41 results about "Globular protein" patented technology

A nanoparticles-containing composite porous body according to the present invention includes a porous body having a solid skeleton and pores and nanoparticles of an inorganic substance. The nanoparticles are carried on the solid skeleton without coagulating together or being chemically bonded to the skeleton. The nanoparticles may be coated with organic aggregates and carried as composite particles on the solid skeleton. As the organic aggregates, spherical organic aggregates such as a spherical protein or a dendrimer are preferably used. Also, the organic aggregates may be decomposed and removed if necessary.

Macro hydrophobic clusters and complexes of soybean globular proteins were observed using TEM (Transmission Electron Microscope). Upon unfolding, hydrophobic groups of the proteins became exposed toward the surface of the protein and actively interacted with other hydrophobic groups of other protein molecules, thereby forming hydrophobic bonding. The hydrophobic bonding resulted in hydrophobic protein clusters, the formation of which was affected by the degree of protein unfolding, protein structure, and hydrophobic components. Such hydrophobic clusters followed the global minimum free energy theory and formed spherical like structures with diameters ranging from 100 nm to 3000 nm. Such an understanding lends applicability to many uses in adhesives, molding composites, surfactants for oil-water systems, bio-based interior construction paints and paper coatings, fiber production, and metal powder molding applications.

An immobilized protein catalyst is prepared by applying an adhesive to a polymeric support, applying a layer of a globular protein over the layer of adhesive, binding a crosslinking agent to the protein layer, and binding the protein catalyst by reaction with the crosslinking agent.

The present invention relates to systems and methods for the determination of the secondary structure composition of proteins using coherent two-dimensional infrared (2DIR) spectroscopy of backbone amide I vibrations (1580-1720 cm−1). Fractions of α-helix, β-sheet, and unassigned regions in globular proteins were determined by singular value decomposition using basis spectra from sixteen commercially-available proteins with known crystal structures. Preferred methods included removing each protein from the set and comparing the predicted composition against the crystal structure. The root-mean-squared (RMS) errors of the predicted secondary structure compositions were found to be 7.9% for α-helix, 5.5% for β-sheet, and 7.6% for unassigned regions. The structure analysis can also be performed using one-dimensional absorption spectra and the RMS errors are compared with those obtained from 2DIR.

The invention provides a processing method of instant crisp fish. The method is performed according to the following ten steps: step one, fish selection, dissection and cleaning; step two, strip cutting; step three, salting; step four, drying; step five, aging; step six, frying; step seven, marinating; step eight, vacuum packaging; step nine, sterilizing; and step ten, cooling. Instant crisp fish processed through the method has no earthy taste, original flavors are maintained, the oil infiltration capacity during frying is small, the fish is free of greasy feelings when eaten, globular proteins in fish meet after aging are reorganized to form thread-shaped lean meat structures, the chewing feeling is good, the frying time is short, the fish is crisp and tender, tastes are good, anise and pepper are put in a leaching liquid mode to be seeped into fibers in fish meet, flavors are rich, and the appearance has no particles. According to the processing method, original flavors and nutrition values of fish meet are maintained, and the instant crisp fish is convenient to carry and eat.

A food product is provided comprising at least 50 grams of a pH responsive hydrogel comprising a cross-linked globular protein having an unfolding transition pH in the range pH 2 to 6. Also provided are a process for manufacturing the food product and use of a pH responsive hydrogel to provide an enhanced feeling of satiety to a person consuming the hydrogel and / or to aid adherence to a weight loss or weight control plan.

The invention related to a method for producing molded bodies made of cross-linked native polymers in such a way that a network is formed by chemically coupled functional groups, hydrogen bridges or polymer or oligomer structures helically connected to each other and up to 200 mass % of micro-encapsulated phase change material is included into a polymer matrix with respect to the cross-linked polymer. Said cross-linked polymers can, for example be embodied in the form of polysaccharides and / or globular proteins. In the form of fibers the molded bodies can be processed to textile fabrics having enhanced thermoregulation properties and an improved wearability to the textiles produced therefrom, as well as a high functionality with respect to heat storage and heat removal when used in other applications.

