Collagen peptide composition having good ability to enter the blood and food or beverage containing the same

An object of the present invention is to elucidate a collagen peptide effective for causing dipeptides or tripeptides serving as the active component to enter the blood, and thus to reduce the required intake thereof. According to the present invention, a collagen peptide composition obtained by digesting collagen or gelatin with protease is provided, wherein: (a) the ratio of hydroxyproline to total of amino acid residues at the second position from the N terminus of the peptides in the composition is 2 mol % or more and 20 mol % or less, and the ratio of glycine to total of amino acid residues at the third position from the N terminus of the peptides in the composition is 20 mol % or more and 50 mol % or less; and (b) the average molecular weight is 500 or more and 2000 or less.

Topical Pharmaceutical Foam Composition

A stable topical alcohol-free aerosol foam containing one or more keratolytic agents is provided. The foam-forming formulation is an oil-in-water emulsion which contains one or more hydrofluoroalkane (HFA) propellants and one or more keratolytic agents. The keratolytic agent may be present in either phase of the emulsion or dispersed in the emulsion. The oil phase may consist at least in part of the HFA propellant. The foam is stable on the skin for at least 5 minutes at body temperature and disappears into the skin upon rubbing or after prolonged standing. The formulations may not contain additional co-solvents or non-HFA co-propellants. The formulations demonstrate reduced intensity of the odor and/or color associated with the keratolytic agent(s) as compared to conventional formulations containing keratolytic agents.

Compositions for Relieving the Symptoms of Gluten Sensitivity and Methods of Use Thereof

The disclosure relates to a composition that may be used to prevent the symptoms of non-celiac gluten sensitivity and may include ingredients that degrade or inactivate gluten and other components that may cause these symptoms. 1. A composition for reducing gluten sensitivity , comprising at least three proteases;at least one carbohydrase;at least one probiotic; andwherein said composition relieves symptoms of gluten sensitivity.2. The composition of further comprising ginger and turmeric.3. The composition of wherein said composition relieves the symptoms of non-celiac gluten sensitivity.4Aspergillus oryzaeAspergillus melleus. The composition of wherein said at least three proteases are selected from the group consisting of Protease 3.0 claim 1 , Protease 4.5 claim 1 , Protease 6.0 claim 1 , Papain claim 1 , Bromelain claim 1 , Protease claim 1 , Protease claim 1 , Proteases I-V claim 1 , and DPP IV and combinations thereof.5. The composition of wherein said at least one carbohydrase is selected from the group consisting of lactase claim 1 , α-galactosidase claim 1 , β-glucanase claim 1 , xylanase claim 1 , glucoamylase claim 1 , amylase claim 1 , hemicellulase claim 1 , invertase and pectinase and combinations thereof.6Lactococcus lactisLactococcus cremoris.. The composition of wherein said at least one probiotic is selected from the group consisting of and7. The composition of wherein said composition prevents the symptoms of non-celiac gluten sensitivity where said symptoms are selected from the group consisting of abdominal pain claim 1 , cramping claim 1 , bloating/distention claim 1 , diarrhea claim 1 , constipation and fatigue and combinations thereof.8. The composition of wherein said symptoms of non-celiac gluten sensitivity are selected from the group consisting of abdominal pain claim 7 , bloating claim 7 , changes in bowel habits and fatigue and combinations thereof.9. The composition of wherein said composition reduces the concentration of gluten to ...

ULTRAPURE HYPOALLERGENIC SOLUTIONS OF SACROSIDASE

One aspect provides an ultrapure, hypoallergenic sacrosidase. Another aspect provides a solution of sacrosidase in about 1:1 glycerol/water having an enzymatic activity of at least about 7500 IU/mL and a residual papain concentration that does not include an allergic reaction in a human patient when given a dose of about 2.0 mL/day. 1. A protein composition consisting essentially of sacrosidase having a band volume ratio of sacrosidase to other proteins comprising papain of at least about 35:1 by SDS-PAGE of about 20 μg of said composition , wherein the primary structure of the sacrosidase is a 513 amino acid polypeptide that is glycosylated.25. The protein composition of claim , wherein the band volume ratio is about 35-55:1.35. The protein composition of claim that is not produced by chromatographic purification of the sacrosidase. This application is a continuation and claims the benefit of priority of U.S. patent application Ser. No. 14/828,006, filed on Aug. 17, 2015 which claims the benefit of priority of U.S. patent application Ser. No. 14/175,263, filed on Feb. 7, 2014, which is incorporated by reference herein in its entirety.Congenital sucrose-isomaltase deficiency (CSID) is a chronic, autosomal recessive, inherited, phenotypically heterogenous disease with variable enzyme activity. CSID is usually characterized by a subject having complete or almost complete lack of endogenous human sucrase activity, along with a very marked reduction in isomaltase activity, a moderate decrease in maltase activity, and the subject can have normal or abnormal lactase levels.The human enzyme sucrase-isomaltase is naturally produced in the brush border of the small intestine, primarily the distal duodenum and jejunum. The natural human enzyme hydrolyzes the disaccharide sucrose into its component monosaccharides, glucose and fructose. Isomaltase breaks down disaccharides from starch into simple sugars.In the absence of endogenous human sucrase-isomaltase enzyme, as in CSID, ...

DISSOLVABLE GEL-FORMING FILM FOR DELIVERY OF ACTIVE AGENTS

Disclosed is a dissolvable, gel-forming film, and methods for its use, comprising a water-soluble cellulose ether, a hydrophilic rheological modifying agent, and an active proteolytic enzyme or other drug substance. The gel-forming film has a water content of less than 15% w/w and is capable of forming a hydrogel when contacted with water or other aqueous medium. The disclosed films achieve delivery of stable proteolytic enzymes to the desired site of action in a manner that provides uniform delivery of the enzymes. 1. A dissolvable , gel-forming film comprising:(a) a water-soluble cellulose ether;(b) a hydrophilic rheological modifying agent; and(c) a proteolytic enzyme,wherein the dissolvable, gel-forming film has a water content of less than 15% w/w, and the dissolvable, gel-forming film is capable of forming a hydrogel when contacted with water or other aqueous medium.2. The dissolvable claim 1 , gel-forming film of claim 1 , wherein the proteolytic enzyme is in crystalline form.32. The dissolvable claims 1 , gel-forming film of any of - claims 1 , wherein the hydrogel that is formed has a viscosity of 1 claims 1 ,000 to 100 claims 1 ,000 cps claims 1 , as measured using a Brookfield RV Model Viscometer using small sample adapter with spindle #SC4-14 and chamber #SC4-6R claims 1 , at 10 rpm at room temperature claims 1 , reading taken at 1 minute.43. The dissolvable claims 1 , gel-forming film of any of - claims 1 , wherein the proteolytic enzyme is themolysin claims 1 , collagenase claims 1 , or papain.5. The dissolvable claim 4 , gel-forming film of claim 4 , wherein the proteolytic enzyme is thermolysin.65. The dissolvable claims 1 , gel-forming film of any of - claims 1 , wherein the thickness of the film ranges from 10 to 1000 μm.76. The dissolvable claims 1 , gel-forming film of any of - claims 1 , wherein the film is capable of dissolving in water at a rate from 100 to 0.1 mg/min.8. The dissolvable claim 7 , gel-forming film of claim 7 , wherein the film ...

ENZYMATIC DEBRIDEMENT THERAPY FOR ABNORMAL CELL PROLIFERATION

Compositions and methods are provided to destroy internal cancerous lesions selectively by the administration of a combination of a debridement protease enzyme and a denaturant of cell structural proteins and or cell adhesion proteins. 1. A method for the treatment of a neoplasm , comprising administering to a patient in need thereof a treatment effective amount of a composition consisting essentially of one or more debridement enzyme and one or more denaturant , wherein the neoplasm is not a disorder of the skin.2. The method of wherein the debridement enzyme is selected from the group consisting of a plasma enzyme claim 1 , a pancreatic enzyme claim 1 , a cysteine protease claim 1 , a serine protease claim 1 , and a metallopeptidase.3. The method of wherein the debridement enzyme is selected from the group consisting of fibrinolysin claim 1 , desoxyribonuclease claim 1 , trypsin claim 1 , chymotrypsin claim 1 , krillase claim 1 , bromelain claim 1 , papain claim 1 , ficin claim 1 , subtilisins claim 1 , proteinase K claim 1 , collagenase claim 1 , vibriolysin claim 1 , thermolysin claim 1 , streptokinase and streptodomase.4. The method of wherein the debridement enzyme is papain.5. The method of wherein the debridement enzyme is administered in a dose in the range 1×10to 1×10USP per gram.6. The method of wherein the debridement enzyme is administered in a dose of about 1.1×10USP per gram.7. The method of wherein the denaturant is selected from the group consisting of urea claim 1 , lactic acid claim 1 , citric acid claim 1 , an aliphatic alcohol claim 1 , β-mercaptoethanol claim 1 , a detergent claim 1 , sodium dodecyl sulfate claim 1 , formaldehyde claim 1 , acetone claim 1 , acetonitrile claim 1 , dimethylsulfoxide claim 1 , dimethylformamide claim 1 , propylene carbonate claim 1 , ethylene carbonate; a metal scavenger; crown ethers; a crown amine; a polyether; polyethyleneoxide; a polyamine; polyethyleneamine; cryptands; ethylenediaminetetraacetic acid or its ...

DETERMINING THE CONDITION OF A WOUND

A product for monitoring the condition of the wound comprising a biologically inert matrix which absorbs wound exudate and one or more reagents on or in the matrix for measuring one or more markers comprised within the wound exudate. A change in the one or more reagents caused by the one or more markers comprised within the wound exudate provides a visual indication of an alteration in the condition of the wound. Companion wound dressings, kits and methods are also provided. 2. The product according to wherein the one or more reagents comprise a complete test unit integrated on or in the matrix.3. The product according to wherein the one or more reagents form a discrete reaction zone on or within the matrix.4. The product according to wherein the alteration is a deterioration.5. The product according to wherein the matrix is able to absorb and retain a volume of wound exudate sufficient for further analysis of the wound exudate.6. The product according to wherein the matrix has the capacity to absorb a volume of at least 0.2 ml wound exudate.7. The product according to wherein the matrix is dimensioned to facilitate positioning between a wound dressing and the wound.8. The product according to wherein the matrix comprises:(i) a first matrix portion comprising one or more reagents on or in the matrix portion for measuring one or more markers comprised within the wound exudate; and(ii) a second matrix portion which is able to absorb and retain a volume of wound exudate sufficient for further analysis of the wound exudate.9. The product according to wherein:(a) the two matrix portions are laminated together; or(b) the two matrix portions are separate, independent components.10. The product according to wherein the surface of the first matrix portion that is not in contact with the second matrix portion is coated or surrounded by a transparent protective layer.11. The product according to wherein the matrix does not measurably alter the condition of the exudate or its ...

Method of Treating and Diagnosing Parkinson's Disease and Related Dysautonomic Disorders

A method for treating a Parkinson's patient with digestive/pancreatic enzymes involves administering an effective amount of digestive/pancreatic enzymes to an individual having the disorder in order to improve a symptom of the disorder. In addition, a method is provided for determining whether an individual has, or may develop, Parkinson's disease or related dysautonomic disorders and for determining whether an individual will benefit from the administration of pancreatic/digestive enzymes to treat the dysautonomic disorder. 1. A pharmaceutical preparation to treat a dysautonomic disorder in an individual comprising a therapeutically effective amount of digestive enzymes.2. The pharmaceutical preparation of claim 1 , wherein the dysautonomic disorder is Parkinson's disease.3. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is selected from the group consisting of: amylase claim 1 , lipase claim 1 , protease claim 1 , and a combination thereof.4. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is further selected from the group consisting of: chymotrypsin claim 1 , trypsin claim 1 , pancreatin claim 1 , papaya claim 1 , papain claim 1 , and a combination thereof.5. The pharmaceutical preparation of claim 1 , wherein the enzymes are derived from a source selected from the group consisting of animal enzymes claim 1 , plant enzymes claim 1 , synthetic enzymes claim 1 , and a combination thereof.6. The pharmaceutical preparation of wherein the preparation is manufactured using a technology selected from the group consisting of Prosolv technology claim 1 , enteric coating claim 1 , lipid encapsulation claim 1 , direct compression claim 1 , dry granulation claim 1 , wet granulation claim 1 , and a combination thereof.7. The pharmaceutical preparation of claim 1 , wherein the preparation is administered orally via a dosage formulation selected from the group consisting of: pills claim 1 , tablets claim 1 , capsules claim 1 , ...

LIPOSOMAL NUTRACEUTICAL COMPOSITIONS AND METHODS OF MAKING THE SAME

Disclosed are liposomal supplement compositions and methods of formulating the same. A liposomal composition includes a nutraceutical compound such as cannabidiol (CBD), a proteolytic enzyme component such as papain and/or bromelain, and a phytochemical component such as piceatannol. These components are encapsulated within liposomes for enhanced bioavailability and effectiveness. 1. A method of forming a liposomal composition comprising liposomes and a target compound encapsulated by the liposomes , the method comprising:mixing oil-soluble ingredients and a liposome subunit component into an oil carrier;homogenizing the oil-soluble ingredients, liposome subunit component, and the oil carrier to form an oil-based suspension;mixing water-soluble ingredients and a surfactant into an aqueous carrier;mixing the water-soluble ingredients with the surfactant and the aqueous carrier to form an aqueous suspension;mixing the homogenized oil-based suspension with the homogenized aqueous suspension to form a dual suspension comprising a suspension of liposomal oil droplets and a suspension of droplets containing the target compound; andcooling the suspension to allow liposomes to encapsulate the target compound and form the liposomal composition.2. The method of claim 1 , wherein the method omits the addition of polyethylene glycol (PEG).3. The method of claim 1 , wherein the method omits the addition of alcohol.4. The method of claim 1 , wherein the oil carrier includes medium chain triglyceride (MCT) oil.5. The method of claim 1 , wherein the oil-soluble ingredients comprise one or more plant essential oils as a preservative.6. The method of claim 5 , wherein the preservatives include citrus oil claim 5 , oregano oil claim 5 , or both.7. The method of claim 1 , wherein the liposome subunit component includes phosphatidylcholine.8. The method of claim 1 , wherein the surfactant includes a polyethoxylated oil.9. The method of claim 1 , wherein cooling is carried out for about ...

