US20130216518A1 - Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis - Google Patents
Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis Download PDFInfo
- Publication number
- US20130216518A1 US20130216518A1 US13/519,534 US201113519534A US2013216518A1 US 20130216518 A1 US20130216518 A1 US 20130216518A1 US 201113519534 A US201113519534 A US 201113519534A US 2013216518 A1 US2013216518 A1 US 2013216518A1
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- United States
- Prior art keywords
- composition
- lipase
- candida
- enzyme
- triglycerides
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/465—Hydrolases (3) acting on ester bonds (3.1), e.g. lipases, ribonucleases
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/04—Anorexiants; Antiobesity agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/06—Antihyperlipidemics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
Definitions
- the present invention relates to a composition comprising a combination of at least one proteolytic enzyme, such as subtilisin, and at least one lipolytic enzyme, for use in preventing triglyceride synthesis, advantageously by degrading 2-monoacylglycerol in the intestine.
- the composition of the present invention comprises several lipases.
- the invention also relates to such a composition for use as a drug, cosmetic agent, medical device, dietary composition, dietary supplement or nutraceutical, notably for use in preventing or treating obesity, atherosclerosis, type 2 diabetes or for use in preventing or reducing excess weight.
- Metabolic syndrome represents a set of factors that occur simultaneously and increase the risk of cardiovascular disease, stroke and type 2 diabetes. Having only one of these factors—increase in blood pressure, high insulin level, excess fat around the waist or abnormal cholesterol level—increases the risk of contracting a serious illness; when several factors combine, the risk is even greater.
- Fats by their physical, chemical and physiological properties, play an important role in man's nutrition. In addition to the fats ingested by man in the form of food, the body itself manufactures lipids.
- Dietary fats, and fats of adipose tissue are primarily comprised of triglycerides.
- a triglyceride is a glycerol molecule with three fatty acids bound to it. Triglycerides are classified as lipids (fats), but only the three fatty acids are fats, as glycerol is a polyol that belongs rather to the class of carbohydrates. For example, glycerol is soluble in water and not in oil; glycerol is thus not a fat.
- Lipolytic lipases or enzymes are enzymes secreted in the mouth, stomach and pancreas that cut triglycerides (TAG) into molecules small enough to be assimilable.
- TAG triglycerides
- lipases attack triglycerides (TAG) only at positions 1 and 3 of the glycerol, leading to the formation of free fatty acids and 2-monoacylglycerol (glycerol molecule comprising one fatty acid bound at position 2).
- lipase activity is greater, even free fatty acids and glycerol can be obtained. All these molecules are assimilable by the body.
- This triglyceride (TAG) reformation is achieved in particular by the activity of four enzymes (acyl-CoA synthetase, monoglyceride transacylase, diglyceride transacylase and diglyceride synthetase) which act as several stages of the synthesis.
- enzymes acyl-CoA synthetase, monoglyceride transacylase, diglyceride transacylase and diglyceride synthetase
- Free fatty acids then will be bound to 2-monoacylglycerol in positions 1 and 3, which will reform triglycerides.
- These triglycerides which are not soluble in the blood, will have to integrate chylomicrons which will evolve to VLDL, LDL and HDL and will transport throughout the body triglycerides (TAG), cholesterol and phospholipids.
- adipocytes fat cells
- the body does not use their energy immediately since they are stored in adipocytes.
- the body cannot metabolize fatty acids when they are bound to glycerol, as in triglycerides. To be metabolized, fatty acids must be free.
- glucose which is omnipresent in the body. This is what makes us say that humans are hybrid vehicles. But glucose, in contrast to fatty acids, has many disadvantages:
- glucose to be used and to penetrate cells, needs the hormone insulin. Also, for glucose to penetrate all its cells, the body must secrete even more insulin, beyond its capacities, and under extreme conditions. Thus at some point the body and in particular the pancreas can no longer secrete so much insulin, giving rise to the phenomenon of insulin resistance; glucose accumulates in the blood and can no longer penetrate the cells. This is called glucose intolerance; the body becomes insulin-resistant.
- This hyperinsulinemia has perverse effects; too much insulin keeps fatty acids from exiting fat cells, which is called lipolysis. There is thus a still greater deficiency in fatty acids available to be used; since no more fatty acids are leaving fat cells, there is no possibility of losing weight notably for those suffering from obesity. Thus, the deficiency in available fatty acids is still greater, and glucose is used even more intensely in metabolism, from where still other complications arise, such as an increase in triglyceridemia and cholesterolemia.
