166results about "Plasma/lacto globulins" patented technology

The invention discloses a protein separation method and related application thereof, and relates to the technical field of dairy product processing, the method comprises the following steps: heating a whey solution of which the pH value is adjusted to 3.5-4.2 by a citric acid solution, carrying out microfiltration on the heated product, carrying out beta-lactoglobulin and / or alpha-lactalbumin separation on permeate and trapped fluid obtained by microfiltration, the method is based on the membrane filtration technology, high-purity separation of beta-lactoglobulin and alpha-lactalbumin is achieved, the purity can reach 70%-90% or above, the method is compatible with whey from multiple sources, equipment is simple, the method has the advantages of being low in separation cost, high in efficiency, easy to implement, large in flux and the like, and a way is provided for large-scale industrial production of beta-lactoglobulin and alpha-lactalbumin.

A method for separating protein from a milk raw material, the method comprising separating beta-lactoglobulin and alpha-lactalbumin from the milk raw material, the method comprising: a whey separation step for separating whey protein from the milk raw material; a step of ion exchange treatment: adsorbing the whey protein by using strong anion exchange resin, then eluting by using an eluent, adsorbing the whey protein by using strong anion exchange resin to obtain a flow-through liquid, enriching alpha-lactalbumin in the flow-through liquid, and carrying out gradient elution by using the eluent to obtain an elution component, at least one of the elution components is enriched with beta-lactoglobulin; and purifying the flow-through liquid to obtain an alpha-lactalbumin solid, and purifying the elution component enriched with beta-lactoglobulin to obtain a beta-lactoglobulin solid.

This invention discloses a milk protein containing composition comprising: at least one milk protein; at least a first protein; at least a second protein; and at least a linker comprising an amino acid sequence coded by nucleotide sequence which is at least 80% similar to sequences selected from the group consisting of SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, and SEQ ID NO: 21

To provide a packaged acidic heat-treated beverage preparation which contains whey protein and has an improved organoleptic property and / or visual property.SOLUTION: A packaged heat-treated preparation includes the following: a) proteins in a total amount of 2 to 45% w / w based on a weight of a beverage, whose at least 85% w / w is β-lactoglobulin (BLG); and optionally b) a sweetener, a sugar polymer, and / or an aroma material, the preparation having a pH in a range of 2 to 4.7.SELECTED DRAWING: None

The invention discloses a beta-lactoglobulin modified near-infrared fluorescent targeting probe as well as a preparation method and application thereof. The probe comprises indocyanine green (ICG) and beta-lactoglobulin (beta-LG) which are covalently bound. Compared with the prior art, the probe disclosed by the invention has the advantages that (1) the probe disclosed by the invention improves the stability of the near-infrared fluorescent dye in a body and prolongs the retention time of the near-infrared fluorescent dye, so that the observation window time is prolonged, imaging information is fully acquired in real time, and the effective circulation time in the body is prolonged; (2) the probe has the advantages of good biocompatibility, low toxicity and the like; and (3) the probe can specifically enrich in renal tubules and perform targeted imaging in kidneys, so that diagnosis and treatment of kidney injury, especially acute injury, are realized.

The invention belongs to the technical field of gene engineering, and particularly relates to a strain for efficiently expressing beta-lactoglobulin as well as a construction method and application of the strain. By utilizing the beta-lactoglobulin expression vector disclosed by the invention, beta-lactoglobulin is guided to be secreted out of a host cell by an exogenous signal peptide, and efficient secretory expression of the beta-lactoglobulin in the host cell is realized by integrating a multi-copy expression cassette through a genome and co-expressing ATP enzyme Ssa4 participating in protein folding and coping with pressure; the amino terminal and the carboxyl terminal of the secreted and expressed beta-lactoglobulin do not contain redundant amino acids, and do not contain animal-derived components. Meanwhile, the invention provides a construction method and a fermentation culture method of the engineering strain, compared with a single-copy genetically engineered strain, the expression quantity of the genetically engineered strain in shake-flask fermentation is increased by 2.47 times, and the genetically engineered strain has a good industrial application prospect.

The present invention relates to an improved process for producing a product comprising a protein of interest (TP) capable of crystallizing under salt soluble conditions by crystallization of said TP. The present invention uses at least two different TP-containing protein feeds, which are mixed to produce a supersaturated protein solution in which TP crystallizes. One of the protein feeds must have a pH at least plus 0.1 to the pH (pHMCY, TP) providing the maximum crystallization yield of the TP, and one of the protein feeds must have a pH at most minus 0.1 to the pHMCY, TP.