REDUCED-PRESSURE TREATMENT SYSTEMS AND METHODS EMPLOYING DEBRIDEMENT MECHANISMS

Reduced-pressure treatment systems and methods are disclosed that employ debridement mechanisms to remove unwanted tissue. In one instance, a reduced-pressure treatment system for treating a tissue site on a patient includes a manifold member for distributing reduced pressure to the tissue site, a support member for disposing proximate the tissue site and the manifold, and a debridement mechanism coupled to the support member. The debridement mechanism is for debriding the tissue site. The system further includes a sealing drape for placing over the tissue site and manifold member. The sealing drape is operable to form a fluid seal over the tissue site and manifold member. The system also includes a reduced-pressure subsystem for delivering a reduced pressure to the sealing drape. The system may further include a chemical-debridement subsystem. Other systems, manifolds, and methods are disclosed. 119.-. (canceled)20. A method for treating a tissue site on a patient , the method comprising:placing a manifold member adapted to contract in response to application of reduce pressure proximate the tissue site, wherein the manifold member comprises a support member and a debridement arm having a proximal end and a distal end, the proximal end operatively coupled to the support member and the distal end having a face including an edge to debride the tissue site in response to contraction of the manifold member when induced by the application of reduced pressure;disposing a sealing drape over the manifold member and the patient's epidermis;forming a fluid seal between the sealing drape and the patient's epidermis to form a fluid seal over the tissue site and the manifold member; andproviding a reduced pressure to the manifold member whereby the debridement arm is deformable to drive the edge of the face against the tissue site in response to contraction of the manifold member.21. The method of claim 20 , further comprising introducing a debriding chemical to the tissue site ...

METHOD FOR PREPARING BROCCOLI PROTEIN PEPTIDE, BROCCOLI PROTEIN PEPTIDE PREPARED THEREFROM AND USE THEREOF

Provided is a method for preparing a broccoli protein peptide. The method uses a broccoli protein as the raw material, and obtains a broccoli protein peptide powder through the steps of preprocessing, enzymatic hydrolysis, terminating enzymatic hydrolysis, separation, and drying and the like. Also provided is the use of the prepared broccoli protein peptide in resisting oxidation, reducing cholesterol and lowering blood lipids. 112-. (canceled)13. A method for preparing a broccoli protein peptide , the method comprising:(a) adding water, anhydrous sodium sulfite, and EDTA to a raw material broccoli protein thereby making a predigestion mixture,wherein the weight of the water is 4 to 8 times that of raw material broccoli protein, the EDTA has a mass/volume ratio of 0.02-0.05 g/L, and the anhydrous sodium sulfite has a mass/volume ratio of 0.05-0.1 g/L;(b) digesting the predigestion mixture for 3-4 hours at a temperature with an enzyme selected from the group consisting of neutral protease, papain, alkaline protease, trypsin, pepsin, bromelain and compound protease thereby forming a digested mixture;(c) terminating the digestion by heating the digested mixture to from 80-90° C. for from 5-15 minutes;(d) optionally, centrifuging or filtering the mixture from (c);(e) filtering the liquid from (c) or (d) with a membrane having a pore size of 100 to 500 nm;(f) optionally, debittering the mixture from (e) by treating with active carbon or clay; and(g) concentrating and/or drying the mixture from (e) or (f), thereby obtaining the broccoli protein peptide.14. The method of claim 13 , wherein the enzyme is selected from trypsin and neutral protease claim 13 , or alkaline protease and papain claim 13 , or alkaline protease and neutral protease.151. A broccoli protein peptide prepared according to the method of claim .16. A method of antioxidizing claim 15 , lowering cholesterol or lowering blood lipid claim 15 , comprising administering the broccoli protein peptide according ...

CANNABINOID COMPOSITION AND METHOD OF SUBLINGUAL, BUCCAL AND ORAL MUCOSA DELIVERY

A formulation includes a cannabinoid extract that is pharmaceutically effective by systemic delivery via a recipient's oral mucosal lining. The method of delivery avoids the digestive tract processing and liver metabolizing of the active ingredients of the formulation, whereby lower doses cause a desired therapeutic effect or other intended effect. Variations of the formulation include a cannabinoid extract and one or more of pregelatinized tapioca starch polymethylsilsesquioxane, bromelain, volume Fenugreek gum, vitamin B12, luo han guo fruit extract, mannitol, microcrystalline cellulose, sodium alginate, gellan gum, menthol Natural peppermint flavor or oil, Grapefruit flavored powder or oil, magnesium stearate and/or citric acid. The cannabinoid extract may include Tetrahydrocannabinol, tetrahydrocannabinolic acid, Cannabidiol, Cannabidiol acid, and/or other cannabinoid sourced from a cannabis sativa plant. The formulation includes at least one cannabinoid in a volume and measure that is pharmaceutically effective and/or effectual in achieving an intended systemic state or response of the recipient. 121.-. (canceled)22. A unit dose sublingual composition , comprising:(a) an extract of a cannabinoid containing Cannabis plant material, said extract comprising (i) one or more cannabinoid active agent(s) or (ii) a combination of said extract and one or more additional cannabinoid active agent(s), said additional cannabinoid active agent(s) selected from the group consisting of partially or completely purified cannabinoid compounds, synthetic cannabinoid compounds, and mixtures thereof;(b) an amount per unit dose of pregelatinized tapioca starch, wherein the amount of pregelatinized tapioca starch is 0.25 mg-2.0 mg per unit dose; and(c) an amount per unit dose of bromelain, wherein the amount of bromelain per unit dose is 0.05 mg-3.0 mg.23. The unit dose sublingual composition of claim 22 , wherein:i) the amount of pregelatinized tapioca starch is 0.75 mg per unit dose ...

CANNABINOID EMULSION PRODUCT AND PROCESS FOR MAKING THE SAME

A dry consumable preparation and related methods are disclosed. The preparation has a bulking agent, and a cannabinoid and/or a cannabinoid extract containing one or more cannabinoids plated onto the bulking agent. The preparation also has an effervescence agent. The effervescence agent has sodium bicarbonate, potassium bicarbonate, and at least one acid, the at least one acid having at least one of citric acid, tartaric acid, or malic acid. The effervescence agent further has a ratio of sodium bicarbonate to potassium bicarbonate to the acid(s) that creates a chemical pH buffering system at a targeted pH range when the dry consumable preparation is added to a targeted amount of water. 1. A dry consumable preparation comprising:a bulking agent;at least one of a cannabinoid or a cannabinoid extract containing one or more cannabinoids, the at least one of the cannabinoid or the cannabinoid extract containing one or more cannabinoids plated onto the bulking agent;an effervescence agent, the effervescence agent having sodium bicarbonate, potassium bicarbonate, and at least one acid, the at least one acid having at least one of citric acid, tartaric acid, or malic acid, the effervescence agent further having a ratio of the sodium bicarbonate to the potassium bicarbonate to the at least one acid; whereinthe ratio is configured to create a chemical pH buffering system at a targeted pH range when the dry consumable preparation is added to a targeted amount of water.2. The preparation of claim 1 , wherein:the targeted pH range is between 2 and 6.3. The preparation of claim 2 , wherein:the bulking agent comprises sucrose and fructose; and wherein a ratio of the sucrose to the fructose is about 1:1.4. The preparation of claim 3 , wherein:the preparation comprises at least 30% by weight sucrose; andthe preparation comprises at least 30% by weight fructose.5. The preparation of claim 1 , wherein:the preparation is a pressed tablet or a powder encapsulated in a water-dissolvable ...

COMPOSITION AND METHOD OF PREPARATION OF PROTEASE MICROPARTICULATE SLOW RELEASE PREPARATION

Compositions containing microparticles loaded with one or protease enzymes and optionally auxiliary therapeutic agents and methods of treating conditions such as keloids therewith are disclosed. The biodegradable polymer and the protease enzyme therein form a controlled release matrix for extended release of the enzyme after administration to a mammal in need thereof. 1. A composition , comprising a plurality of biodegradable polymer microparticles comprising a protease enzyme therein , the biodegradable polymer and the protease enzyme forming a controlled release matrix for extended release of the enzyme; wherein the plurality of microparticles include a mixture of microparticles containing different proteases.2. The composition of claim 1 , wherein the protease is selected from the group consisting of collagenase claim 1 , papain claim 1 , elastase and mixtures thereof.3. The composition of claim 1 , wherein the biodegradable polymer wherein the biodegradable polymer is selected from the group consisting of polylactic acid (PLA) claim 1 , polylactic co-glycolic acid (PLGA) claim 1 , polyglycolic acid (PGA) polylactones claim 1 , polyorthocarbonate claim 1 , polyhydroxybutyrate claim 1 , polyalkylcyanoacrylates claim 1 , polyanhydrides claim 1 , polyorthoesters claim 1 , polyester claim 1 , polyimide claim 1 , polyglycolides (PGA) claim 1 , polyorthoester claim 1 , polyacetates claim 1 , polystyrene claim 1 , polycarbonates claim 1 , polysaccharides claim 1 , polycaprolactone claim 1 , L-polylactides claim 1 , block co-polymers of polyesters and linear or star-polyethyleneglycol claim 1 , poly-beta-hydroxybutyrate claim 1 , beta-hydroxyvalerate-copolymers claim 1 , polyaminoacids claim 1 , hydrophobized hyaluronic acid claim 1 , dextrans claim 1 , starches claim 1 , methyl methacrylate claim 1 , acrylamide claim 1 , bisacrylamide claim 1 , albumin claim 1 , cellulose claim 1 , cellulose-based polymers claim 1 , chitosan claim 1 , collagen claim 1 , gelatin claim 1 ...

BMP Peptides & Methods of Use

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition.

PROTEOLYTIC ENZYME COMPOSITION

The present invention provides a novel proteolytic enzyme composition more particularly an orally administered proteolytic enzyme composition comprising of one or more acid proteases, one or more alkaline protease and one or more plant proteases. More particularly, the composition comprises of microbial (fungal, bacterial or other microbes) protease enzymes, proteases from plant and animals proteases thereof. 1. A proteolytic enzyme composition comprising of:a) one or more of an acid protease;b) one or more of an alkaline protease;c) one or more of a plant protease.2. The proteolytic enzyme composition according to claim 1 , wherein the proteolytic enzyme composition comprises of:a) an acid protease;b) an alkaline protease;c) two plant proteases.3. The proteolytic enzyme composition according to claim 1 , wherein the proteolytic composition comprises:a) acid protease enzyme selected from fungal enzyme or bacterial enzyme or a combination of both fungal enzyme and bacterial enzyme.b) alkaline protease enzyme selected from fungal enzyme or bacterial enzyme or a combination of both fungal enzyme and bacterial enzyme.c) plant protease enzyme selected from kiwi, papaya, fig, mango and pineapple plants.4. The proteolytic enzyme composition according to claim 3 , wherein the proteolytic composition comprises:{'i': Rhizopus oryzae', 'Rhizopus niveus', 'Aspergillus niger', 'Aspergillus oryzae', 'Bacillus subtilis', 'Bacillus licheniformis;, 'a) acid protease fungal enzyme selected from the group consisting of or or or or the acid protease bacterial enzyme selected from the group consisting of or'}{'i': Rhizopus niveus', 'Rhizopus oryzae', 'Aspergillus niger', 'Aspergillus oryzae', 'Bacillus subtilis', 'Bacillus licheniformis;, 'b) alkaline protease fungal enzyme selected from the group consisting of or or or or alkaline protease bacterial enzyme is selected from the group consisting of or'}c) plant proteases selected from actinidin, papain, ficin and bromelain.5. The ...

Methods and Compositions for the Treatment of Symptoms of Prion Diseases

A therapeutic composition for the treatment of the symptoms of prion diseases and the method for preparing the therapeutic agents is disclosed. The therapeutic composition is a stable pharmaceutical composition comprising one or more digestive and/or pancreatic enzymes. The therapeutic composition may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic composition may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using fecal chymotrypsin level as a biomarker for the presence of a prion disease, or the likelihood of an individual to develop a prion disease is disclosed. 1. A method for treating a prion disease in an individual in need thereof , comprising administering to the individual a therapeutically effective amount of a pharmaceutical composition that comprises digestive enzymes , wherein the digestive enzymes comprise a protease , an amylase and a lipase.2. The method of claim 1 , wherein the pharmaceutical composition further comprises one or more enzymes selected from the group consisting of a cellulase claim 1 , a sucrase claim 1 , a maltase claim 1 , a papaya claim 1 , and a papain.3. The method of claim 1 , wherein the digestive enzymes comprise pancreatic enzymes.4. The method of claim 1 , wherein the digestive enzymes comprise a mixture of proteases comprising chymotrypsin and trypsin.5. The method of claim 1 , wherein the digestive enzymes are claim 1 , independently claim 1 , animal enzymes claim 1 , microbial enzymes claim 1 , plant enzymes claim 1 , or synthetically prepared enzymes.6. The method of claim 5 , wherein the digestive enzymes are animal enzymes derived from a pig.7. The method of claim 2 , wherein the pharmaceutical composition comprises at least one amylase claim 2 , a mixture of proteases comprising chymotrypsin and trypsin claim 2 , at least one lipase claim 2 , and papain.8. (canceled)9. (canceled)10. The method of claim 1 , wherein a ...

CHROMATOGRAPHIC PURIFICATION OF AT LEAST ONE ENZYME SELECTED FROM A GROUP INCLUDING COLLAGENASE TYPE I, COLLAGENASE TYPE II, NEUTRAL PROTEASE AND CLOSTRIPAIN

The present invention relates to a method for purifying at least one enzyme selected from the group consisting of collagenase type I, collagenase type II, neutral protease and clostripain from a mixture of substances, comprising as a method step at least one hydrophobic interaction chromatography, characterized in that, in the hydrophobic interaction chromatography, the stationary phase comprises a material selected from the group consisting of polypropylene glycol and butyl sepharose. The present invention further relates to the use of an enzyme thus purified for pharmaceutical, cosmetic and/or biochemical purposes.

MIXTURE TO INCREASE THE EFFECTIVENESS OF ANTISEPTICS AND/OR DISINFECTANTS, AN AGENT CONTAINING THE MIXTURE, AND THE USE OF THIS MIXTURE

The invention relates to the increase (improvement) of the effectiveness of antiseptics and/or disinfectants administered in a mixture with hydrolytic or proteolytic enzymes to a mucous membrane, a skin of a mammal or inanimate surfaces in the form of a solution, gel, paste, capsules or other as an agent. The use of the mixture is also stated. 115-. (canceled)16. An antiseptic or a disinfectant composition comprising chlorhexidine digluconate in an amount of 0.001% to 1% by weight and proteolytic or hydrolytic enzyme in an amount of 0.01% to 2% by weight based on the total weight of the composition and further comprising buffered saline and water.17. The antiseptic or a disinfectant composition according to claim 16 , wherein the amount of chlorhexidine digluconate is 0.01% to 0.12% by weight and the amount of proteolytic or hydrolytic enzyme is 0.01% to 0.4% by weight based on the total weight of the composition.18. The antiseptic or a disinfectant composition according to claim 16 , comprising two different enzymes.19. The antiseptic or a disinfectant composition according to claim 18 , wherein the two different enzymes are each a hydrolytic enzyme.20. The antiseptic or a disinfectant composition according to claim 19 , wherein the hydrolytic enzyme is selected from protease claim 19 , lipase or amylase.21. The antiseptic or a disinfectant composition according to claim 16 , comprising two hydrolytic enzymes claim 16 , wherein the two hydrolytic enzymes are both proteases claim 16 , lipases or amylases.22. The antiseptic or a disinfectant composition according to claim 21 , wherein the protease is selected from the group consisting of trypsin claim 21 , chymotrypsin claim 21 , bromelain and papain.23. The antiseptic or a disinfectant composition according to claim 22 , wherein the amount of chlorhexidine digluconate is 0.001% to 1% by weight claim 22 , the amount of trypsin or chymotrypsin is 0.01% to 0.2% by weight and the content of bromelain is 0.01% to 0.4% by ...