- Substances notably used to that end include flavonoid-rich tea extract to block the enzyme O′-methyltransferase which destroys adrenalin, or flavan-3-ol-rich grape seed extract and bioflavonoid-rich pine bark, the latter both increasing thermogenesis, i.e., releasing fatty acids from fat cells; similarly, polyphenols extracted from cocoa have the same effect.
- CLA conjugated linoleic acid
- TAG triacylglycerol
- the Applicant sought to find a better means of confronting metabolic syndrome, fighting the obesity gene and using the energy of fats all while not promoting the formation of fat deposits.
- the solution proposed by the present invention is to inhibit, reduce and/or prevent the reformation of triglycerides in the enterocytes or cells of the intestine of the body by the use of a combination of proteolytic enzyme or protease with at least one lipolytic enzyme or lipase.
- proteolytic enzymes disrupt the activity of the four enzymes (acyl-CoA synthetase, monoglyceride transacylase, diglyceride transacylase and diglyceride synthetase) in the enterocyte, which help triglyceride resynthesis,
- the present invention thus has as an object a composition comprising a combination of at least one proteolytic enzyme or protease and at least one lipolytic enzyme or lipase for its use in preventing the synthesis or the reformation of triglycerides, notably in the enterocytes or cells of the intestine, advantageously by degrading 2-monoacylglycerol.
- the proteolytic enzyme is selected from the group comprising subtilisin, nagarse, nattokinase, chymotrypsin, trypsin, elastase, thermolysin, serrapeptase, and mixtures thereof.
- the proteolytic enzyme is subtilisin or nattokinase or a mixture of subtilisin or nattokinase with one or more other proteolytic enzymes.
- the proteolytic enzyme is present in a proportion of 5-30% by weight, typically 10-20% by weight, in relation to the total weight of the composition.
- the lipolytic enzyme is present in a proportion of 70-95% by weight, typically 80-90% by weight, in relation to the total weight of the composition.
- the composition enables the administration of a daily dose of proteolytic enzyme ranging between 10 mg and 200 mg, more particularly between 10 mg and 100 mg, typically between 20 mg and 100 mg, for example between 50 mg and 100 mg.
- the composition enables the administration of a daily dose of lipolytic enzyme ranging between 100 mg and 400 mg, more particularly between 100 mg and 300 mg, typically between 100 mg and 200 mg or 200 mg and 300 mg.
- the composition is formulated to be administered orally.
- the composition is provided in the form of a hard or soft capsule, tablet, granule, powder or oral solution.
- the composition is provided in the form of a hard or soft capsule or a gastro-resistant tablet.
- the composition is gastro-resistant so that the composition releases the proteolytic enzyme and the lipolytic enzyme in the intestine.
- the composition is a pharmaceutical, cosmetic, nutraceutical or dietary composition, a dietary supplement, or a medical device, and can comprise any carrier or suitable excipient, acceptable from a pharmaceutical, cosmetic, dietary or nutraceutical point of view, as well as conventional additives, known to the person skilled in the art.
- the composition comprises at least one lipase, such as a lipase extracted from Thermomyces lanuginosus, Rhizopus niveus, Penicillium roqueforti, Penicillium camemberti, Geotrichum candidum, Candida rugosa, Candida lipolytica, Candida parapsilosis, Aspergillus niger, Rhizopus oryzae, Mucor javanicus , or a lipase from Candida anthartica, Geotrichum candidum or a lipase extracted from oats, as well as mixtures thereof.
- a lipase such as a lipase extracted from Thermomyces lanuginosus, Rhizopus niveus, Penicillium roqueforti, Penicillium camemberti, Geotrichum candidum, Candida rugosa, Candida lipolytica, Candida parapsilosis, Aspergillus niger, Rhizopus oryzae
- the composition comprises several lipases.
- the lipases used in the context of the present invention are active at position 2 on the triglycerides and will reduce 2-monoacylglycerol and prevent triglycerides from forming again, a pathway that produces 80% of triglycerides.
- the composition comprises at least one lipase selected from the group comprising Cal A or Cal B lipase of Candida anthartica, Geotrichum candidum, Candida rugosa , and binary or ternary mixtures of these lipases.
- the composition comprises a mixture of Cal A or Cal B of Candida anthartica, Geotrichum candidum and Candida rugosa.
- the composition of the present invention is intended for use in preventing or reducing excess weight, adipogenesis or excess cholesterol, or as an anti-cellulite agent, typically in a cosmetic composition or a medical device.