The invention discloses a method for extracting a target product from a milk raw material, and relates to the technical field of food processing. According to the method, before strong anion exchange chromatography is carried out, a synergistic pretreatment step of ultrafiltration and conductivity adjustment is introduced, so that acceleration, synergism, quality improvement and cost reduction of the chromatography process are realized, and the technical bottlenecks of low speed, easiness in pollution, instability and the like of the traditional ion exchange chromatography during treatment of milk raw materials are overcome; and a solution is provided for high-efficiency, high-purity and large-scale production of the beta-lactoglobulin and the alpha-lactalbumin. According to the method, strong anion exchange chromatography and weak anion exchange chromatography can be combined, so that the extraction purity of beta-lactoglobulin and alpha-lactalbumin can be further improved; in addition, the method can synchronously realize high-efficiency extraction of various target substances such as casein micelles, lactose and milk mineral salts, so that the additional value and resource utilization efficiency of milk source byproducts are greatly improved.

The invention discloses a method for preparing low-bitterness micromolecular bovine colostrum protein peptide powder by adopting a multi-stage membrane separation and enzyme membrane coupling combined technology, and belongs to the technical field of food processing. The preparation method comprises the following steps: firstly, dividing a colostrum component into components to be hydrolyzed by adopting a multi-stage membrane separation technology, namely casein intercepted by ceramic membrane microfiltration and lactoglobulin and lactalbumin filtered by an ultrafiltration membrane, and non-hydrolytic components, namely immune globulin and lactoferrin; the preparation method comprises the following steps: firstly, separating bovine coloctrum, then deeply hydrolyzing the separated lactoglobulin, milky white and casein flocculate with the molecular weight of less than 50kDa by adopting an enzyme membrane coupling technology, mixing with unhydrolyzed immunoglobulin and lactoferrin, and freeze-drying, so that the peptide content in the treated bovine coloctrum is more than 40%, the peptide content of 200-1000Da is more than 30%, the peptide content of 200-1000Da is more than 30%, and the peptide content of 200-1000Da is more than 30%. The preparation method is simple, the preparation dispersion time is within 10 s, no obvious bitter taste exists, the retention rate of immune globulin in bovine coloctrum reaches 90% or above, and the preparation method is suitable for large-scale industrial popularization.

Provided herein are compositions and methods for producing milk proteins, which allow for safe, sustainable and humane production of milk proteins for commercial use, such as use in food compositions. The disclosure provides recombinant fusion proteins comprising at least first protein and a second protein, wherein at least one of the first protein and the second protein is a milk protein, or fragment thereof. The disclosure also provides methods for producing the recombinant fusions proteins, and food compositions comprising the same.

The disclosure relates to synthetic peptides that are capable of modulating metabolism and find uses e.g. in treating metabolic diseases or disorders.

The invention relates to bacillus subtilis for expressing bovine-derived beta-lactoglobulin and a construction method of the bacillus subtilis, and belongs to the technical field of microorganisms. According to the bacillus subtilis provided by the invention, bacillus subtilis BSF01 is used as a host, a constitutive promoter P566 is used for heterologous expression of a bovine-derived beta-lactoglobulin coding gene optimized by a codon, the yield of beta-lactoglobulin obtained by shake flask fermentation for 30 hours reaches 0.37 g / L, the yield of beta-lactoglobulin obtained by 3L fermentation tank fermentation for 44 hours reaches 3.06 g / L, the production intensity is 0.07 g / L / h, and the production cost is low. The bovine-derived beta-lactoglobulin is efficiently and insolubly expressed in a food safety level strain, the food industrial application of the beta-lactoglobulin is promoted, and the problems of food safety and excessive glycosylation possibly existing in heterologous expression of the beta-lactoglobulin in the prior art are solved.