ACTIVE PEPTIDE FOR INHIBITING AMPA RECEPTOR AND PREPARATION METHOD AND USE THEREOF

Provided is an active peptide for inhibiting an AMPA receptor and a preparation method and use thereof. The method for preparing the active peptide comprises the following steps: 1) soaking a salmon skin and crushing, adding water and beating, and then adjusting pH to 6.5-7.5; 2) subjecting to a first enzymolysis using a neutral protease; 3) subjecting to a second enzymolysis using papain enzyme and then inactivating enzyme; and 4) centrifuging the enzymatic hydrolysate, and then subjecting the centrifuged supernatant to membrane filtration, concentration and decoloration, to prepare the active peptide. The active peptide contains a tetrapeptide with an amino-acid sequence of Glu-Gly-Ala-Arg. The tetrapeptide has good solubility, can selectively inhibit neuronal synaptic transmission caused by an AMPA receptor, and has a significant antiepileptic effect. 1. A method for preparing an active peptide , comprising the following steps:1) soaking a salmon skin and crushing, adding water and beating, and then adjusting pH to 6.5-7.5, to obtain a slurry;2) subjecting the slurry to a first enzymolysis by using a neutral protease, to obtain a first enzymatic hydrolysate;3) subjecting the first enzymatic hydrolysate to a second enzymolysis by using papain enzyme and then inactivating enzyme, to botain a second enzymatic hydrolysate; and4) centrifuging the second enzymatic hydrolysate, and then subjecting the centrifuged supernatant to membrane filtration, concentration and decoloration, to prepare the active peptide;wherin the active peptide contains a tetrapeptide with an amino-acid sequence of Glu-Gly-Ala-Arg.2. The method according to claim 1 , wherein an alkaline solution with a mass content of 0.1-0.5% is used to soak the salmon skin claim 1 , a mass/volume ratio of the salmon skin to the alkaline solution is controlled to 1:(2-4) claim 1 , and soaking time is 5-20 h.3. The method according to claim 1 , wherein the amount of the neutral protease is 50-500 U/g claim 1 , ...

DENTAL GEL COMPOSITION OF PAPAIN FOR THE ATRAUMATIC TREATMENT OF CARIES AND METHOD OF PREPARING SAME

A papain dental gel composition is disclosed for the atraumatic treatment of caries which comprises papain with a final activity of at least 3,000 U/mg, wherein the papain is bio-encapsulated in a mixture of pH=7 buffer-Cpolyol-pectin-Calkanolamine-nonionic emulsifier, together with pharmaceutically acceptable coloring agents, preservatives and solvents. A method of preparing said papain composition is also disclosed. 1. A dental composition of papain in the form of a gel for the atraumatic treatment of caries comprising papain with a final activity of at least 3 ,000 U/mg , wherein the papain is bio-encapsulated in a mixture of pH=7 buffer-Cpolyol-pectin-Calkanolamine-nonionic emulsifier , together with pharmaceutically acceptable coloring agents , preservatives and solvents.2. The composition according to claim 1 , wherein the pH=7 buffer is selected from the group consisting of: disodium or dipotassium acid phosphate (NaHPO claim 1 , KHPO)/citric acid (CHO) claim 1 , sodium chloride (NaCl)/sodium citrate (CHONa.2HO)/sodium hydroxide (NaOH) claim 1 , sodium or potassium diacid phosphate (NaHPO claim 1 , KHPO)/disodium or dipotassium acid phosphate (NaHPO claim 1 , KHPO) claim 1 , tris-(hydroxymethyl)-aminomethane (TRIS)/hydrochloric acid (HCl).3. The composition according to claim 2 , wherein the pH=7 buffer is KHPO/NaHPO.4. The composition according to claim 1 , wherein the Cpolyol is selected from the group consisting of: 1 claim 1 ,2 claim 1 ,3-propanetriol (glycerin) claim 1 , 1 claim 1 ,2-propanediol (propyleneglycol) claim 1 , 1 claim 1 ,3-butanediol claim 1 , 1 claim 1 ,4-butanediol claim 1 , 1 claim 1 ,3-butenediol claim 1 , 2 claim 1 ,3-butenediol claim 1 , 2 claim 1 ,2-dimethyl-1 claim 1 ,3 propanediol (neopentylglycol) claim 1 , erythritol claim 1 , sorbitol claim 1 , mannitol claim 1 , and mixtures thereof.5. The composition according to claim 4 , wherein the Cpolyol is 1 claim 4 ,2-propanediol (propyleneglycol).6. The composition according to claim 1 ...

COMPOSITION OF NOVEL POWDER FORMULATIONS OF TRANEXAMIC ACID

Powder composition of Tranexamic acid have been provided for the treatment of wound and bleeding. The powder composition may also contain aprotinin and epsilon-aminocaproic acid as active antifibrinolytic agent. The composition may also contain antibiotic(s), anti-inflammatory agent(s), local anesthetic(s) and hydrophilic polymer(s). The powder composition in this patent application is applied to mucosal or non-mucosal surfaces, but it is not for an oral administration. 1) (canceled)2) (canceled)3) (canceled)4) (canceled)5) (canceled)6) (canceled)7) (canceled)8) (canceled)9) (canceled)10) (canceled)11) (canceled)12) (canceled)13) (canceled)14) (canceled)15) (canceled)16) (canceled)17) (canceled)18) (canceled)19) (canceled)20) (canceled)21) A wound-healing powder composition applied locally to mucosal or non-mucosal surfaces of the wound comprising (a) tranexamic acid in an amount from 70.1 wt % to 99.5% wt % , (b) one or more antibiotic in an amount from 1 wt % to 10 wt % , (c) optionally one or more of aprotinin , bromelain , and epsilon-aminocaproic acid in an amount from 1 wt % to 15 wt % , (d) optionally a local anesthetic in an amount from 0.1% to 5% , (e) optionally an anti-inflammatory agent in an amount from 0.1% to 5% , (f) one or more hydrophilic polymer(s) , (g) optionally a cyclodextrin , (h) a preservative , and (I) excipient(s).22) A wound-healing powder composition of wherein one or more antibiotic(s) are selected from the group consisting of penicillins claim 21 , cephalosporins claim 21 , glycopeptides claim 21 , amoniglycosides claim 21 , tetracyclines claim 21 , fluoroquinolones claim 21 , quinolones claim 21 , moxifloxacin claim 21 , mupirocin claim 21 , erythromycin claim 21 , sulfacetamide claim 21 , sulfadiazine claim 21 , mafenide claim 21 , tetracycline claim 21 , bacitracin claim 21 , neomycin claim 21 , vancomycin claim 21 , teicoplanin claim 21 , amikacin claim 21 , tobramycin claim 21 , streptomycin claim 21 , doxycycline claim 21 , ...

Methods and compositions for the treatment of amyloidosis

Methods and compositions for the treatment or prevention of amyloidosis are provided. In some embodiments, the methods comprise administering to the subject a therapeutically effective amount of at least one catabolic enzyme or a biologically active fragment thereof. Such methods and compositions may be employed to reduce, prevent, degrade and/or eliminate amyloid formation in the lysosome and/or extracellularly.

Composition and Uses Thereof

The invention relates to compositions comprising stem bark extract, papain, and extract, and methods of manufacturing same. There are also described methods of treating or preventing a variety of conditions, including treating or preventing elevated blood glucose, pre-diabetes, type 2 diabetes, autoimmune diseases, reducing or decreasing inflammation, treating or preventing diseases characterised by elevated levels of inflammation, and lowering blood cholesterol, said methods comprising administering an effective amount of a composition according to the invention to a subject in need thereof. Uses of the composition of the invention for the manufacture of a medicament for treating or preventing a variety of conditions are also described. 135-. (canceled)36Pinus pinasterAloe vera. An aqueous composition comprising stem bark extract , papain , extract , and an acid , said acid provided to the aqueous composition in an amount and at a concentration effective to adjust the pH of the composition to between about 3.2 and about 4.2.37Aloe veraAloe vera. The composition according to claim 36 , wherein the extract is leaf extract.38. The composition according to claim 36 , wherein the acid is acetic acid.39. The composition according to claim 36 , wherein the composition further comprises honey.40. The composition according to claim 36 , wherein the composition comprises one or more additives selected from the group consisting of: a preservative claim 36 , a flavouring agent claim 36 , a salt claim 36 , and a pigment.41. The composition according to claim 36 , wherein the composition comprises a salt claim 36 , and wherein the salt is sodium chloride.42. The composition according to claim 36 , further comprising an additional component selected from the group consisting of: an omega-3 fatty acid claim 36 , a phytonutrient claim 36 , a source of protein claim 36 , an amino acid claim 36 , an antioxidant claim 36 , a vitamin claim 36 , a mineral claim 36 , a plant extract ...

CELL-TARGETED CYTOTOXIC CONSTRUCTS

Cell-targeted cytotoxic agents, including sortase serine protease constructs, are provided. Such compounds can be used in methods for targeted cell killing such as for treatment cell of proliferative diseases (e.g., cancer). In some aspects, recombinant sortase serine proteases, such as Granzyme B polypeptides, are provided that exhibit improved stability and cell toxicity. 176.-. (canceled)78. The cell-targeted construct of claim 77 , wherein the linking polypeptide comprises LPETG.79. The cell-targeted construct of claim 78 , wherein the linking polypeptide comprises LPETGG.80. The cell-targeted construct of claim 77 , wherein the construct further comprises at least one spacer positioned between the targeting moiety and the polypeptide linker.81. The cell-targeted construct of claim 80 , wherein the construct comprises two spacers.82. The cell-targeted construct of claim 80 , wherein the at least one spacer comprises the sequence G4S (GGGGS; SEQ ID NO: 36).83. The cell-targeted construct of claim 77 , wherein the cytotoxic moiety is an auristatin.84. The cell-targeted construct of claim 77 , wherein the auristatin is monomethylaurostatin E (MMAE).85. The cell-targeted construct of claim 77 , wherein the auristatin comprises a protease-cleavable linker.86. The cell-targeted construct of claim 85 , wherein the protease-cleavable linker is citrulline-valine. The present application is a continuation of U.S. application Ser. No. 15/434,648, filed Feb. 16, 2017, which claims the priority benefit of U.S. Provisional Application No. 62/295,636, filed Feb. 16, 2016, the entire contents of each of which are hereby incorporated by reference.The present invention relates generally to the field of molecular biology and recombinant protein production. More particularly, it concerns the linkage of cytotoxic agents, such as serine protease polypeptides (e.g., granzymes) to cell-targeting moieties.The successful development of targeted therapeutics (e.g., for cancer applications ...

Peptide Pet Food Material Having Anti-Stress Action and Palatability-Increasing Effect

The present invention provides a safe pet food material having an anti-stress action and effect of increasing palatability. Livestock meat or fish meat is treated with a protease such as papain to obtain a pet food material with excellent thermal stability having peptides consisting of 2-10 amino acid residues as a principal active ingredient. A pet food exhibiting an anti-stress action and having high palatability is obtained by blending this material. 1. A method of preparing cat food having anti-stress action and increased palatability , comprising the steps of:performing, using an extruder, extrusion molding of a raw material at 110° C. for 30 seconds to provide an extruded product, wherein the raw material comprises a peptide material consisting of 2-10 amino acid residues and the peptide materials is obtained from treatment of livestock meat of fish meat with a protease; anddrying the extruded product at 140° C. for 15 minutes,wherein the peptide material comprises by weight about 10% of the mixture and at least one peptide having a sequence Val-Glu-Pro-Ser, Ile-Arg-Val-Val-Glu, Val-Gly-Arg, or Glu-Pro-Ala-Val-Lys.2. The method according to claim 1 , wherein the livestock meat or fish meat is chicken meat or bonito meat.3. The method according to claim 1 , wherein the livestock meat or fish meat is bonito meat.4. The method according to claim 1 , wherein the livestock meat or fish meat is treated with a protease in an amount of 0.25-1.50 wt % for one hour at 50° C.5. A method of increasing palatability of cat food claim 1 , comprising the steps of:performing, using an extruder, extrusion molding of a raw material at 110° C. for 30 seconds to provide an extruded product, wherein the raw material comprises a peptide material consisting of 2-10 amino acid residues and the peptide materials is obtained from treatment of livestock meat of fish meat with a protease; anddrying the extruded product at 140° C. for 15 minutes,wherein the peptide material comprises by ...

PRODUCTION OF FC FRAGMENTS

In one aspect, the disclosure provides cells and transgenic non-human mammals for the production of Fc fragments, as well as compositions and uses thereof. 1. A method of producing a fragment crystallizable (Fc) fragment , the method comprisingproviding a transgenic non-human mammal that has been modified to express an antibody comprising an Fc fragment in the mammary gland;harvesting the antibody comprising the Fc fragment from milk produced by the mammary gland of the transgenic mammal; andisolating the Fc fragment from the antibody.2. A method of producing an Fc fragment , the method comprisingproviding a mammary epithelial cell that has been modified to express an antibody comprising an Fc fragment;harvesting the antibody comprising the Fc fragment from the mammary epithelial cell; andisolating the Fc fragment from the antibody.3. A method of producing an Fc fragment , the method comprisingproviding a transgenic non-human mammal that has been modified to express an Fc fragment in the mammary gland;harvesting the Fc fragment from the milk produced by the mammary gland of the transgenic mammal; andisolating the Fc fragment.4. A method of producing an Fc fragment , the method comprisingproviding a mammary epithelial cell that has been modified to express an Fc fragment;harvesting the Fc fragment from the mammary epithelial cell; andisolating the Fc fragment.5. The method of or , wherein isolating the Fc fragment comprises subjecting the antibody sequentially to(a) hydrophobic interaction chromatography; and(b) ultrafiltration.6. The method of or , wherein isolating the Fc fragment comprises subjecting the Fc fragment sequentially to(a) hydrophobic interaction chromatography; and(b) ultrafiltration.7. The method of or , wherein the ultrafiltration is performed in a solution comprising phosphate , NaCl and Tween 80 , wherein the phosphate has a concentration between 10 and 100 mM , the NaCl has a concentration between 100 and 500 mM , and the Tween 80 has a ...

Method for the preparation of low molecular weight porcine lympho-reticular polypeptides and formulations thereof

A method for preparation of low molecular weight porcine lympho-reticular polypeptides. The method comprises the enzymatic hydrolysis of a source of protein, wherein the source of protein comprises a blend of porcine liver and porcine spleen, with a first enzyme having proteolytic activity and a second enzyme having amylase activity.