- composition or the product of the present invention is intended for use in preventing or treating obesity or atherosclerosis, or cardiovascular disorders, or type 2 diabetes, and in general what is referred to as metabolic syndrome, to fight the obesity gene.
- the present invention also has as an object a composition or a product containing:
- the proteolytic enzyme is selected from the group comprising subtilisin, nagarse, nattokinase, chymotrypsin, trypsin, elastase, thermolysin, serrapeptase, and mixtures thereof.
- the lipase is extracted from Thermomyces lanuginosus, Rhizopus niveus, Penicillium roqueforti, Penicillium camemberti, Geotrichum candidum, Candida rugosa, Candida Candida parapsilosis, Aspergillus niger, Rhizopus oryzae, Mucor javanicus , or is extracted from Candida anthartica, Geotrichum candidum or from oats.
- the proteases are typically administered in the form of a gelatin capsule.
- the proteases are advantageously administered two to three times per day, one gelatin capsule with each meal.
- the product comprises at least one lipase of Candida anthartica such as lipase Cal A or Cal B of Candida anthartica, a Geotrichum candidum lipase, a Candida rugosa lipase and/or a lipase extracted from oats.
- lipases act at position 2 on the triglycerides and thus break down 2-monoacylglycerol and help proteases prevent triglycerides from reforming in the body. Without 2-monoacylglycerol, TAG resynthesis is much more difficult (remember that this pathway produces 80% of the TAG in the body).
- the lipases are typically administered in the form of a gelatin capsule.
- the lipases are advantageously administered three times per day, one gelatin capsule with each meal.
- composition or the product of the present invention is intended for use as a drug, cosmetic agent, medical device, dietary composition, nutraceutical or dietary supplement.
- composition or the product of the present invention is intended for its use in preventing or reducing excess weight, adipogenesis or excess cholesterol, or as an anti-cellulite agent.
- composition or the product of the present invention is intended for its use in preventing or treating obesity, atherosclerosis, cardiovascular disorders, or type 2 diabetes, and in general what is referred to as metabolic syndrome, in order to fight the obesity gene.
- the first condition, the control group, did not receive any active product.
- the other two conditions each comprising groups of 10 rats, received for 8 days (once per day), respectively, a mixture of 50 mg of subtilisin and 100 mg of Cal A lipase of Candida anthartica for group 1, and a mixture of 50 mg of subtilisin and 50 mg of Geotrichum candidum lipase, as well as 50 mg of Candida rugosa lipase for group 2.
- Groups 1 and 2 did not have TAG in the blood.
- Olive oil was then administered twice again at a one-week interval—conditions 1 and 2 all the while continuing to receive subtilisin in combination with the lipases mentioned above.
- TAG did not reform in groups 1 and 2, whereas the control group had a high concentration of TAG in the blood, for the three samples.
- subtilisin and lipases prevented the formation of triglycerides (TAG).
- the control pig did not receive enzyme.
- the three other conditions received three formulas of enzymes.
- Formula 1 was composed of 10 mg of subtilisin and 300 mg Cal A lipase, as well as pancreatin. It was administered to the pigs of group 1 at a dose of 20 mg/kg.
- Formula 2 was composed of 10 mg of subtilisin and 300 mg of Candida rugosa lipase, as well as pancreatin. It was administered to the pigs of group 2 at a dose of 40 mg/kg.
- Formula 3 was composed of 10 mg of subtilisin and 300 mg of Geotrichum candidum lipase, as well as pancreatin. It was administered to the pigs of group 3 at a dose of 40 mg/kg.
- the two remaining pigs per batch received the same enzyme formulas as those mentioned above.