A manufacturing method for a protein structure quick switch memristor array relates to the manufacturing method for protein structure memristor array. The manufacturing method solves the problems that the existing manufacturing method for a memristor model has low manufacturing cost and the prepared memristor manufacturing model has low on-off speed. The manufacturing method uses a method combining a micro electronic technique and a biochemistry technique for fixing bovine immunity globular protein on semiconductor material, prepares biology cell membranes, and then manufactures the protein structure quick switch memristor array; the preparation method for the nanometer structure memristor array is simple; the used raw materials have low price and low manufacturing cost; and the manufactured memristor array has quicker on-off speed.

The invention relates to a sterilized liquid or semi-solid acid enteral composition comprising per 100 ml 9 to 20 g of non-hydrolysed globular proteins, fat and at least 100 mg of divalent metal cations and having a pH ranging between 3 and 5. The invention further relates to a method for preparing a composition according to the invention, comprising a step wherein at least the non-hydrolysed globular proteins are subjected to a direct steam injection (DSI) at specific holding values, such as a holding temperature of 100 to 140° C. during a holding time of about 0.5 to 10 seconds, followed by a homogenization step and a sterilization step The composition according to the invention has a reduced astringency and can be used for medical purposes, such as for stimulating muscle protein synthesis in a mammal, in particular for treating sarcopenia, and for specific groups of people, such as elderly and sportsman.

An immobilized protein catalyst is prepared by applying an adhesive to a polymeric support, applying a layer of a globular protein over the layer of adhesive, binding a crosslinking agent to the protein layer, and binding the protein catalyst by reaction with the crosslinking agent.

The present invention relates in general to a shelf-stable liquid enteral composition for providing nutrition, either as a supplement, or as a complete nutrition, with a high protein content of a non-hydrolysed globular protein, in particular a whey protein.

A method for cross-linking albumin for use as a sealant or glue for a biological system, for example to induce hemostasis and / or prevent leakage of any other fluid from a biological tube or tissue, such as lymph for example. The cross-linked albumin may optionally and preferably be applied as part of a bandage for example. In other embodiments, the present invention provides a method of enzymatically cross-linking globular proteins, by altering the structure of the protein to improve the accessibility of the protein to the cross-linking enzyme.

Protein engineering is an emerging area that has expanded the understanding in the art of protein folding and laid the groundwork for the creation of unprecedented structures with unique functions. The first native-like pore-forming protein, small globular protein (SGP), has previously been designed. It has now been discovered that this artificially engineered protein, and analogs and homologs thereof, have membrane-disrupting properties and anti-tumor activity in several cancer animal models. A mechanism for the selectivity of SGP toward cell membranes in tumors is proposed and validated herein, thereby confirming the proposed mechanism of action. Thus, SGP is established herein as the prototype for a new class of artificial proteins designed for therapeutic applications.

The invention provides a detection method used for measuring doxercalciferol and impurities contained by doxercalciferol. According to the detection method, high performance liquid chromatography is adopted, and chromatographic conditions are determined as following: globular protein bonded with hydrophilic silicone or octadecyl silane is taken as the stationary phase, a mixed solution composed of an acid solution and an organic solvent is taken as the mobile phase, flow velocity is controlled to be 1.5 to 2.0ml / min, detection wavelength is controlled to be 210nm, column temperature is controlled to be room temperature, sample size is controlled to be 5 to 10<mu>L, sample concentration is controlled to be 3 to 5mg / ml, and the volume ratio of the acid solution to the organic solvent solution in the mixed solution is reduced in a gradient manner with elution progress of high performance liquid chromatography. In the gradient elution process of high performance liquid chromatography, the volume ratio of the acid solution to the organic solvent solution in the mixed solution is reduced in a gradient manner with elution progress of high performance liquid chromatography, so that synchronous separation and detection of doxercalciferol and three impurities contained by doxercalciferol are realized, separation and detection efficiency is increased, and detection time and relative retention time of main peaks are shortened.