Novel compositions for the treament of cancer

The present invention relates to novel compositions comprising proteolytic enzymes and fining agents as well as methods for the treatment and/or prevention of cancer using these compositions.

METHOD FOR PREPARING BROCCOLI PROTEIN PEPTIDE, BROCCOLI PROTEIN PEPTIDE PREPARED THEREFROM AND USE THEREOF

Provided is a method for preparing a broccoli protein peptide. The method uses a broccoli protein as the raw material, and obtains a broccoli protein peptide powder through the steps of preprocessing, enzymatic hydrolysis, terminating enzymatic hydrolysis, separation, and drying and the like. Also provided is the use of the prepared broccoli protein peptide in resisting oxidation, reducing cholesterol and lowering blood lipids. 112-. (canceled)13. A method for preparing a broccoli protein peptide , the method comprising:(a) adding water, anhydrous sodium sulfite, and EDTA to a raw material broccoli protein thereby making a predigestion mixture,wherein the weight of the water is 4 to 8 times that of raw material broccoli protein, the EDTA has a mass/volume ratio of 0.02-0.05 g/L, and the anhydrous sodium sulfite has a mass/volume ratio of 0.05-0.1 g/L;(b) digesting the predigestion mixture for 3-4 hours at a temperature with an enzyme selected from the group consisting of neutral protease, papain, alkaline protease, trypsin, pepsin, bromelain and compound protease thereby forming a digested mixture;(c) terminating the digestion by heating the digested mixture to from 80-90° C. for from 5-15 minutes;(d) optionally, centrifuging or filtering the mixture from (c);(e) filtering the liquid from (c) or (d) with a membrane having a pore size of 100 to 500 nm;(f) optionally, debittering the mixture from (e) by treating with active carbon or clay; and(g) concentrating and/or drying the mixture from (e) or (f), thereby obtaining the broccoli protein peptide.14. The method of claim 13 , wherein the enzyme is selected from trypsin and neutral protease claim 13 , or alkaline protease and papain claim 13 , or alkaline protease and neutral protease.151. A broccoli protein peptide prepared according to the method of claim .16. A method of antioxidizing claim 15 , lowering cholesterol or lowering blood lipid claim 15 , comprising administering the broccoli protein peptide according ...

COMPOSITION AND USES THEREOF

The invention relates to compositions comprising stem bark extract, papain, and extract, and methods of manufacturing same. There are also described methods of treating or preventing a variety of conditions, including treating or preventing elevated blood glucose, pre-diabetes, type 2 diabetes, autoimmune diseases, reducing or decreasing inflammation, treating or preventing diseases characterised by elevated levels of inflammation, and lowering blood cholesterol, said methods comprising administering an effective amount of a composition according to the invention to a subject in need thereof. Uses of the composition of the invention for the manufacture of a medicament for treating or preventing a variety of conditions are also described. 1Pinus pinasterAloe vera. A composition comprising stem bark extract , papain , and extract.2Pinus pinasterAloe vera. A composition comprising a therapeutically effective amount of stem bark extract , papain , and extract.3Aloe veraAloe vera. The composition according to claim 1 , wherein the extract is leaf extract.4Pinus pinasterPinus pinaster. The composition according to claim 2 , wherein the therapeutically effective amount of stem bark extract corresponds to a daily adult human dosage of from about 60 mg to about 1500 mg stem bark extract;the therapeutically effective amount of papain corresponds to a daily adult human dosage of from about 30 mg to about 1200 mg papain; and{'i': Aloe vera', 'Aloe vera, 'the therapeutically effective amount of extract corresponds to a daily adult human dosage of from about 15 mg to about 600 mg extract.'}5Pinus pinaster. The composition according to any one of claim 2 , wherein the therapeutically effective amount of stem bark extract corresponds to a daily adult human dosage of about 260 mg;the therapeutically effective amount of papain corresponds to a daily adult human dosage of about 240 mg; and{'i': 'Aloe vera', 'the therapeutically effective amount of extract corresponds to a daily adult ...

Method of Treating Proteinuria in Pregnancy

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed. 1. A method for treating an individual exhibiting one or more symptoms of preeclampsia , the method comprising administering a therapeutically effective amount of digestive enzymes to the individual.2. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is selected from the group consisting of: amylase claim 1 , lipase claim 1 , protease claim 1 , and a combination thereof.3. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is further selected from the group consisting of: chymotrypsin claim 1 , trypsin claim 1 , pancreatin claim 1 , papaya claim 1 , papain claim 1 , and a combination thereof.4. The pharmaceutical preparation of claim 1 , wherein the enzymes are derived from a source selected from the group consisting of animal enzymes claim 1 , plant enzymes claim 1 , synthetic enzymes claim 1 , and a combination thereof.5. The pharmaceutical preparation of wherein the preparation is manufactured using a technology selected from the group consisting of enteric coating claim 1 , lipid encapsulation claim 1 , direct compression claim 1 , dry granulation claim 1 , wet granulation claim 1 , and a combination thereof.6. The pharmaceutical preparation of claim 1 , wherein the preparation is administered orally via a dosage formulation ...

Novel Pharmaceutical Preparation for Preeclampsia, Eclampsia, and Toxemia and Their Related Symptoms and Related Disorders of Pregnancy

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed. 1. A method for treating an individual exhibiting one or more symptoms of pregnancy-induced hypertension , the method comprising administering a therapeutically effective amount of a pharmaceutical preparation comprising digestive enzymes to the individual , wherein the digestive enzymes comprise an amylase , a lipase , a protease , or a combination thereof , whereby pregnancy-induced hypertension is treated.2. The method of claim 1 , wherein the protease comprises chymotrypsin or trypsin.3. The method of claim 1 , wherein the digestive enzymes are provided as pancreatin.4. The method of claim 1 , wherein the digestive enzymes are obtained from a source selected from the group consisting of animal enzymes claim 1 , plant enzymes claim 1 , synthetic enzymes claim 1 , and a combination thereof.5. The method of wherein the pharmaceutical preparation is manufactured using a technology selected from the group consisting of enteric coating claim 1 , lipid encapsulation claim 1 , direct compression claim 1 , dry granulation claim 1 , wet granulation claim 1 , and a combination thereof.6. The method of claim 1 , wherein the pharmaceutical preparation is administered orally via a dosage formulation selected from the group consisting of: pills claim 1 , tablets claim 1 , capsules claim 1 ...

Enzyme Preparation for Modifying Food Material

An enzyme preparation for suppressing bitterness of food contains phospholipase and, if necessary, further contains protease. A method for suppressing bitterness of food includes treating a food material with a food bitterness suppressor containing the enzyme preparation. A method for producing a processed food product includes treating a food material with a food bitterness suppressor containing the enzyme preparation. Food treated with the enzyme preparation for suppressing bitterness of food tastes less bitter even when cooked after long-term preservation. Furthermore, an enzyme preparation for suppressing bitterness of food and for, if necessary, tenderizing food can be provided. 1. An enzyme preparation for suppressing bitterness of food , comprising phospholipase.2. The enzyme preparation of claim 1 , further comprising protease.3. The enzyme preparation of claim 1 , wherein the food is edible meat.4. The enzyme preparation of claim 1 , wherein the bitterness is derived from peptide generated due to an action of protease on a material of the food.5. The enzyme preparation of claim 1 , wherein the phospholipase is phospholipase D.6. The enzyme preparation of claim 1 , wherein the phospholipase is contained in a proportion of 60 to 1500 units (U) with respect to 100 units (U) of the protease.7. A method for suppressing bitterness of food claim 1 , which comprises treating a food material with a food bitterness suppressor containing the enzyme preparation of .8. A method for producing a processed food product claim 1 , which comprises treating a food material with a food bitterness suppressor containing the enzyme preparation of .9. A processed food product claim 1 , comprising a food material treated with a food bitterness suppressor containing the enzyme preparation of .10. The enzyme preparation of claim 2 , wherein the food is edible meat.11. The enzyme preparation of claim 2 , wherein the bitterness is derived from peptide generated due to an action of ...

Use of Proteases for Gluten Intolerance

The present technology relates to an enzyme composition. The enzyme composition may be used to treat gluten intolerant subjects, including suffering from non-Celiac gluten intolerance and/or non-Celiac gluten sensitivity. The enzyme composition may also be used to reduce gluten exposure in certain individuals. For example, the enzyme composition may also be used as a prophylactic to reduce exposure to gluten oligopeptides. 1. A method of treating gluten intolerance or reducing gluten exposure in a human subject comprising:{'i': 'Aspergillus oryzae', 'providing the subject with a therapeutically effective amount of an enzyme cocktail comprising a gluten degrading enzyme preparation isolated from with specificity for peptide substrate leucyl-glycyl-glycine (GDEP-LGG) and papain,'}wherein the enzyme cocktail degrades a gluten oligopeptide of SEQ ID NO:1 at acidic conditions.2. The method of claim 1 , wherein the enzyme cocktail further comprises a semi-alkali protease.3. The method of claim 1 , wherein the enzyme cocktail is formulated in a pharmaceutically acceptable excipient.4. The method of claim 1 , wherein the enzyme cocktail is formulated for oral delivery.5. The method of claim 2 , wherein the semi-alkali protease is Protease P.6. The method of claim 1 , wherein the papain has been activated by a reductant.7Penicillium citrinum.. The method of claim 1 , wherein the enzyme cocktail further comprises an enzyme preparation from8Penicillium citrinum.. The method of claim 2 , wherein the enzyme cocktail further comprises an enzyme preparation from9. The method of claim 1 , wherein the enzyme cocktail degrades the gluten oligopeptide into fragments of nine amino acids or less.10Aspergillus oryzae. The method of claim 9 , wherein the gluten degrading enzyme preparation isolated from with specificity for peptide substrate leucyl-glycyl-glycine (GDEP-LGG) and papain are in a percent relative activity ratio of 80:20 to 20:80.11. The method of claim 10 , wherein the ...

MILK COAGULANT AND METHOD FOR PRODUCING CHEESE

Provided in the present disclosure are a milk coagulant, a method for obtaining asclepain of Asclepias Linn. and cysteine protease B of Calotropis R. Br., as well as a method of producing cheese. The milk coagulant includes at least one of the asclepain of Asclepias Linn. and the cysteine protease B of Calotropis R. Br. 1. A milk coagulant , comprising at least one of asclepain of Asclepias Linn. and cysteine protease B of Calotropis R. Br.2Cynanchum otophyllum. The milk coagulant according to claim 1 , wherein the asclepain of Asclepias Linn. and the cysteine protease B of Calotropis R. Br. are from Schneid.3Cynanchum otophyllum. The milk coagulant according to claim 1 , wherein the asclepain of Asclepias Linn. and the cysteine protease B of Calotropis R. Br. are from leaves of the Schneid.4. The milk coagulant according to claim 1 , further comprising at least one of a calcium-containing compound and an aluminum-containing compound.5. The milk coagulant according to claim 1 , wherein the milk coagulant functions under a temperature of 40° C. to 70° C. and at a pH value of 5.5 to 8.0.6. The milk coagulant according to claim 1 , wherein the asclepain of Asclepias Linn. is capable of hydrolyzing Ser132-Thr133 peptide linkage on κ-casein.7. The milk coagulant according to claim 1 , wherein the cysteine protease B of Calotropis R. Br. is capable of hydrolyzing Asp14-Glu15 peptide linkage and Ser132-Thr133 peptide linkage on κ-casein.8. A method for obtaining asclepain of Asclepias Linn. and cysteine protease B of Calotropis R. Br. claim 1 , comprising:{'i': 'Cynanchum otophyllum', 'soaking leaves of Schneid. in a buffer, followed by collecting an extracted solution; and'}purifying the extracted solution, so as to obtain the asclepain of Asclepias Linn. and the cysteine protease B of Calotropis R. Br., respectively,{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'wherein the asclepain of Asclepias Linn. and the cysteine protease B of Calotropis R. Br. are those in the ...

METHODS AND COMPOSITIONS FOR THE TREATMENT OF AMYLOIDOSIS

Methods and compositions for the treatment or prevention of amyloidosis are provided. In some embodiments, the methods comprise administering to the subject a therapeutically effective amount of at least one catabolic enzyme or a biologically active fragment thereof. Such methods and compositions may be employed to reduce, prevent, degrade and/or eliminate amyloid formation in the lysosome and/or extracellularly. 1. A method of treating or preventing AA amyloidosis in a subject comprising administering to the subject a composition comprising a therapeutically effective amount of cathepsin L or a biologically active fragment thereof.217.-. (canceled)18. The method of claim 1 , wherein cathepsin L acts to prevent the formation of and/or degrade amyloid within a lysosome.19. The method of claim 1 , wherein cathepsin L is targeted to a cell lysosome.2024.-. (canceled)25. The method of claim 1 , wherein the subject is a human.2648-. (canceled)49. The method of claim 1 , wherein the cathepsin L comprises an amino acid sequence with at least 85% sequence identity to SEQ ID NO: 12 or SEQ ID NO: 65.50. The method of claim 49 , wherein the cathepsin L comprises an amino acid sequence selected from SEQ ID NO: 12 and SEQ ID NO: 65.51. The method of claim 50 , wherein the cathepsin L comprises SEQ ID NO: 12.52. The method of claim 1 , wherein the cathepsin L is a recombinant cathepsin L.53. The method of claim 1 , wherein the cathepsin L is administered intravenously.54. The method of claim 1 , wherein the cathepsin L is administered subcutaneously.55. The method of claim 1 , wherein the cathepsin L is administered at a dose of about 0.5 mg/kg to 12 mg/kg.56. The method of claim 55 , wherein the cathepsin L is administered at a dose of about 1 mg/kg to about 10 mg/kg.57. The method of claim 55 , wherein the cathepsin L is administered at a dose of about 2 mg/kg to 8 mg/kg.58. The method of claim 55 , wherein the cathepsin L is administered at a dose of about 4 mg/kg to 6 mg/kg. ...

ANTI-INFLAMMATORY PROTEINS AND PEPTIDES AND METHODS OF PREPARATION AND USE THEREOF

The present disclose relates to anti-inflammatory proteins/peptides, their uses, methods of preparation and methods of their detection. In particular, the invention relates to major royal jelly proteins modified by methyglyoxal and fragments thereof from a Leptospermum derived honey and royal jelly. 124.-. (canceled)2629.-. (canceled)30. The isolated functional fragment of claim 25 , which is chemically synthesized.31. The isolated functional fragment of claim 25 , which is recombinantly produced.32. A composition comprising the isolated functional fragment of claim 25 , or an analogue thereof.3444.-. (canceled)4653.-. (canceled)54. The method of claim 45 , wherein the method reduces inflammation in the cellular tissue.55. The method of claim 54 , wherein the inflammation is associated with one or more of the group consisting of: an inflammatory disorder claim 54 , a cardiovascular disorder claim 54 , a neurological disorder claim 54 , a pulmonary disorder claim 54 , a proliferative disorder claim 54 , an infectious disease or associated syndrome claim 54 , an allergic claim 54 , immunological or autoimmune disorder claim 54 , and inflammation associated with a wound.56. The method of claim 54 , wherein the inflammation is associated with one or more of the group consisting of: rheumatoid arthritis and polyarthritis.57. The method of claim 54 , wherein the inflammation is associated with one or more of the group consisting of: Alzheimer's disease claim 54 , progressive multifocal leukoencephalopathy (PML) claim 54 , and multiple sclerosis.58. The method of claim 54 , wherein the inflammation is associated with one or more of the group consisting of: asthma claim 54 , bronchitis claim 54 , bronchopneumonia claim 54 , adult respiratory distress syndrome claim 54 , emphysema claim 54 , and chronic obstructive pulmonary disease (COPD).59. The method of claim 54 , wherein the inflammation is associated with one or more of the group consisting of: genital herpes claim 54 ...