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- Life Sciences & Earth Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Diabetes (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Obesity (AREA)
- Hematology (AREA)
- Emergency Medicine (AREA)
- Endocrinology (AREA)
- Child & Adolescent Psychology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Vascular Medicine (AREA)
- Urology & Nephrology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Plant Substances (AREA)
- Medicinal Preparation (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Enzymes And Modification Thereof (AREA)
- Cosmetics (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR1058957 | 2010-10-29 | ||
FR1058957A FR2966734B1 (fr) | 2010-10-29 | 2010-10-29 | Composition comprenant au moins une enzyme proteolytique pour son utilisation pour empecher la synthese des triglycerides |
PCT/EP2011/069045 WO2012056024A1 (fr) | 2010-10-29 | 2011-10-28 | Composition comprenant en association au moins une enzyme protéolytique et au moins une enzyme lipolytique pour son utilisation pour empêcher la synthèse des triglycérides |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/EP2011/069045 A-371-Of-International WO2012056024A1 (fr) | 2010-10-29 | 2011-10-28 | Composition comprenant en association au moins une enzyme protéolytique et au moins une enzyme lipolytique pour son utilisation pour empêcher la synthèse des triglycérides |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US13/900,084 Continuation US9375461B2 (en) | 2010-10-29 | 2013-05-22 | Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis |
Publications (1)
Publication Number | Publication Date |
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US20130216518A1 true US20130216518A1 (en) | 2013-08-22 |
Family
ID=43759412
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US13/519,534 Abandoned US20130216518A1 (en) | 2010-10-29 | 2011-10-28 | Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis |
US13/900,084 Active US9375461B2 (en) | 2010-10-29 | 2013-05-22 | Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US13/900,084 Active US9375461B2 (en) | 2010-10-29 | 2013-05-22 | Composition comprising a combination of at least one proteolytic enzyme and at least one lipolytic enzyme, for use in preventing triglyceride synthesis |
Country Status (14)
Country | Link |
---|---|
US (2) | US20130216518A1 (ja) |
EP (1) | EP2504026B1 (ja) |
JP (1) | JP5834027B2 (ja) |
CN (1) | CN102811731A (ja) |
AU (1) | AU2011322462C1 (ja) |
BR (1) | BR112012015925A2 (ja) |
CA (1) | CA2785887C (ja) |
ES (1) | ES2537716T3 (ja) |
FR (1) | FR2966734B1 (ja) |
MX (1) | MX340828B (ja) |
NZ (1) | NZ600966A (ja) |
PL (1) | PL2504026T3 (ja) |
RU (1) | RU2536295C2 (ja) |
WO (1) | WO2012056024A1 (ja) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB201115417D0 (en) | 2011-09-06 | 2011-10-19 | Ip Science Ltd | Products and methods |
US8268305B1 (en) * | 2011-09-23 | 2012-09-18 | Bio-Cat, Inc. | Method and compositions to reduce serum levels of triacylglycerides in human beings using a fungal lipase |
KR102011556B1 (ko) * | 2016-07-19 | 2019-08-16 | 연세대학교 산학협력단 | 2-모노아실글리세롤 절단 효소를 포함하는 간지방증 또는 비알코올성 지방간의 예방, 개선 또는 치료용 조성물 |
CN107375914A (zh) * | 2017-09-18 | 2017-11-24 | 郭恒立 | 一种治疗ⅱ型糖尿病及并发症的中药贴膏制备和使用方法 |
Citations (2)
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US6699496B1 (en) * | 1998-12-04 | 2004-03-02 | Amano Enzyme Inc. | Enzyme in a dosage form for oral use in mammals, enzyme-containing food material and method for administering the enzyme in a dosage form |
US20090299093A1 (en) * | 2005-12-21 | 2009-12-03 | Pfizer Inc. | Preparation of Gamma-Amino Acids Having Affinity for The Alpha-2-Delta Protein |
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US5618710A (en) * | 1990-08-03 | 1997-04-08 | Vertex Pharmaceuticals, Inc. | Crosslinked enzyme crystals |
IS4130A (is) | 1993-03-01 | 1994-09-02 | Ab Astra | Ný fjölpeptíð |
JP2711436B2 (ja) * | 1995-02-22 | 1998-02-10 | マルホ株式会社 | アレルギー治療剤及びアレルギー対応食品 |
FR2758143B1 (fr) * | 1997-01-07 | 1999-02-19 | Laphal Laboratoire De Pharmaco | Inhibiteurs specifiques de la lipase pancreatique et leurs applications |