The invention discloses an enzymolysis preparation method of high-immunocompetence bovine coloctrum peptide, active peptide and application thereof, and belongs to the field of biotechnology and functional foods.The enzymolysis preparation method is characterized by comprising the steps that bovine coloctrum is degreased, trehalose is added into obtained supernate, first stirring is conducted, and first mixed liquid is obtained; wherein the supernate comprises whey protein and Ig; adding medium protease into the first mixed solution for hydrolysis to obtain enzymatic hydrolysate; wherein the enzymatic hydrolysate comprises a mixture of bovine colostrum hydrolyzed peptides, the Ig activity retention rate is larger than or equal to 90% through the targeted protection and directional enzymolysis technology, the beta-lactoglobulin peptide with the synergistic immune enhancement effect is obtained, the Ig and small molecule peptides in the product have the synergistic effect, the body immune regulation capacity and the intestinal immune function are remarkably improved, the immunity of the human body is improved, and the immunity of the human body is improved. The method can be widely applied to the fields of infant formulas, postoperative nutrition, functional drinks and the like.

The invention discloses composite modified beta-lactoglobulin as well as a preparation method and application thereof. The preparation method comprises the following steps: dissolving beta-lactoglobulin powder in deionized water to form a beta-lactoglobulin solution; the preparation method comprises the following steps: sequentially carrying out microjet treatment and succinylation treatment to obtain microjet-assisted acylated beta-lactoglobulin, then dialyzing the acylated beta-lactoglobulin solution for purification treatment, and finally freeze-drying to obtain the composite modified acylated beta-lactoglobulin powder. The beta-lactoglobulin is subjected to composite modification by fusing microjet and succinylation, the compact structure of the protein is expanded by the microjet, reaction active sites in the protein are exposed, the solubility of the protein is improved, and meanwhile, convenience is provided for subsequent chemical modification by breakage of non-covalent bonds. The introduction of the succinyl group adjusts the surface property of the protein and improves the emulsifying property of the beta-lactoglobulin. And meanwhile, the oxidation resistance of the beta-lactoglobulin is enhanced due to the oxidation resistance of the succinyl.

The present invention relates to a method to increase the physical stability of a β-lactoglobulin and to a β-lactoglobulin with increased physical stability. The present invention further relates to the use of an extraneous β-lactoglobulin to enhance the physical stability of a composition comprising a protein and the extraneous β-lactoglobulin.

The invention relates to a T7RNA polymerase-guided bacillus subtilis cytosine base editor and application thereof, and belongs to the technical field of gene editing. A T7RNAP guided cytosine base editor is developed in bacillus subtilis, four kinds of cytidine deaminase from different sources are selected to be fused with T7RNAP, the cytidine deaminase is fused at the N end of the T7RNAP, and a fusion body with the highest mutation activity is obtained through screening; the cytosine base editor is used for evolving a global transcriptional regulatory factor CodY, in-situ evolution of genome protein is achieved, and the expression level of bovine-derived beta-lactoglobulin (beta-Lg) is improved. According to the cytosine base editor, the operable range of the cytosine base editor on a genome is widened, multi-site base (C-T) editing can be realized, and an editing window is large.

The invention relates to the technical field of gene engineering and cell engineering, in particular to an sgRNA combination for precisely editing a dairy cow BLG gene, a primer and application. The sgRNA combination comprises: sgRNA1, the sequence of which is as shown in SEQ ID NO. 1; the sequence of the sgRNA2 is as shown in SEQ ID NO. 2; the sequence of the sgRNA3 is as shown in SEQ ID NO. 3; and the sequence of the sgRNA4 is as shown in SEQ ID NO. 4. The BLG gene edited mammary epithelial cells and the BLG gene single base edited dairy cow can be successfully obtained, and the method has a wide application prospect in the aspect of dairy cow breeding.

The invention relates to a truncated casein polypeptide (TCP), said truncated casein polypeptide being preferably selected from alpha S1-casein (αS1-casein), alpha S2-casein (αS2-casein), beta-casein (β-casein), or kappa-casein (κ-casein) polypeptide or a mixture thereof, and compositions comprising thereof. The invention further relates to a dairy product or dairy-like product comprising said truncated casein polypeptide (TCP). Such composition can also be used for the preparation of nutritional product. Finally, the invention further relates to methods of making the truncated casein polypeptide (TCP) of the invention and methods of making the dairy product or dairy-like product of the invention.

The present invention relates generally to food products comprising proteins comprising sulfur-comprising amino acids, and to methods for producing such food products.

Disclosed herein are methods for treating eye diseases, for example eye diseases associated with lipid accumulation, with lipid binding protein-based complexes such as CER-001; lipid binding protein-based complexes, compositions comprising a lipid binding protein-based complex as a carrier for one or more ophthalmic drugs, and uses thereof.