CANNABINOID EMULSION PRODUCT AND PROCESS FOR MAKING THE SAME

A dry consumable preparation and related methods are disclosed. The preparation has a plurality of excipient particles and at least one of a cannabinoid and a cannabinoid extract, the at least one of the cannabinoid or the cannabinoid extract containing one or more cannabinoids plated to the plurality of excipient particles. The preparation further comprises an effervescence agent, the effervescence agent comprising a carbonate salt, and at least one acid. The carbonate salt comprises sodium, potassium and/or calcium. The at least one acid comprises at least one of citric acid, tartaric acid, lactic, acetic, benzoic, ascorbic, oxalic, tannic, phosphoric, or malic acid. A ratio of the at least one of the carbonate salt to the at least one acid is at least 1:1, the ratio configured to create a chemical pH buffering system at a targeted pH range when the dry consumable preparation is added to a targeted amount of water. 1. A dry consumable preparation comprising:a plurality of excipient particles;at least one of a cannabinoid and a cannabinoid extract containing one or more cannabinoids, the at least one of the cannabinoid or the cannabinoid extract containing one or more cannabinoids plated to the plurality of excipient particles;an effervescence agent, the effervescence agent comprising a carbonate salt and at least one acid; wherein,the carbonate salt comprises at least one of sodium, potassium and calcium;the at least one acid comprises at least one of citric acid, tartaric acid, lactic, acetic, benzoic, ascorbic, oxalic, tannic, phosphoric, or malic acid; anda ratio of the carbonate salt to the at least one acid is at least 1:1, the ratio configured to create a chemical pH buffering system at a targeted pH range when the dry consumable preparation is added to a targeted amount of water.2. The preparation of claim 1 , further comprising claim 1 ,an encapsulant; wherein,the encapsulant is coupled to an outer surface of one or more of the at least one of a ...

ULTRAPURE HYPOALLERGENIC SOLUTIONS OF SACROSIDASE

One aspect provides an ultrapure, hypoallergenic sacrosidase. Another aspect provides a solution of sacrosidase in about 1:1 glycerol/water having an enzymatic activity of at least about 7500 IU/mL and a residual papain concentration that does not include an allergic reaction in a human patient when given a dose of about 2.0 mL/day. 1. A method for treating a subject who lacks endogenous sucrase activity , comprising orally administering an effective amount of a protein composition consisting essentially sacrosidase having a band volume ratio of sacrosidase to other proteins comprising papain of at least about 35:1 by SDS-PAGE of about 20 □g of said composition , wherein the primary structure of the sacrosidase is a 513 amino acid polypeptide that is gycosylated.2. The method of wherein the band volume ratio is about 35-55:1.3Saccharomyces. A method of treating a subject who lacks endogenous sucrase activity comprising orally administering an effective amount of a protein composition consisting essentially of sacrosidase derived from having residual papain in a concentration of less than about 10 ng/mL papain.4. The method of wherein the protein composition is administered in a solution.5. The method of wherein the sacrosidase has an enzyme activity of at least about 7500 IU/ml.6. The method of wherein a daily dose of the solution of about 2-10 mL per day does not induce an allergic reaction in a human patient afflicted with congenital sucrase-isomaltase deficiency.7. The method of wherein the sacrosidase contains less than about 3.0 ng/mL papain.8. The method of wherein the sacrosidase contains no detectable papain by an enzyme-linked immunosorbant assay having a lower limit of quantification of 3 ng/mL.9. The method of wherein the solution of sacrosidase contains no detectable papain by SDS-PAGE of up to about 15 □g of said solution.10. The method of wherein the solution of sacrosidase has enzymatic activity of about 7500-10 claim 5 ,000 IU/ml. This application is ...

METHODS AND COMPOSITIONS FOR THE TREATMENT OF SYMPTOMS OF WILLIAMS SYNDROME

A therapeutic composition for the treatment of the symptoms of Williams Syndrome and the method for preparing the therapeutic agents is disclosed. The therapeutic composition is a stable pharmaceutical composition comprising one or more digestive and/or pancreatic enzymes. The therapeutic composition may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic composition may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using fecal chymotrypsin level as a biomarker for the presence of Williams Syndrome, or the likelihood of an individual to develop Williams Syndrome is disclosed. 1. A method for treating one or more symptoms associated with Williams Syndrome in a patient diagnosed with Williams Syndrome comprising administering to the patient a therapeutically effective amount of a pharmaceutical composition comprising one or more digestive enzymes.2. The method of wherein the one or more digestive enzymes comprise one or more enzymes selected from the group consisting of proteases claim 1 , hydrolases claim 1 , amylases claim 1 , celluloses claim 1 , sucrases claim 1 , maltases claim 1 , papaya claim 1 , papain claim 1 , bromelain claim 1 , and lipases.3. The method of wherein the one or more digestive enzymes comprise one or more pancreatic enzymes.4. The method of wherein the proteases comprise chymotrypin and trypsin.5. The method of wherein the one or more digestive enzymes are independently derived from an animal source claim 1 , a microbial source claim 1 , or a plant source claim 1 , or are synthetically prepared.6. The method of wherein the animal source is a pig.7. The method of wherein the pharmaceutical composition comprises at least one amylase claim 1 , a mixture of proteases comprising chymotrypsin and trypsin claim 1 , at least one lipase claim 1 , and papain.8. The method of wherein the pharmaceutical composition further comprises papaya.9. The method of ...

METHODS AND COMPOSITIONS FOR THE TREATMENT OF AMYLOIDOSIS

Methods and compositions for the treatment or prevention of amyloidosis are provided. In some embodiments, the methods comprise administering to the subject a therapeutically effective amount of at least one catabolic enzyme or a biologically active fragment thereof. Such methods and compositions may be employed to reduce, prevent, degrade and/or eliminate amyloid formation in the lysosome and/or extracellularly. 148-. (canceled)49. A method of treating or preventing AL amyloidosis in a subject comprising administering to the subject a composition comprising a therapeutically effective amount of at least one catabolic enzyme or a biologically active fragment thereof.50. The method of claim 49 , wherein the catabolic enzyme is selected from cathepsin L claim 49 , protective protein/cathepsin A (PPCA) claim 49 , neuraminidase 1 (NEU1) claim 49 , tripeptidyl peptidase 1 (TPP1) claim 49 , cathepsin B claim 49 , cathepsin D claim 49 , cathepsin E claim 49 , and cathepsin K.51. The method of claim 50 , wherein the catabolic enzyme is cathepsin L claim 50 , and wherein the cathepsin L comprises an amino acid sequence with at least 85% identity to SEQ ID NO: 12 claim 50 , 59 claim 50 , 61 claim 50 , 63 claim 50 , 65 or 67.52. The method of claim 50 , wherein the catabolic enzyme is cathepsin L claim 50 , and wherein the cathepsin L is encoded by a nucleotide sequence having at least 85% identity to SEQ ID NO: 11 claim 50 , 58 claim 50 , 60 claim 50 , 62 claim 50 , 64 claim 50 , or 66.53. The method of claim 49 , wherein at least two catabolic enzymes are administered claim 49 , and wherein the catabolic enzymes are selected from cathepsin L claim 49 , protective protein/cathepsin A (PPCA) claim 49 , cathepsin B claim 49 , cathepsin D claim 49 , cathepsin E claim 49 , and cathepsin K.54. The method of claim 49 , wherein the catabolic enzyme acts to prevent the formation of and/or degrade amyloid within the lysosome.55. The method of claim 49 , wherein the catabolic enzyme is ...

COMPOSITIONS FOR CONTROL OF HEMIPTERAN INSECT STYLET SHEATH STRUCTURE FORMATION

Compositions having at least one compound which inhibits the formation of Hemipteran stylet sheaths and/or degrades hemipteran style sheaths that have already been formed, and thus deters or blocks hemipteran insects from feeding on plants, especially agriculturally important plants and methods of use of such compositions are described. Such compositions can be applied onto plants by spraying, dripping, or other methods and/or can be applied to the soil for uptake by the roots. These compositions and methods prevent and/or reduce the transmission of vascular associated diseases (caused by hemipteran vector-borne pathogens) to plants. 1. A composition for preventing or reducing hemipteran insect feeding on a plant comprising an agriculturally acceptable carrier , a surfactant , and at least one compound effective in preventing or reducing hemipteran insect feeding in an amount effective in preventing formation of said hemipteran insect's stylet sheath or in degrading said hemipteran insect's stylet sheath , wherein said compound is selected from the group consisting of (i) at least one carbohydrate-degrading enzyme that prevents stylet sheath formation and/or degrades stylet sheath , (ii) at least one protease that prevents stylet sheath formation and/or degrades stylet sheath , (iii) at least one small molecule that prevents stylet sheath formation and/or degrades stylet sheath , and (iv) a combination thereof.2. The composition of wherein said surfactant is selected from the group consisting of Tween-80 claim 1 , Triton X-100 claim 1 , an alchohol alkoxylate claim 1 , an alkylaryl ethoxylate claim 1 , a fatty amine ethoxylate claim 1 , an organo-silicone claim 1 , and a combination thereof.3Aspergillus oryzae,. The composition of wherein said protease is selected from the group consisting of cellulase claim 1 , protease from carboxypeptidase claim 1 , chymopapin claim 1 , papain claim 1 , bromelain claim 1 , ficin claim 1 , proteinase K claim 1 , calpain claim 1 , ...

Ultrapure hypoallergenic solutions of sacrosidase

One aspect provides an ultrapure, hypoallergenic sacrosidase. Another aspect provides a solution of sacrosidase in about 1:1 glycerol/water having an enzymatic activity of at least about 7500 IU/mL and a residual papain concentration that does not include an allergic reaction in a human patient when given a dose of about 2.0 mL/day.

THERAPEUTIC VEGETABLE SUBSTANCES

A pharmaceutical product containing papain, bromelain or mixtures thereof is intended for the treatment of several pathologies, such as Alzheimer's disease and depression, at a dosage of at least 7000 mg administered in a single dose. This dosage relates to papain powder having a titre of 3 U/mg and bromelain powder having a titre of 2 U/mg, and to a patient with a body weight of 55 kg. In the case of variations of the titre and/or of the body weight of the patient, the dosage must be adjusted in proportion to said variations. 1. A therapeutic method for treating Alzheimer's disease , comprising administering to a mammal in need thereof a product containing papain , bromelain or mixtures thereof at a dosage of at least 7000 mg delivered for at least 30 consecutive days in a single daily dose , said dosage being referred to a papain powder having a titer of 3 U/mg and a bromelain powder having a titer of 2 U/mg , as well as to a patient with a body weight of 55 kg , wherein in case of variations of the titer and/or the body weight of the patient the dosage must be adjusted in proportion to said variation.2. The therapeutic method according to claim 1 , wherein the administration of papain and bromelain is combined with the administration of monosodium phosphate in a catalytic amount.3. A therapeutic method for treating depression claim 1 , comprising administering to a mammal in need thereof a product containing papain claim 1 , bromelain or mixtures thereof at a dosage of at least 7000 mg delivered for at least 30 consecutive days in a single daily dose claim 1 , said dosage being referred to a papain powder having a titer of 3 U/mg and a bromelain powder having a titer of 2 U/mg claim 1 , as well as to a patient with a body weight of 55 kg claim 1 , wherein in case of variations of the titer and/or the body weight of the patient the dosage must be adjusted in proportion to said variation.4. The therapeutic method according to claim 2 , wherein the administration of ...

METHOD FOR DIAGNOSING AND TREATING DYSAUTONOMIA AND OTHER DYSAUTONOMIC CONDITIONS

A method for treating a Parkinson's patient with digestive/pancreatic enzymes involves administering an effective amount of digestive/pancreatic enzymes to an individual having the disorder in order to improve a symptom of the disorder. In addition, a method is provided for determining whether an individual has, or may develop, Parkinson's disease or related dysautonomic disorders and for determining whether an individual will benefit from the administration of pancreatic/digestive enzymes to treat the dysautonomic disorder. 1. A pharmaceutical preparation to treat a dysautonomic disorder in an individual comprising a therapeutically effective amount of digestive enzymes , wherein the digestive enzymes comprise protease , amylase and lipase , wherein lipase is present in the pharmaceutical composition in an amount of from about 4 ,000 to about 80 ,000 USP units/dose.2. The pharmaceutical preparation of claim 1 , wherein the dysautonomic disorder is Parkinson's disease.3. (canceled)4. The pharmaceutical preparation of claim 1 , wherein the digestive enzymes are provided as pancreatin.5. The pharmaceutical preparation of claim 1 , wherein the enzymes are derived from a source selected from the group consisting of animal enzymes claim 1 , plant enzymes claim 1 , synthetic enzymes claim 1 , and a combination thereof.6. The pharmaceutical preparation of wherein the preparation is manufactured using a technology selected from the group consisting of enteric coating claim 1 , lipid encapsulation claim 1 , direct compression claim 1 , dry granulation claim 1 , wet granulation claim 1 , and a combination thereof.7. The pharmaceutical preparation of claim 1 , wherein the preparation is administered orally via a dosage formulation selected from the group consisting of: pills claim 1 , tablets claim 1 , capsules claim 1 , microcapsules claim 1 , mini-capsules claim 1 , time released capsules claim 1 , mini-tabs claim 1 , sprinkles claim 1 , and a combination thereof.8. The ...