US20030095961A1 (en) * | 1998-02-13 | 2003-05-22 | Devin Houston | Composition and method for treating disease by increasing activated alpha2 macroglobulin in the blood and extravascular tissue |
JP2001220134A (ja) * | 2000-02-14 | 2001-08-14 | S F C:Kk | 天日塩とその製造方法とその製造装置ならびに酵素入り天日塩とその製造方法 |
RU2213557C2 (ru) * | 2001-12-26 | 2003-10-10 | Закрытое акционерное общество "Аксис" | Фармацевтическая композиция, обладающая тромболитическими, противовоспалительными и цитопротективными свойствами |
AU2003212195A1 (en) * | 2002-02-06 | 2003-09-02 | N-Zyme Biotec Gmbh | Protease screening and novel use of proteases |
JP4309108B2 (ja) * | 2002-09-26 | 2009-08-05 | 大和薬品株式会社 | 糖尿病治療薬 |
FR2848847B1 (fr) * | 2002-12-18 | 2005-10-14 | Coletica | Composition cosmetique ou dermopharmaceutique comprenant une enzyme insoluble en milieu aqueux, ainsi que ses utilisations |
US20050003027A1 (en) | 2003-05-09 | 2005-01-06 | Diaz Jose A. | Chemical composition and method to bind fat, enhance metabolization, and aid digestion |
US20050059567A1 (en) * | 2003-09-11 | 2005-03-17 | The Procter & Gamble Company | Methods of formulating enzyme cocktails, enzyme cocktails for the removal of egg-based and grass-based stains and/or soils, compositions and products comprising same |
UA91521C2 (ru) * | 2004-10-14 | 2010-08-10 | Элтус Фармасьютикалз Инк. | Композиции, содержащие липазу, протеазу и амилазу, предназначенные для лечения недостаточности поджелудочной железы |
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NZ593831A (en) * | 2009-01-06 | 2013-09-27 | Curelon Llc | Compositions and methods for the treatment or prevention of staphylococcus aureus infections and for the eradication or reduction of staphylococcus aureus on surfaces |
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2010
- 2010-10-29 FR FR1058957A patent/FR2966734B1/fr not_active Expired - Fee Related
-
2011
- 2011-10-28 NZ NZ600966A patent/NZ600966A/en not_active IP Right Cessation
- 2011-10-28 EP EP11778574.1A patent/EP2504026B1/fr active Active
- 2011-10-28 JP JP2012555449A patent/JP5834027B2/ja not_active Expired - Fee Related
- 2011-10-28 WO PCT/EP2011/069045 patent/WO2012056024A1/fr active Application Filing
- 2011-10-28 US US13/519,534 patent/US20130216518A1/en not_active Abandoned
- 2011-10-28 MX MX2012007670A patent/MX340828B/es active IP Right Grant
- 2011-10-28 ES ES11778574.1T patent/ES2537716T3/es active Active
- 2011-10-28 RU RU2012126983/15A patent/RU2536295C2/ru not_active IP Right Cessation
- 2011-10-28 AU AU2011322462A patent/AU2011322462C1/en not_active Ceased
- 2011-10-28 PL PL11778574T patent/PL2504026T3/pl unknown
- 2011-10-28 CN CN201180005178XA patent/CN102811731A/zh active Pending
- 2011-10-28 BR BR112012015925A patent/BR112012015925A2/pt not_active IP Right Cessation
- 2011-10-28 CA CA2785887A patent/CA2785887C/fr not_active Expired - Fee Related
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2013
- 2013-05-22 US US13/900,084 patent/US9375461B2/en active Active
Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6699496B1 (en) * | 1998-12-04 | 2004-03-02 | Amano Enzyme Inc. | Enzyme in a dosage form for oral use in mammals, enzyme-containing food material and method for administering the enzyme in a dosage form |
US20090299093A1 (en) * | 2005-12-21 | 2009-12-03 | Pfizer Inc. | Preparation of Gamma-Amino Acids Having Affinity for The Alpha-2-Delta Protein |
Also Published As
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BR112012015925A2 (pt) | 2017-03-14 |
JP5834027B2 (ja) | 2015-12-16 |
NZ600966A (en) | 2014-10-31 |
RU2536295C2 (ru) | 2014-12-20 |
AU2011322462B9 (en) | 2014-02-13 |
CA2785887A1 (fr) | 2012-05-03 |
EP2504026B1 (fr) | 2015-04-08 |
PL2504026T3 (pl) | 2015-11-30 |
CA2785887C (fr) | 2016-04-19 |
WO2012056024A1 (fr) | 2012-05-03 |
US20130323219A1 (en) | 2013-12-05 |
MX2012007670A (es) | 2012-11-21 |
RU2012126983A (ru) | 2014-01-20 |
FR2966734A1 (fr) | 2012-05-04 |
CN102811731A (zh) | 2012-12-05 |
AU2011322462B2 (en) | 2014-01-09 |
US9375461B2 (en) | 2016-06-28 |
JP2013521262A (ja) | 2013-06-10 |
ES2537716T3 (es) | 2015-06-11 |
MX340828B (es) | 2016-07-26 |
FR2966734B1 (fr) | 2014-07-18 |
AU2011322462A1 (en) | 2012-07-19 |
EP2504026A1 (fr) | 2012-10-03 |
AU2011322462C1 (en) | 2014-04-03 |
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