Provided herein are multi-functional chimeric antigen receptor (CAR)-based compositions and their use in directing immune responses to target cells. The compositions have uses that include treating hyperproliferative disorders such as cancer. The provided methods generally include the use of a CAR cell in combination with an Adapter. The Adapter confers the ability to modulate, alter, and / or redirect CAR cell- mediated immune response in vitro and in vivo. In some embodiments, the CAR cell comprises a genetic modification to reduce or eliminate the expression of a targeted antigenic determinant.

Disclosed herein are methods for treating ocular diseases, e.g., ocular diseases associated with lipid accumulation, using lipid-binding protein-based conjugates, such as CER-001; compositions comprising the lipid-binding protein-based conjugates as carriers for one or more ophthalmic drugs, and uses thereof.

The invention belongs to the technical field of protein processing, and particularly relates to modified beta-lactoglobulin as well as a preparation method and application thereof. The modified beta-lactoglobulin is a composite modified product which is obtained by performing a papain hydrolysis treatment process on beta-lactoglobulin to obtain a hydrolysate and then performing glycosylation modification on the hydrolysate by adopting chitosan oligosaccharide and transglutaminase. The product has significantly improved oxidation resistance, emulsifying properties and foaming activity, and is suitable as a food processing ingredient, such as an antioxidant, an emulsifier or a foaming agent.

The invention relates to a truncated casein polypeptide (TCP), said truncated casein polypeptide being preferably selected from alpha S1-casein (αS1-casein), alpha S2-casein (αS2-casein), beta-casein (β-casein), or kappa-casein (κ-casein) polypeptide or a mixture thereof, and compositions comprising thereof. The invention further relates to a dairy product or dairy-like product comprising said truncated casein polypeptide (TCP). Such composition can also be used for the preparation of nutritional product. Finally, the invention further relates to methods of making the truncated casein polypeptide (TCP) of the invention and methods of making the dairy product or dairy-like product of the invention.

The invention features compositions and methods for editing deleterious mutations associated with heme pathologies such as sickle cell disease (SCD). In a specific embodiment, the invention provides a method for correcting mutations in beta globin polynucleotides using a modified adenosine base editor called "ABE8" with unprecedented levels of efficiency (e.g., >60 to 70%).

The present disclosure describes a genetically modified microbial host cell expressing one or more heterologous genes encoding a modified beta-lactoglobulin (BLG), thereby producing the said modified BLG, wherein the modified BLG comprises at least one substitution of a non-essential and / or non-branched amino acid with an essential and / or branched amino acid compared to a parent unmodified BLG.

The purpose of the present invention is to provide a novel peptide, a novel use of the peptide and a method for producing the peptide.　An intestinal barrier function-improving agent, a blood sugar elevation-inhibiting agent, an insulin sensitivity-improving agent, an FGF21 secretion promoter, a stress suppressant or a neuroprotectant, or a fatigue-reducing agent containing a peptide that comprises any one of amino acid sequences LIVTQTMKGL (SEQ ID NO: 1), LIVTQTMKG (SEQ ID NO: 2), LIVTQTMK (SEQ ID NO: 3), IVTQTMKGL (SEQ ID NO: 4), IVTQTMKG (SEQ ID NO: 5) and VTQTMKGL (SEQ ID NO: 6). A peptide that comprises any one of amino acid sequences of SEQ ID NOS: 1, 4, 5 and 6. A method for producing a whey protein hydrolyzate containing a peptide that comprises any one of amino acid sequences of SEQ ID NOS: 1 to 6, said method comprising a step for hydrolyzing whey protein with chymotrypsin.

The invention discloses a construction method and application of a B2m gene knockout SKOV3 cell line, the B2m gene knockout SKOV3 cell line is creatively constructed for the first time, establishment of a cell model will promote precise research of ovarian cancer immunotherapy, a theoretical basis is provided for an individualized treatment strategy of a B2M deletion patient, and the cell model has a good application prospect. The method has a good application prospect and important conversion significance.

A recombinant protein for use in the treatment of a proliferative disease or disorder in a subject is provided, wherein the recombinant protein comprises at least one amino acid substitution or deletion relative to a corresponding native protein, and wherein the recombinant protein is not a hormone, an enzyme or an antibody.