METHODS AND COMPOSITIONS FOR THE TREATMENT OF SYMPTOMS OF PRION DISEASES

A therapeutic composition for the treatment of the symptoms of prion diseases and the method for preparing the therapeutic agents is disclosed. The therapeutic composition is a stable pharmaceutical composition comprising one or more digestive and/or pancreatic enzymes. The therapeutic composition may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic composition may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using fecal chymotrypsin level as a biomarker for the presence of a prion disease, or the likelihood of an individual to develop a prion disease is disclosed. 1. A method for treating one or more symptoms associated with a prion disease in a patient diagnosed with a prion disease comprising administering to the patient a therapeutically effective amount of a pharmaceutical composition comprising one or more digestive enzymes.2. The method of wherein the one or more digestive enzymes comprise one or more enzymes selected from the group consisting of proteases claim 1 , amylases claim 1 , celluloses claim 1 , sucrases claim 1 , maltases claim 1 , papaya claim 1 , papain claim 1 , and lipases.3. The method of wherein the one or more digestive enzymes comprise one or more pancreatic enzymes.4. The method of wherein the proteases comprise chymotrypin and trypsin.5. The method of wherein the one or more digestive enzymes are claim 1 , independently claim 1 , derived from an animal source claim 1 , a microbial source claim 1 , or a plant source claim 1 , or are synthetically prepared.6. The method of wherein the animal source is a pig.7. The method of wherein the pharmaceutical composition comprises at least one amylase claim 1 , a mixture of proteases comprising chymotrypsin and trypsin claim 1 , at least one lipase claim 1 , and papain.8. The method of wherein the pharmaceutical composition further comprises papaya.9. The method of wherein the pharmaceutical ...

TOBACCO PROTEASE GENES

The invention provides protease genes which are regulated in a specific manner during curing of tobacco plants material and which affect the flavour of cured tobacco.

Novel Pharmaceutical Preparation for Preeclampsia, Eclampsia, and Toxemia and Their Related Symptoms and Related Disorders of Pregnancy

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed. 1. A method for treating an individual exhibiting one or more symptoms of preeclampsia , the method comprising administering a therapeutically effective amount of digestive enzymes to the individual.2. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is selected from the group consisting of: amylase claim 1 , lipase claim 1 , protease claim 1 , and a combination thereof.3. The pharmaceutical preparation of claim 1 , wherein the digestive enzyme is further selected from the group consisting of: chymotrypsin claim 1 , trypsin claim 1 , pancreatin claim 1 , papaya claim 1 , papain claim 1 , and a combination thereof.4. The pharmaceutical preparation of claim 1 , wherein the enzymes are derived from a source selected from the group consisting of animal enzymes claim 1 , plant enzymes claim 1 , synthetic enzymes claim 1 , and a combination thereof.5. The pharmaceutical preparation of wherein the preparation is manufactured using a technology selected from the group consisting of enteric coating claim 1 , lipid encapsulation claim 1 , direct compression claim 1 , dry granulation claim 1 , wet granulation claim 1 , and a combination thereof.6. The pharmaceutical preparation of claim 1 , wherein the preparation is administered orally via a dosage formulation ...

Method and composition for hydrolyzing eggshell membrane

The present invention relates to a method for hydrolyzing eggshell membrane, comprising the step of treating a suitable amount of eggshell in a solution containing a denaturing agent, a reducing agent, a buffer, and an enzyme. The invention also relates to a composition for hydrolyzing eggshell membrane according to the preceding method.

COMPOSITIONS AND METHODS FOR CONTROL OF HEMIPTERAN INSECT STYLET SHEATH STRUCTURE FORMATION

Compositions having at least one compound which inhibits the formation of Hemipteran stylet sheaths and/or degrades hemipteran style sheaths that have already been formed, and thus deters or blocks hemipteran insects from feeding on plants, especially agriculturally important plants and methods of use of such compositions are described. Such compositions can be applied onto plants by spraying, dripping, or other methods and/or can be applied to the soil for uptake by the roots. These compositions and methods prevent and/or reduce the transmission of vascular associated diseases (caused by hemipteran vector-borne pathogens) to plants. 1. A composition for preventing or reducing hemipteran insect feeding on a plant comprising an agriculturally acceptable carrier , at least one compound effective in preventing or reducing hemipteran insect feeding in an amount effective in preventing formation of said hemipteran insect's stylet sheath or in degrading said hemipteran insect's stylet sheath , and optionally an adjuvant , wherein said compound is selected from the group consisting of at least one carbohydrate-degrading enzyme , at least one protease , at least one small molecule that prevents stylet sheath formation , and a combination thereof.2Aspergillus oryzae. The composition of wherein said protease is selected from the group consisting of cellulase claim 1 , protease from claim 1 , carboxypeptidase claim 1 , chymopapin claim 1 , papain claim 1 , bromelain claim 1 , ficin claim 1 , proteinase K claim 1 , calpain claim 1 , caspase claim 1 , cathepsin claim 1 , actinidin claim 1 , tobacco etch virus protease claim 1 , γ-glutamyl hydrolase claim 1 , and a combination thereof.3. The composition of wherein said carbohydrate-degrading enzyme is selected from the group consisting of amyloglucosidase claim 1 , α-amylase claim 1 , laminarinase claim 1 , licheninase claim 1 , cellulase claim 1 , hemicellulase claim 1 , glucuronyl hydrolase claim 1 , lytic polysaccharide ...

COMPOSITION AND METHOD OF PREPARATION OF PROTEASE MICROPARTICULATE SLOW RELEASE PREPARATION

Compositions containing microparticles loaded with one or protease enzymes and optionally auxiliary therapeutic agents and methods of treating conditions such as keloids therewith are disclosed. The biodegradable polymer and the protease enzyme therein form a controlled release matrix for extended release of the enzyme after administration to a mammal in need thereof. 1. A composition , comprising a plurality of biodegradable polymer microparticles comprising a protease enzyme therein , the biodegradable polymer and the protease enzyme forming a controlled release matrix for extended release of the enzyme.2. The composition of claim 1 , wherein the protease is selected from the group consisting of collagenase claim 1 , papain claim 1 , elastase and mixtures thereof.3. The composition of claim 2 , wherein the plurality of microparticles include a mixture of microparticles containing different proteases.4. The composition of claim 1 , wherein the biodegradable polymer wherein the biodegradable polymer is selected from the group consisting of polylactic acid (PLA) claim 1 , polylactic co-glycolic acid (PLGA) claim 1 , polyglycolic acid (PGA) polylactones claim 1 , polyorthocarbonate claim 1 , polyhydroxybutyrate claim 1 , polyalkylcyanoacrylates claim 1 , polyanhydrides claim 1 , polyorthoesters claim 1 , polyester claim 1 , polyimide claim 1 , polyglycolides (PGA) claim 1 , polyorthoester claim 1 , polyacetates claim 1 , polystyrene claim 1 , polycarbonates claim 1 , polysaccharides claim 1 , polycaprolactone claim 1 , L-polylactides claim 1 , block co-polymers of polyesters and linear or star-polyethyleneglycol claim 1 , poly-beta-hydroxybutyrate claim 1 , beta-hydroxyvalerate-copolymers claim 1 , polyaminoacids claim 1 , hydrophobized hyaluronic acid claim 1 , dextrans claim 1 , starches claim 1 , methyl methacrylate claim 1 , acrylamide claim 1 , bisacrylamide claim 1 , albumin claim 1 , cellulose claim 1 , cellulose-based polymers claim 1 , chitosan claim 1 , ...

Composition of probiotics and digestive enzymes and method of preparing and using the same

Disclosed are compositions and methods useful for improving blood cholesterol profiles in a mammal, particularly for improving metabolism of cholesterol, for reducing the levels of low-density lipoprotein cholesterol (LDL-C) in the blood, increasing the levels of high-density lipoprotein (HDL-C) in the blood, for improving weight loss in a mammal, and/or for enhancing overall cardiovascular health in a mammal. Methods can involve identifying a mammal in need of lowering of blood LDL-C and/or triglyceride concentrations, and administering to said mammal a specific formulation consisting of a blend of probiotics; specifically, Bifidobacterium infantis, Bifidobacterium bifidum, Lactobacillus acidophilus, Lactobacillus salivarius, Lactobacillus plantarum, Lactobacillus rhamnosus, Bifidobacterium longum, Lactobacillus casei, Lactobacillus paracasei, in combination with a blend of digestive enzymes; specifically, amylase, glucoamylase, lipase, bromelain, maltase, lactase, hemicellulase, xylanase, papain, and invertase. Preferably, the aforementioned probiotics and digestive enzymes are combined into capsules and administered to said mammal three times daily to achieve said lowering of LDL-C and triglyceride concentrations in blood.

METHOD OF TREATING FIBROSIS IN SKELETAL MUSCLE TISSUE

A method is disclosed to dissolve protein deposited in muscle. The method includes the step of administering an effective amount of an agent selected from the group consisting of fibrinolytics, proteolytics, photolytic and magnelytic agents. 1. A method to dissolve protein deposited in muscle or tissue , said method comprising injecting an effective amount of a fibrinolytic agent selected from the group consisting of serrapeptase , nattokinase , and combinations thereof into the muscle or tissue , wherein the fibrinolytic agent is injected in an amount ranging from 5000 to 5 ,000 ,000 IU.2. The method according to claim 1 , wherein the muscle is a skeletal muscle selected from the group consisting of the spine claim 1 , head claim 1 , neck and the limbs.3. The method according to claim 1 , wherein the fibrinolytic agent is administered in a daily dosage of 5000 to 5 million International Units.4. The method according to claim 3 , wherein the fibrinolytic agent is administered in a daily dosage of 250 claim 3 ,000 to 1.5 million IU.5. The method according to claim 1 , wherein the fibrinolytic agent is formulated in a physiologically acceptable solution at a concentration in the range of about 0.1 mg/ml to about 2 mg/ml.6. The method according to claim 1 , wherein the fibrionolytic agent is administered in combination with at least one of a protease claim 1 , an anti-inflammatory agent and an anti-oxidant.7. The method of claim 6 , wherein the fibrinolytic agent is administered with a serine protease.8. The method of claim 7 , wherein the serine protease is urokinase.9. The method of claim 1 , wherein the formulation comprises 2000 to 20 claim 1 ,000 IU of fibrinolytic agent and 2000-20 claim 1 ,000 IU urokinase.10. The method according to claim 1 , wherein the fibrinolytic agent is formulated to comprise claim 1 , per 30 mL claim 1 , 10-50 claim 1 ,000 IU of serrapeptase claim 1 , 10-50 claim 1 ,000 IU of nattokinase claim 1 , 10-50 claim 1 ,000 IU of lipase claim 1 ...

PROCESS FOR DETERMINING ENZYME ACTIVITY IN A CELL BY ACTIVITY-BASED REPORTER GENE TECHNOLOGY (ABRGT)

Methods and materials for specific imaging of active enzyme in a live or intact cell are disclosed. The enzyme of interest tagged to reporter protein (donor) is exogenously expressed in a cell. The conversion of proenzyme to active enzyme (containing reporter protein) is achieved upon applying an appropriate stimulus to the target cells. The activated enzyme is labelled with an activity-based probe carrying a fluorophore (acceptor). The covalent labelling of active enzyme by the activity-based probe creates a FRET pair which provides the opportunity to exquisitely image the function of an “active enzyme”. This method is used for specific imaging of the function of active caspase-3,-7,-8,-9 and cathepsin-B and also for profiling of inhibitors of caspases and cathepsin B. 1. A process for determining the activity of an enzyme in a cell by using activity-based reporter gene technology (AbRGT) comprising;(a) preparing a cell overexpressing the enzyme of interest (EoI) tagged to a reporter protein acting as a fluorescence donor with an inducing agent,(b) introducing an fABP comprising a warhead, a linker sequence, and a fluorescent acceptor moiety into the cell,(c) allowing the fABP containing fluorescent acceptor to covalently modify the EoI tagged to reporter protein (fluorescence donor) to form an in-situ FRET pair, and(d) measuring a fluorescence signal from the FRET pair.2. The process as claimed in claim 1 , wherein the enzyme of interest is a cysteine protease.3. The process as claimed in claim 2 , wherein the cysteine protease is selected from the group consisting of caspase-3 claim 2 , caspase-7 claim 2 , caspase-8 claim 2 , caspase-9 and cathepsin B.4. The process as claimed in claim 1 , wherein the fluorescent donor is an exogenously expressed fluorescent reporter protein.5. The process as claimed in claim 4 , wherein the exogenously expressed fluorescent reporter protein is selected from the group consisting of GFP (Green Fluorescent protein) claim 4 , CFP ( ...

BACTERIAL STRAIN CLOSTRIDIUM HISTOLYTICUM AND ITS USE

Bacterial strain was deposited in CCM (Czech Collection of Microorganisms at Masaryk University, Faculty of Science) under No. CCM 8656. This strain produces proteolytic enzymes including collagenase, elastinase, neutral proteases and clostripain under anaerobic conditions at a temperature from 25° C. to 45° C. The strain is used for the production of a mixture of two collagenases, col 1 and col 2, with molecular weight 116 kDa and 126 kDa, and possibly clostripain. The mixture of the above-mentioned collagenases and possibly clostripain obtained from the above-mentioned strain is used for the isolation of Langerhans islets. 1Clostridium histolyticum. A bacterial strain deposited under deposit number CCM 8656 , wherein said bacterial strain produces proteolytic enzymes including collagenase , elastinase , neutral proteases and clostripain under anaerobic conditions at a temperature from 25° C. to 45° C.2Clostridium histolyticum. A method for producing a mixture of two collagenases claim 1 , col 1 (SEQ ID NO: 1) and col 2 (SEQ ID NO: 2) claim 1 , with molecular weight of 116 kDa and 126 kDa claim 1 , the method comprising culturing the bacterial strain CCM 8656 of under anaerobic conditions at a temperature from 25° C. to 45° C.3Clostridium histolyticum. A method for producing a mixture of two collagenases claim 1 , col 1 (SEQ ID NO: 1) and col 2 (SEQ ID NO: 2) claim 1 , with molecular weight of 116 kDa and 126 kDa claim 1 , and clostripain claim 1 , the method comprising culturing the bacterial strain CCM 8656 of under anaerobic conditions at a temperature from 25° C. to 45° C.4Clostridium histolyticum. A method for isolating Langerhans islets claim 2 , the method comprising digesting pancreatic tissue with a mixture of two collagenases claim 2 , col 1 (SEQ ID NO: 1) and col 2 (SEQ ID NO: 2) claim 2 , with molecular weight of 116 kDa and 126 kDa claim 2 , produced by the bacterial strain CCM 8656 according to the method of claim 2 , to release the Langerhans islets ...

COVALENT MODIFICATION OF BIOLOGICAL MACROMOLECULES

The present disclosure provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a biological macromolecule comprising one or more thiol groups; and (b) a molecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure also provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a molecule comprising one or more thiol groups; and (b) a biological macromolecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure further provides a covalently modified biological macromolecule prepared by any of the disclosed methods. The covalently modified biological macromolecules may be further crosslinked to form a scaffold. 1. A method of covalently modifying a biological macromolecule , the method comprising subjecting a reaction mixture comprising:(a) a biological macromolecule comprising one or more thiol groups; and(b) a molecule comprising one or more olefin or alkyne moietiesto a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule.2. The method of claim 1 , wherein the biological macromolecule is a protein.3. The method of claim 1 , wherein the radical reaction is a photoinitiated radical reaction.4. The method of claim 1 , wherein the radical reaction is performed under non-denaturing conditions.5. The method of claim 1 , wherein the biological macromolecule comprises one or more lysine side chains claim 1 , and wherein the one or more thiol groups are introduced into the biological macromolecule by converting the one or more lysine side chains into the one or more thiol groups.6. The method of claim 1 , ...