The invention relates to the field of the chemical analysis and in particular to a method for measuring an atosiban acetate related substance. The method for measuring the atosiban acetate related substance comprises the following steps: using globular protein hydrophilic modified silica gel as a chromatographic column filling and loading a sample of test solution, after eluting by using a mobilephase A of which solution is acidic and an organic solvent as a mobile phase B, detecting, wherein the eluting is performed in a volume proportion of the mobile phase A and the mobile phase B which is60-90:10-40. The method is capable of rapidly and effectively separating and detecting atosiban acetate crude drugs and the related substances in injection.

The present invention relates to a buffering composition, more closely a composition comprising porous matrix-enclosed buffering agent(s) giving a stabilisation of pH when applied in for example aqueous environment.The composition comprises buffering agent(s) enclosed in a first porous matrix with an impenetrability corresponding to a fractionation range for globular proteins and peptides of <10000 g / mol, preferably <5000 g / mol, more preferably <700 g / mol.

This invention relates to SPPs, spherical nanocrystalline composite particles or crystalline SPPs of biologically active proteins or compositions, including formulations, comprising such SPPs, spherical nanocrystalline composite particles or crystalline SPPs. More particularly, methods are provided for the production of SPPs, spherical nanocrystalline composite particles or crystalline SPPs of high concentrations of biologically active proteins, and for the preparation of stabilized SPPs, spherical nanocrystalline composite particles or crystalline SPPs for use alone, or in dry or slurry compositions. This invention also relates to methods for stabilization, storage and delivery of biologically active proteins using SPPs, spherical nanocrystalline composite particles or crystalline SPPs. The present invention further relates to methods using SPPs, spherical nanocrystalline composite particles or crystalline SPPs, or compositions or formulations comprising such SPPs, spherical nanocrystalline composite particles or crystalline SPPs, for biomedical applications, including biological delivery to humans and animals.

The invention provides a method for detecting a related substance II of cefpirome in cefpirome sulfate / sodium chloride injection. According to the method, experiments on chromatographic conditions and system suitability are performed by using high-performance liquid chromatography. For the color spectrum which is suitable for separating globular protein of which the molecular weight is 1,000-5,000, hydrophilic silica gel serves as a filler, and phosphate buffer solution-acetonitrile of which the volume ratio is 85:15 serves as a mobile phase, wherein the flow velocity is 0.5 ml / min, the phosphate buffer solution consists of 0.05 mol / L disodium hydrogen phosphate and 0.05 mol / L sodium dihydrogen phosphate which are mixed in the volume ratio of 50:50, and the measurement wavelength is 254 nm. The method comprises the following steps of: placing appropriate amount of cefpirome sulfate / sodium carbonate mixed powder which comprises 10 mg of cefpirome into a 10 ml measuring flask, wherein the mixed powder is taken out of an infusion bag; adding water to dissolve the mixed powder and diluting to certain scale, and shaking up; and injecting 20 mu l of the diluted solution into a liquid chromatograph to perform chromatography, and recording a chromatogram. The detection method is advanced, reliable, high in accuracy and high in specificity, the experimental apparatus is high in precision, high in reproducibility and high in stability, the related substance II of the cefpirome can be effectively detected, and the method can be used for quality control.

The invention discloses a flame-retardant wool fabric finishing method. The method includes the steps of adding a monopotassium phosphate aqueous solution to preprocess a wool fabric, dispersing globular proteins slightly cross-linked between fiber cells of the wool fabric, and conducting later-period enzyme processing; conducting enzymolysis preprocessing on the wool fabric through mixed protease obtained by mixing ficus proteinase, pronase and bromelain, making mixed protease adsorbed to surfaces of wool fibers and penetrate through the whole fibers, dispersing mixed protease along the fibers, and conducting hydrolysis, so hydrolysis is continuously conducted in sebum layers of wool fibers, and it is ensured that inner layers of wool fibers are prevented from damage; modifying the wool fabric through alkaline protease. The content of disulfide bonds in the wool fibers is decreased, the content of sulfydryl groups is increased, and the flame retardance of the wool fabric is improved; meanwhile, the washable degree of the wool fabric can be improved, the influences on the whiteness and hand feeling of wool are small, and high economic benefits are achieved.

