone and the 2, 4-di-tert-butylphenol can reach 75.72 mg / L and 42.48 mg / L; compared with chemical synthesis, the method for preparing the 6-methyl-2-heptanone and the 2, 4-di-tert-butylphenol is low in production cost, simple to operate, high in safety, environment-friendly and suitable for industrial popularization.