Substituted pyrazine dithiol reducing agents

Substituted dithiol pyrazine compounds useful as reducing agents in biologically relevant media having formula: where variables are defined herein and corresponding oxidized pyrazine dithianes. Reducing agents useful to reduce disulfide bonds, particularly in proteins, or to prevent the formation of disulfide bonds, particularly in proteins, and other biological molecules. Reducing agents useful to regulate protein function in proteins in which a sulfhydryl group is associated with biological activity. Reducing agents useful and suitable for application in a variety of biological applications, particularly as research and synthetic reagents. S-acylated dithiol pyrazine compounds, where R 3 is an acyl group, are selectively activated as reducing agents by removal of the S-acyl groups enzymatically or chemically. Dithiol pyrazine reducing agents and corresponding S-acylated dithiol pyrazines, immobilized on surfaces or conjugated to other chemical species, are provided.

BMP PEPTIDES AND METHODS OF USE

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition. 1. A peptide consisting of an amino acid sequence selected from SEQ ID NOs: 20 , 21 , 22 , 24 , 25 , 26 , 27 and 28.2. A pharmaceutical composition comprising the peptide of and a pharmaceutically acceptable carrier.3. A method of increasing a biological activity of a cell claim 2 , comprising treating the cell with an effective amount of the composition of .4. The method of claim 3 , wherein the cell is derived from placenta claim 3 , bone marrow claim 3 , adipose tissue claim 3 , blood vessel claim 3 , amniotic fluid claim 3 , synovial fluid claim 3 , synovial membrane claim 3 , pericardium claim 3 , periosteum claim 3 , dura claim 3 , peripheral blood claim 3 , umbilical blood claim 3 , menstrual blood claim 3 , teeth claim 3 , nucleus pulposus claim 3 , brain claim 3 , skin claim 3 , hair follicle claim 3 , intestinal crypt claim 3 , neural tissue claim 3 , or muscle.5. The method of claim 3 , wherein the cell is a progenitor cell or adult stern cell.6. The method of claim 3 , wherein the cell is a pluripotent stem cell.7. The method of claim 3 , wherein the cell is selected from the group consisting of mesenchymal stem cells claim 3 , adipose-derived stem cells claim 3 , embryonic stem cells claim 3 , progenitor cells claim 3 , differentiated cells claim 3 , undifferentiated cells claim 3 , and induced pluripotent stem cells.8. The method of claim 3 , wherein the biological activity is an osteoinductive activity.9. The method of claim 3 , wherein the biological activity is a chondroinductive activity.10. The method of claim 3 , wherein the biological activity is a ligament/tendon ...

Implantable Device for Sustained Release of a Macromolecular Drug Compound

An implantable device for delivery of a macromolecular drug compound is provided. The device comprises a core having an outer surface and a membrane layer positioned adjacent to the outer surface of the core. The core comprises a core polymer matrix within which is dispersed a drug compound having a molecular weight of about 0.5 kDa or more, the polymer matrix containing a hydrophobic polymer. Further, the membrane layer comprises a membrane polymer matrix within which the macromolecular drug compound is optionally dispersed. The concentration of the macromolecular drug compound in the core is greater than the concentration of the macromolecular drug compound in the membrane layer. 1. An implantable device for delivery of a macromolecular drug compound , the device comprising:a core having an outer surface, wherein the core comprises a core polymer matrix within which is dispersed a drug compound having a molecular weight of about 0.5 kDa or more, the polymer matrix containing a hydrophobic polymer; anda membrane layer positioned adjacent to the outer surface of the core, wherein the membrane layer comprises a membrane polymer matrix within which the macromolecular drug compound is optionally dispersed, wherein the concentration of the macromolecular drug compound in the core is greater than the concentration of the macromolecular drug compound in the membrane layer.2. The implantable device of claim 1 , wherein the device has a generally circular cross-sectional shape.3. The implantable device of claim 2 , wherein the device has a diameter of from about 0.5 to about 50 millimeters.4. The implantable device of claim 1 , wherein the device is in the form of a cylinder.5. The implantable device of claim 1 , wherein the device is in the form of a disc.6. The implantable device of claim 1 , wherein macromolecular drug compounds constitute from about 5 wt. % to about 60 wt. % of the core and the core polymer matrix constitutes from about 40 wt. % to about 95 wt. % of the ...

Cannabinoid Composition and Method of Sublingual, Buccal and Oral Mucosa Delivery

A formulation includes a cannabinoid extract that is pharmaceutically effective by systemic delivery via a recipient's oral mucosal lining. The method of delivery avoids the digestive tract processing and liver metabolizing of the active ingredients of the formulation, whereby lower doses cause a desired therapeutic effect or other intended effect. Variations of the formulation include a cannabinoid extract and one or more of pregelatinized tapioca starch polymethylsilsesquioxane, bromelain, volume Fenugreek gum, vitamin B12, luo han guo fruit extract, mannitol, microcrystalline cellulose, sodium alginate, gellan gum, menthol Natural peppermint flavor or oil, Grapefruit flavored powder or oil, magnesium stearate and/or citric acid. The cannabinoid extract may include Tetrahydrocannabinol, tetrahydrocannabinolic acid, Cannabidiol, Cannabidiol acid, and/or other cannabinoid sourced from a cannabis sativa plant. The formulation includes at least one cannabinoid in a volume and measure that is pharmaceutically effective and/or effectual in achieving an intended systemic state or response of the recipient. 1. A sublingual formulation comprising:an extract of a cannabinoid containing plant material, said extract containing (i) one or more first cannabinoid active agent(s) or (ii) a combination of said extract and one or more additional cannabinoid active agent(s), said additional cannabinoid active agent(s) selected from the group consisting of (a) partially or completely purified cannabinoid compounds, (b) synthetic cannabinoid compounds, and (c) mixtures thereof; anda pregelatinized tapioca starch.2. The formulation of further comprising fenugreek gum.3. The formulation of further comprising vitamin B12.4. The formulation of further comprising bromelain.5. The formulation of further comprising luo han guo fruit extract.6. The formulation of further comprising mannitol.7. The formulation of further comprising microcrystalline cellulose.8. The formulation of further ...

PROTEASIS TOBACCO GENES

РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2017 105 148 A (51) МПК A01H 5/12 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ЗАЯВКА НА ИЗОБРЕТЕНИЕ (21)(22) Заявка: 2017105148, 16.07.2015 (71) Заявитель(и): ФИЛИП МОРРИС ПРОДАКТС С.А. (CH) Приоритет(ы): (30) Конвенционный приоритет: 18.07.2014 EP 14177715.1 (85) Дата начала рассмотрения заявки PCT на национальной фазе: 20.02.2017 R U (43) Дата публикации заявки: 20.08.2018 Бюл. № 23 (72) Автор(ы): БОВЭ Люсьен (CH), ФЛОРАК Дион (CH), БЭТТИ Джеймс (CH) (86) Заявка PCT: (87) Публикация заявки PCT: WO 2016/009006 (21.01.2016) R U (54) ГЕНЫ ПРОТЕАЗ ТАБАКА (57) Формула изобретения 1. Мутантная, не встречающаяся в природе или трансгенная клетка растения табака, содержащая: (i) полинуклеотид, содержащий последовательность, состоящий из последовательности или по существу состоящий из последовательности, выполненной с возможностью кодирования функциональной протеазы и характеризующейся по меньшей мере 96% идентичностью последовательности с любой из SEQ ID NO:1 - SEQ ID No: 80; (ii) полипептид, кодируемый полинуклеотидом, указанным в (i); (iii) полипептид, содержащий последовательность, состоящий из последовательности или по существу состоящий из последовательности, выполненной с возможностью кодирования протеазы и характеризующейся по меньшей мере 96% идентичностью последовательности с SEQ ID NO:81 - SEQ ID No: 160; или (iv) структуру, вектор или вектор экспрессии, содержащие выделенный полинуклеотид, указанный в (i), и где экспрессия или активность указанной протеазы модулированы по сравнению с контрольной клеткой растения табака, в которой экспрессия или активность указанной протеазы не были изменены. 2. Клетка растения табака по п. 1, где экспрессия или активность указанной протеазы подверглись повышающей регуляции по сравнению с контрольной клеткой растения Стр.: 1 A 2 0 1 7 1 0 5 1 4 8 A Адрес для переписки: 129090, Москва, ул. Б. Спасская, 25, стр. 3, ООО "Юридическая фирма Городисский и Партнеры" 2 0 1 7 ...

Preparation of triticum aestivum wheat proteinase obtained in soluble form and method for preparation thereof

FIELD: biotechnology. SUBSTANCE: invention relates to the field of molecular biology and biotechnology and is a biologically active protein preparation, having specific activity of papain-like cysteine proteinases, characterized in that it is an amino acid sequence selected from SEQ ID NO:2-4, expressed in soluble form. Invention also relates to a method for producing a biologically active protein preparation, wherein the method comprises transforming cells with plasmids containing DNA, encoding a protein having an amino acid sequence selected from SEQ ID NO: 2-4, cultivation and isolation of a biologically active preparation. EFFECT: invention provides the possibility of obtaining a Triticum aestivum preparation with a high and stable yield, a high level of purification and functional activity. 9 cl, 8 dwg, 7 ex РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2 676 322 C1 (51) МПК C12N 15/11 (2006.01) C12N 15/00 (2006.01) C12N 15/63 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ОПИСАНИЕ ИЗОБРЕТЕНИЯ К ПАТЕНТУ (52) СПК C12N 15/11 (2006.01); C12N 15/70 (2006.01) (21)(22) Заявка: 2017122806, 28.06.2017 (24) Дата начала отсчета срока действия патента: Дата регистрации: 27.12.2018 (73) Патентообладатель(и): федеральное государственное автономное образовательное учреждение высшего образования Первый Московский государственный медицинский университет имени И.М. Сеченова Министерства здравоохранения Российской Федерации (Сеченовский университет) (RU) (45) Опубликовано: 27.12.2018 Бюл. № 36 Адрес для переписки: 119991, Москва, ул. Трубецкая, 8, стр. 2, ФГАОУ ВО Первый МГМУ им. И.М. Сеченова, технопарк C 1 2 6 7 6 3 2 2 R U 2008115428 A2, 25.09.2008. (54) ПРЕПАРАТ ЦИСТЕИНОВОЙ ПРОТЕИНАЗЫ ПШЕНИЦЫ ТРИТИКАИНА-АЛЬФА, ПОЛУЧЕННОЙ В РАСТВОРИМОЙ ФОРМЕ, И СПОСОБ ПОЛУЧЕНИЯ ПРЕПАРАТА (57) Реферат: Изобретение относится к области препарата, где способ включает трансформацию молекулярной биологии и биотехнологии и клеток плазмидами, содержащими ДНК, представляет собой ...

Oral cavity cleaning composition and application thereof

本发明提供一种口腔清洁组合物及其应用，包括蛋白水解酶蛋白、非蛋白水解酶蛋白和益生菌。本发明口腔清洁组合物通过分解口腔残留物，破坏口腔有害细菌的生存环境，抑制口腔有害菌群生长的同时为口腔益生菌提供了良好的生长环境，间接或直接促进口腔益生菌的生长，从而维持良好的口腔环境，降低口腔疾病的发生。

Reduced-pressure treatment systems and methods employing debridement mechanisms

Reduced-pressure treatment systems and methods are disclosed that employ debridement mechanisms to remove unwanted tissue. In one instance, a reduced-pressure treatment system for treating a tissue site on a patient includes a manifold member for distributing reduced pressure to the tissue site, a support member for disposing proximate the tissue site and the manifold, and a debridement mechanism coupled to the support member. The debridement mechanism is for debriding the tissue site. The system further includes a sealing drape for placing over the tissue site and manifold member. The sealing drape is operable to form a fluid seal over the tissue site and manifold member. The system also includes a reduced-pressure subsystem for delivering a reduced pressure to the sealing drape. The system may further include a chemical-debridement subsystem. Other systems, manifolds, and methods are disclosed.

Enzyme preparation for modifying food material

本发明的食品苦味改善用酶制剂含有磷脂酶。根据需要，还含有蛋白酶。本发明的食品苦味改善方法包括用含有该酶制剂的食品苦味改善剂处理食品素材的工序。本发明的食品加工制品的制造方法包括用含有该酶制剂的食品苦味改善剂处理食品素材的工序。经过用本发明的食品苦味改善用酶制剂处理的食品，即使在长期保存后烹调，苦味也被抑制。另外，能够提供用于改善食品的苦味、根据需要用于将食品软化的酶制剂。

Novel compositions for the treatment of cancer

본 발명은 단백질 분해 효소 및 청징제를 포함하는 신규한 조성물, 및 이들 조성물을 사용한 암의 치료 및/또는 예방 방법에 관한 것이다. The present invention relates to novel compositions comprising proteolytic enzymes and fining agents, and methods of treating and/or preventing cancer using these compositions.

A kind of preparation method of green sustained release antisludging agent

本发明涉及一种绿色缓释阻垢剂的制备方法，属于添加剂技术领域。本发明首先利用高碘酸钠对淀粉进行改性，使其形成醛基，随后与再表面活性剂进行球磨改性，提高耐硬水性，而且通过球磨可以增加改性淀粉活性，同时表面活性剂中的3‑氨基丙基三乙氧基硅烷分解产生硅氧键，使改性淀粉结合硅氧键，增加了与基材的结合性能，再与丙烯酸丁酯、丙烯酰胺进行接枝反应，同时加入添加剂引入活性体，增加与钙离子等进行结合，同时利用活性体可以很好的与马来酸酐、氨水等进行混合反应，配合混合酶，利用酶对淀粉的分解，可以使沉积的钙离子等物质缓慢脱离基材，并且所使用的原料可降解，有效解决了目前阻垢剂毒性大，易造成环境污染的问题。

Animal protein hydrolyzes specific enzyme and preparation method thereof

本发明公开了一种动物蛋白水解专用酶及其制备方法，属于酶制剂技术领域。所述的动物蛋白水解专用酶，以重量百分比为单位，包括以下原料：木瓜蛋白酶8‑12％，菠萝蛋白酶8‑12％，核酸酶4‑7％，风味酶8‑12％，食盐18‑22％，海藻糖4‑7％，葡萄糖35‑45％。本发明将多种天然生物酶按照一定比例组合而成，是一种能够根据动物性食品副产品原料以及处理工艺不同而进行水解的复合型动物蛋白水解专用酶产品。利用本发明对各类动物蛋白进行水解，通过控制水解程度可以得到需要的多肽、小肽、氨基酸产物，使产品的得率、溶解性、风味、口感达到新的产品等级，满足人们的各种需求。

Production of fc fragments

In one aspect, the disclosure provides cells and transgenic non-human mammals for the production of Fc fragments, as well as compositions and uses thereof.