The invention belongs to the technical field of drug detection, and particularly relates to a method for detecting polymer impurities of ceftriaxone sodium. According to the method, a ceftriaxone sodium raw material medicine is taken to prepare a test solution, HPLC detection is carried out, and the detection conditions are as follows: a chromatographic column with globular protein hydrophilic modified silica gel as a filler is adopted as a stationary phase; and the mobile phase is a mixed solution composed of a mobile phase A and a mobile phase B in a volume ratio of (93-97): (7-3), the mobile phase A is a 0.1-0.2% triethylamine solution, the pH value is adjusted to 5.5-6.5 by using a phosphoric acid solution, and the mobile phase B is acetonitrile. The method for detecting the polymer impurities in the ceftriaxone sodium is high in specificity, good in operability and good in accuracy and precision.

A biomolecular electronic switch includes a first electrical contact, a second electrical contact, a programmable monolayer of either cytochrome c or cytochrome c3 or bovine serum hormone sandwiched between the first and second electrical contacts and a substrate. These switches have high current-carrying capacities and are very fast. It appears that these protein materials can be either metals or semiconductors. Because of the high conductivity and tiny size, these globular proteins can be used to develop cost-effective, miniaturized FEDs, molecular diodes and rectifiers for nanocomputer chips.

The invention provides a detection method for determining polymer impurities in mezlocillin sodium. The detection method employs a high performance liquid chromatography size exclusion chromatography. The chromatography conditions are as follows: a chromatographic column employs hydrophilic silica for globular protein as a stationary phase and 50 mmol of a phosphate buffered solution as a mobile phase; a flow velocity of the mobile phase is 0.5-2.0 mL / min; a detection wavelength is 230-254 nm; a column temperature is a room temperature; a sample volume is 10-80 [mu]L; granularity of the chromatographic column stationary phase is 5 [mu]m, aperture of the chromatographic column stationary phase is 10 nm; the inner diameter of the chromatographic column is 7.8 mm; and the column length is 300 mm. he detection method can perform rapidly qualitative and quantitative determination on the polymer impurities in mezlocillin sodium, simultaneously simplifies operation steps, increases detection precision and shortens detection time.

The present invention relates to systems and methods for the determination of the secondary structure composition of proteins using coherent two-dimensional infrared (2DIR) spectroscopy of backbone amide I vibrations (1580-1720 cm−1). Fractions of α-helix, β-sheet, and unassigned regions in globular proteins were determined by singular value decomposition using basis spectra from sixteen commercially-available proteins with known crystal structures. Preferred methods included removing each protein from the set and comparing the predicted composition against the crystal structure. The root-mean-squared (RMS) errors of the predicted secondary structure compositions were found to be 7.9% for α-helix, 5.5% for β-sheet, and 7.6% for unassigned regions. The structure analysis can also be performed using one-dimensional absorption spectra and the RMS errors are compared with those obtained from 2DIR.

The invention relates to a sterilized liquid or semi-solid acid enteral composition comprising per 100 ml 9 to 20 g of non-hydrolyzed globular proteins, fat and at least 100 mg of divalent metal cations and having a pH ranging between 3 and 5. The invention further relates to a method for preparing a composition according to the invention, comprising a step wherein at least the non-hydrolyzed globular proteins are subjected to a direct steam injection (DSI) at specific holding values, such as a holding temperature of 100 to 140° C. during a holding time of about 0.5 to 10 seconds, followed by a homogenization step and a sterilization step The composition according to the invention has a reduced astringency and can be used for medical purposes, such as for stimulating muscle protein synthesis in a mammal, in particular for treating sarcopenia, and for specific groups of people, such as elderly and sportsman.

A biomolecular electronic switch includes a first electrical contact, a second electrical contact, a programmable monolayer of either cytochrome c or cytochrome c3 or bovine serum hormone sandwiched between the first and second electrical contacts and a substrate. These switches have high current-carrying capacities and are very fast. It appears that these protein materials can be either metals or semiconductors. Because of the high conductivity and tiny size, these globular proteins can be used to develop cost-effective, miniaturized FEDs, molecular diodes and rectifiers for nanocomputer chips.

The invention discloses an HPLC detection method for high-molecular impurities in cefepime and a preparation thereof. The method comprises the steps of separating and measuring polymer impurities in the cefepime and the preparation thereof by using a high performance liquid chromatograph and an isocratic elution method, wherein a chromatographic column with the detection wavelength of 254 + / -2nm takes globular protein chromatographic hydrophilic silica gel as a filler, and a mixed solution consisting of a phosphate buffer solution with the concentration of 0.005 mol / L and the volume percentage of 87.5 to 92.5% and an organic phase with the volume percentage of 7.5 to 12.5% is used as a mobile phase. According to the method, the quality of the high-molecular impurities in cefepime and the preparation thereof can be controlled, and the product quality and medication safety are guaranteed.

A method for changing a globular protein structure into a fibrillar protein structure. The method comprising the steps of providing a globular protein, forming a solution containing the globular protein, adding a detergent to the solution containing the globular protein, applying the solution to a molecular sizing column with a pore size of at least 70 kDa and eluting with a solution containing detergent. A method for changing an unfolded protein structure into a fibrillar protein structure. The method comprising the steps of providing a globular protein, forming a solution containing the globular protein, adding a urea to the solution to unfold the globular protein, applying the solution to a molecular sizing column and eluting with a solution containing detergent. A method for treating cancer comprising the steps of providing a protein, changing the protein into a fibrillar structure, and administering a therapeutically effective amount of the fibrillar structure protein to a patient in need thereof. A method for producing a vaccine adjuvant or antigen adjuvant comprising the steps of providing a protein, and changing the protein into a fibrillar structure.

The invention provides a surface finishing agent for a textile material. The surface finishing agent is characterized by being prepared from globular protein, a surfactant capable of improving film-forming flexibility, caprolactam, an initiator ethylene acetal capable of reducing reaction activation energy, and water according to proportion, wherein in terms of constituent content for preparing the surface finishing agent, the surface finishing agent comprises 10-20% (solid content, the same as below) of the globular protein, 1-3.5% of the surfactant capable of improving the film-forming flexibility, 1.5-5.5% of the caprolactam, 0.3-1.5% of the initiator capable of reducing the reaction activation energy, 0.7-3% of the ethylene acetal and the balance of water. The surface finishing agent has the following advantages that after the finishing agent is used to carry out surface finishing on the textile materials such as fiber, yarns, threads or fabrics, a finished chemical textile material achieves the characteristic of a natural protein textile material, and therefore, the treated chemical textile material has both the characteristic of the chemical textile material per se and the characteristic of the natural protein textile material, and in addition, the globular protein is readily available and is low in cost.

The invention discloses an HPLC detection method for polymer impurities in flucloxacillin and a preparation thereof. The method comprises the steps of separating and determining the polymer impurities in flucloxacillin and the preparation thereof by using a high performance liquid chromatograph and an isocratic elution method, wherein a chromatographic column with the detection wavelength of 254 nm takes globular protein chromatographic hydrophilic silica gel as a filler, and a mixed solution consisting of a phosphate buffer solution with the concentration of 0.01 mol / L and the volume percentage of 87.5 to 92.5% and an organic phase with the volume percentage of 7.5 to 12.5% is used as a mobile phase. According to the invention, quality control can be performed on the flucloxacillin polymer impurities so as to ensure the product quality and the medication safety.