Method for Production of Silk Peptides

본 발명은 견사 단백질을 효소적 방법으로 가수분해하여 견사 펩타이드를 제조하는 공정에 있어서, 식용 가능한 과일(파인애플)로부터 유래하는 단백질 분해효소인 브로멜라인을 이용하는 새로운 제조기술에 관한 것이다. 또한, 본 발명은 탄산나트륨법으로 정련한 견사를 염화칼슘, 증류수 및 에탄올 혼합액에 용해시킨 후 투석법으로 염화칼슘을 제거하고, 브로멜라인 등의 단백질 분해효소를 처리하여 견사 펩타이드를 수득하는 것이다. 본 발명의 식물성 단백질 분해효소인 브로멜라인 이용기술은 견사 단백질로부터 분자량 500 내지 10,000의 고 가용성인 견사 펩타이드를 고수율로 얻을 수 있어, 기능성 식품소재 또는 화장품의 원료 제조 시 유용하게 활용될 것이다.

Bmp peptides & methods of use

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition.

Production of fc fragments

在一个方面，本公开提供用于Fc片段的产生的细胞和转基因非人哺乳动物，以及其组合物及用途。

Tobacco protease genes

FIELD: biotechnology.SUBSTANCE: invention relates to the field of biotechnology, in particular to a tobacco plant cell giving a modified taste profile to dried tobacco plant material containing the specified cell, as well as to a plant, plant material and a tobacco composition containing the above-mentioned cell. A method for obtaining a tobacco plant with increased protease levels, as well as a method for producing a tobacco plant with decreased protease levels are also disclosed.EFFECT: invention allows for effective obtaining of dried tobacco plant material with a modified taste profile in comparison with dried tobacco plant material of a wild type.22 cl, 3 dwg, 2 tbl, 5 ex РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2 756 102 C2 (51) МПК A01H 5/12 (2006.01) C12N 15/82 (2006.01) C12N 9/50 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ОПИСАНИЕ ИЗОБРЕТЕНИЯ К ПАТЕНТУ (52) СПК A01H 5/12 (2020.08); C12N 15/8201 (2020.08); C12N 15/8213 (2020.08); C12N 15/8242 (2020.08); C12N 9/1029 (2020.08); C12N 9/104 (2020.08); C12N 9/48 (2020.08); C12N 9/63 (2020.08) (21)(22) Заявка: 2017105148, 16.07.2015 16.07.2015 Дата регистрации: (73) Патентообладатель(и): ФИЛИП МОРРИС ПРОДАКТС С.А. (CH) 28.09.2021 18.07.2014 EP 14177715.1 (43) Дата публикации заявки: 20.08.2018 Бюл. № 23 (45) Опубликовано: 28.09.2021 Бюл. № 28 (86) Заявка PCT: EP 2015/066341 (16.07.2015) C 2 C 2 (85) Дата начала рассмотрения заявки PCT на национальной фазе: 20.02.2017 (56) Список документов, цитированных в отчете о поиске: CATHERINE NAVARRE et al., Identification, gene cloning and expression of serine proteases in the extracellular medium of Nicotiana tabacum cells, Plant Cell Rep, 2012, Vol.31, pp.1959-1968. WO 2008034648 A1, 27.03.2008. WO 2009134339 A2, 05.11.2009. GETU BEYENE et al., Two new cysteine proteinases with specific expression patterns in mature and (см. прод.) (87) Публикация заявки PCT: WO 2016/009006 (21.01.2016) 2 7 5 6 1 0 2 2 7 5 6 1 0 2 Приоритет(ы): (30) Конвенционный ...

Methods for preventing, removing, reducing, or disrupting biofilm

Method of treating proteinuria in pregnancy

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed.

Methods and compositions for the treatment of symptoms of prion diseases

A therapeutic composition for the treatment of the symptoms of prion diseases and the method for preparing the therapeutic agents is disclosed. The therapeutic composition is a stable pharmaceutical composition comprising one or more digestive and/or pancreatic enzymes. The therapeutic composition may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic composition may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using fecal chymotrypsin level as a biomarker for the presence of a prion disease, or the likelihood of an individual to develop a prion disease is disclosed.

Methods and compositions for the treatment of symptoms of Williams Syndrome

A therapeutic composition for the treatment of the symptoms of Williams Syndrome and the method for preparing the therapeutic agents is disclosed. The therapeutic composition is a stable pharmaceutical composition comprising one or more digestive and/or pancreatic enzymes. The therapeutic composition may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic composition may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using fecal chymotrypsin level as a biomarker for the presence of Williams Syndrome, or the likelihood of an individual to develop Williams Syndrome is disclosed.

Method of diagnosing preeclampsia or pregnancy-induced hypertension

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed.

New compositions for treating cancer

本发明涉及包含蛋白水解酶和澄清剂的新型组合物以及使用这些组合物治疗和/或预防癌症的方法。

Reduced-pressure treatment systems and methods employing debridement mechanisms

Reduced-pressure treatment systems and methods are disclosed that employ debridement mechanisms to remove unwanted tissue. In one instance, a reduced-pressure treatment system for treating a tissue site on a patient includes a manifold member for distributing reduced pressure to the tissue site, a support member for disposing proximate the tissue site and the manifold, and a debridement mechanism coupled to the support member. The debridement mechanism is for debriding the tissue site. The system further includes a sealing drape for placing over the tissue site and manifold member. The sealing drape is operable to form a fluid seal over the tissue site and manifold member. The system also includes a reduced-pressure subsystem for delivering a reduced pressure to the sealing drape. The system may further include a chemical-debridement subsystem. Other systems, manifolds, and methods are disclosed.

Oral treatment compositions containing an anti-adhesion agent, antibacterial agent and incompatible compound

The present invention encompasses an oral treatment composition containing an anti-adhesion agent, preferably a cysteine protease and most preferably ficin. In another aspect, the cysteine protease is in combination with one or more ingredients, such as antibacterial agent and surfactant. The anti-adhesion agent mitigates interaction between a subject oral cavity and plaque-forming materials.

PROCESS FOR THE ENZYMATIC SYNTHESIS OF ALKYL ESTERS OF PEPTIDES, PRODUCTS THUS OBTAINED, AND USE THEREOF

A method for enzymatically synthesizing peptide alkyl esters, wherein an animal or plant protein substrate is simultaneously contacted both with at least one enzyme having both proteolytic and esterolytic activity on proteins or peptides, and with at least one alcohol which is either entirely water-miscible or at least partially water-soluble. The method is characterized in that the simultaneous contacting of the protein substrate, the enzyme and the alcohol is performed at a pH which allows peptide alkyl esters to be formed.

Method and apparatus for analyzing biomolecules using raman spectroscopy

The present invention provides an apparatus having a sample separation unit, a Raman spectroscopy unit, and a mass spectrometry unit. The present invention further provides a method for specifying a biomolecule and a method for identifying the binding site of the biomolecule and the low-molecular-weight compound, comprising a combination of Raman spectroscopy and mass spectrometry. The present invention further provides a surface-enhanced Raman spectroscopy method with improved sensitivity.

A novel pharmaceutical preparation for preeclampsia, eclampsia, and toxemia and their related symptoms and related disorders of pregnancy

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and the method for preparing the therapeutic agents is disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or other method. Further, a method of using of a biomarker, the presence of chymotrypsin in the maternal GI tract to determine the likelihood of developing preeclampsia, pregnancy induced hypertension, and eclampsia/toxemia is disclosed.

Method for preparing new coffee aromas

The method is characterized in that a soja flour enzymatic proteolysis is carried out, the proteolisate is heated and the water soluble is isolated from the reaction product. Furthermore, are disclosed aromatic compositions characterized by their contents of said new coffee aromas, food stuff and other stimulants which contain such coffee aromas or said aromatic compositions, as well as the utilization of said new aromatic compositions or aromas for aromatizing food stuff and other stimulants or as coffee replacement substances.

Extraction method of collagen peptide from tremella

本发明公开了一种银耳胶原蛋白肽的提取方法，属于胶原蛋白肽制备技术领域。本发明以淀粉和磁性粉末制得固定化蛋白酶，将银耳作为原材料，经预处理后酶解，干燥，从而得到银耳胶原蛋白肽的提取方法。本发明工艺简便，原料易得，在制备过程中避免了漂白剂、氧化剂等化学试剂，对环境无任何污染问题，利用固定化蛋白酶代替游离蛋白酶，降低了生产成本，使得最终制得的蛋白酶产率高达90％以上、纯度高达95％以上，适合大规模应用。

Carboxymethyl chitosan/sodium alginate composite sponge immobilized papain and application thereof

本发明涉及一种羧甲基壳聚糖/海藻酸钠复合海绵固定化木瓜蛋白酶及其应用，所述固定化木瓜蛋白酶的制备方法如下：S1：将羧甲基壳聚糖溶液和海藻酸钠溶液混合得混合溶液，备用；用磷酸缓冲溶液溶解木瓜蛋白酶得木瓜蛋白酶溶液，备用；S2：于搅拌状态下将木瓜蛋白酶溶液加入所述混合溶液中，然后加入戊二醛溶液搅拌10～30min，然后再加入CaCl 2 溶液并搅拌10～30min，得固化混合液备用；S3：将S2所得固化混合溶液真空冷冻干燥，即得所述羧甲基壳聚糖/海藻酸钠复合海绵固定化木瓜蛋白酶；其中，S1中，所述木瓜蛋白酶溶液的酶活为500～700 U/mL；S2中，所述戊二醛溶液的浓度为1.0～1.6%。本发明提供的羧甲基壳聚糖/海藻酸钠复合海绵固定化木瓜蛋白酶具有较好的酶活力回收率和稳定性。

Method of treating toxemia

A therapeutic agent for the treatment of toxemia, preeclampsia and eclampsia and a method for preparing the therapeutic agent are disclosed. The therapeutic agent is a stable pharmaceutical preparation containing, but not limited to, digestive/pancreatic enzymes. The therapeutic agent may be manufactured by a variety of encapsulation technologies. Delivery of the therapeutic agent may be made orally, through injection, by adherence of a medicated patch or by other methods. Further, a method of using the presence of chymotrypsin in the maternal GI tract as a biomarker, to determine the likelihood of developing preeclampsia, a pregnancy induced hypertension, and eclampsia/toxemia is disclosed.

One kind is for improving infiltrative nanoparticle of tumor tissues and its preparation method and application

本发明属于用于治疗肿瘤的医药技术领域。本发明提供了一种用于提高肿瘤组织渗透性的纳米粒子，该纳米粒子的组成包括中空介孔普鲁士蓝纳米粒子、相变材料、肿瘤基质降解材料和抗肿瘤药物；所述相变材料包载于中空介孔普鲁士蓝纳米粒子的中空部分；所述肿瘤基质降解材料和抗肿瘤药物镶嵌于相变材料内部；所述相变材料为月桂酸、9‑十七烷酮、癸酸或1‑十四烷醇。本发明所提供的用于提高肿瘤组织渗透性的纳米粒子可使抗肿瘤药物进入肿瘤组织内部，其抑瘤率可达81.3％。

Methods and apparatus for producing partially hydrolysed proteinaceous products

Methods and apparatus for producing a particulate proteinaceous product are disclosed. Raw animal matter comminuted. Hydrolysing enzymes are added to preheated food-grade oil and added to the ground matter. The resulting suspension is preheated to hydrolysis temperature. Controlled hydrolysis of proteins in the suspension achieves a predetermined partial hydrolysis of the proteins to form a hydrolysate/oil suspension. At the desired level of hydrolysis the enzymes are heat-inactivated. Non-digestible solids are removed from the suspension and the suspension is pasteurized and partially dehydrated to concentrate the hydrolysate. Some of the oil is removed to form the product. The method and apparatus exhibit substantial resistance to equipment clogging.

Novel wet corn soaking process

本发明涉及一种新型湿法玉米浸泡工艺，包括如下步骤：将去胚玉米粉碎至20‑40目，加入水和磁性富勒烯固定化酶，于30‑50℃下搅拌浸泡5‑8小时后，通过磁分离回收磁性富勒烯固定化酶后，余下的浸泡混合物转入粉碎机中细粉碎，过200目筛后滤液静置过夜、离心分离、干燥得玉米淀粉。

Novel compositions for the treatment of cancer

The present invention relates to novel compositions comprising proteolytic enzymes and fining agents as well as methods for the treatment and/or prevention of cancer using these compositions.

Powder compsn. for treatment of dermatomycoses pedis, athletes foot - contains montmorillonite and opt. pyroligneous acid, papaya extract enzymes or lysozyme hydrochloride

Compsn. partic. for treatment of wet dermatomicosis pedis contains powdered montmorillonite opt. in association with pyroligneous acid, papaya extract enzyme or lysozyme hydrochloride. Pyroligneous acid is a by-prod. of wood distillation and is mainly acetic acid contg. other substances and has good permeability and bactericidal activity. Papaya extract enzyme is obtd. by drying the juice of papaya fruit which are not ripe. It contains papaine, chymopapain, protease etc. A pref. compsn. contains 80 pts. wt. montmorillonite, 20 pts. wt. of pyroligneous acid and a small amt. of papaine enzyme, pref. 0.02 wt. pts. A part of the pyroligneous acid may be opt. replaced by 0.5 pts. wt. lysozymehydrochloride.

Process for preparing proteins from a protein-containing substance

In a process for preparing proteins from a protein-containing substance, the substance is dispersed in an alkaline solvent with a pH of over 11.5 and at a temperature of under 30 °C. The proteins in the substance are thus dissolved. The resulting solution is then neutralised and the proteins in it are concentrated. To improve the profitability of the process in large-scale manufacture, the protein-containing substance is treated with a protease before dispersion in the alkaline solvent.

Tobacco protease genes

The invention provides protease genes which are regulated in a specific manner during curing of tobacco plants material and which affect the flavour of cured tobacco.

Topical pharmaceutical foam composition

Methods of treating neurological disorders

公开了一种治疗具有以存在二肽重复蛋白为特征的神经性病症的受试者的方法，所述方法包括使受试者的脑脊液(CSF)与能够去除或降解该毒性蛋白的试剂接触。

Method for extracting and separating bromelain from pineapple peels with reverse micelle having Gemini surfactant

以Gemini表面活性剂反胶束从菠萝皮中萃取分离菠萝蛋白酶的方法，属于生物工程中反胶束萃取技术领域，本发明采用具有季铵盐Gemini表面活性剂的反胶束对菠萝皮中的菠萝蛋白酶进行萃取，萃取过程中仅需少量的表面活性剂，通过控制前萃液的pH值既能使菠萝皮粗提液中的菠萝蛋白酶转移至反胶束，又能减少表面活性剂对菠萝蛋白酶的污染；通过调节正己烷和正己醇的比例，还能提高菠萝蛋白酶的活性。本发明操作过程简单，菠萝蛋白酶活性损失少，酶活性回收率较高，萃取后所得菠萝蛋白酶的活性回收率可达163%，纯化倍数可达到4。

Low fat meat paste