JP2013516431A - 大豆加工ストリームから単離される精製Ｋｕｎｉｔｚトリプシンインヒビタータンパク質 - Google Patents
大豆加工ストリームから単離される精製Ｋｕｎｉｔｚトリプシンインヒビタータンパク質 Download PDFInfo
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- 230000000813 microbial effect Effects 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- VBEGHXKAFSLLGE-UHFFFAOYSA-N n-phenylnitramide Chemical compound [O-][N+](=O)NC1=CC=CC=C1 VBEGHXKAFSLLGE-UHFFFAOYSA-N 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000013500 performance material Substances 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000000886 photobiology Effects 0.000 description 1
- 229940085127 phytase Drugs 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920006393 polyether sulfone Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- KCXFHTAICRTXLI-UHFFFAOYSA-N propane-1-sulfonic acid Chemical compound CCCS(O)(=O)=O KCXFHTAICRTXLI-UHFFFAOYSA-N 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 229940076372 protein antagonist Drugs 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 235000019192 riboflavin Nutrition 0.000 description 1
- 239000002151 riboflavin Substances 0.000 description 1
- 229960002477 riboflavin Drugs 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 239000002210 silicon-based material Substances 0.000 description 1
- 230000037370 skin discoloration Effects 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
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- 229960004072 thrombin Drugs 0.000 description 1
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- 229910052721 tungsten Inorganic materials 0.000 description 1
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- 239000002351 wastewater Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/185—Vegetable proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
- A23J3/16—Vegetable proteins from soybean
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Pharmacology & Pharmacy (AREA)
- Organic Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Nutrition Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Neurology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Dermatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Peptides Or Proteins (AREA)
- Dairy Products (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US29131209P | 2009-12-30 | 2009-12-30 | |
| US61/291,312 | 2009-12-30 | ||
| PCT/US2010/062592 WO2011082359A1 (en) | 2009-12-30 | 2010-12-30 | Purified kunitz trypsin inhibitor proteins isolated from a soy processing stream |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
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| JP2015118467A Division JP2015157873A (ja) | 2009-12-30 | 2015-06-11 | 大豆加工ストリームから単離される精製Ｋｕｎｉｔｚトリプシンインヒビタータンパク質 |
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| JP2013516431A true JP2013516431A (ja) | 2013-05-13 |
| JP2013516431A5 JP2013516431A5 (https=) | 2014-02-27 |
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| JP2012547317A Pending JP2013516432A (ja) | 2009-12-30 | 2010-12-30 | 大豆加工ストリームからＫｕｎｉｔｚトリプシンインヒビタータンパク質を回収する方法 |
| JP2012547311A Pending JP2013516429A (ja) | 2009-12-30 | 2010-12-30 | ボーマン・バークインヒビタープロテインを大豆加工ストリームから回収する方法 |
| JP2012547309A Pending JP2013516427A (ja) | 2009-12-30 | 2010-12-30 | 大豆加工ストリームから単離される精製ボーマン・バークプロテアーゼインヒビタープロテイン |
| JP2015118467A Abandoned JP2015157873A (ja) | 2009-12-30 | 2015-06-11 | 大豆加工ストリームから単離される精製Ｋｕｎｉｔｚトリプシンインヒビタータンパク質 |
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| JP2012547311A Pending JP2013516429A (ja) | 2009-12-30 | 2010-12-30 | ボーマン・バークインヒビタープロテインを大豆加工ストリームから回収する方法 |
| JP2012547309A Pending JP2013516427A (ja) | 2009-12-30 | 2010-12-30 | 大豆加工ストリームから単離される精製ボーマン・バークプロテアーゼインヒビタープロテイン |
| JP2015118467A Abandoned JP2015157873A (ja) | 2009-12-30 | 2015-06-11 | 大豆加工ストリームから単離される精製Ｋｕｎｉｔｚトリプシンインヒビタータンパク質 |
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| EP (5) | EP2519245A4 (https=) |
| JP (5) | JP2013516431A (https=) |
| CN (6) | CN102770439A (https=) |
| BR (2) | BR112012016232A2 (https=) |
| CA (2) | CA2785599A1 (https=) |
| WO (5) | WO2011082335A2 (https=) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ588603A (en) | 2008-03-26 | 2012-03-30 | Oramed Ltd | Methods and compositions for oral administration of a protein of up to 100000 Daltaons, a first protease inhibitor and a second protease inhibitor wherein said protease inhibitors inhibit trypsin |
| US20140141126A1 (en) * | 2011-06-29 | 2014-05-22 | Solae Llc | Baked food compositions comprising soy whey proteins that have been isolated from processing streams |
| CN113769074A (zh) * | 2012-02-01 | 2021-12-10 | 奥拉姆德有限公司 | 含有蛋白酶抑制物的组合物、包含前者的组合物和用于产生和使用前者的方法 |
| BR112015001566A2 (pt) * | 2012-07-26 | 2017-07-04 | Dupont Nutrition Biosci Aps | agente de formação de espuma, produto alimentício, método para a fabricação de um produto alimentício e agente de formação de espuma estabilizado. |
| EP2877249A2 (en) * | 2012-07-26 | 2015-06-03 | Solae, LLC | Emulsifying agent for use in personal care products and industrial products |
| EP2877040A1 (en) * | 2012-07-26 | 2015-06-03 | Solae, LLC | Emulsifying agent for use in food compositions |
| EP2877063A2 (en) * | 2012-07-26 | 2015-06-03 | Solae, LLC | Foaming agent for use in personal care products and industrial products |
| BR112015008661A2 (pt) | 2012-10-23 | 2017-07-04 | Upfront Chromatography As | processos de separação para proteína de soja |
| WO2014106846A2 (en) | 2013-01-03 | 2014-07-10 | Oramed Ltd. | Methods and compositions for treating nafld, hepatic steatosis, and sequelae thereof |
| FR3001362B1 (fr) | 2013-01-31 | 2015-07-10 | Roquette Freres | Procede de fractionnement des solubles de pois, fractions obtenues et leur valorisation |
| CN103392907B (zh) * | 2013-06-08 | 2014-12-17 | 东北农业大学 | 酶法修饰改善乳清蛋白纳米纤维聚合量的方法 |
| WO2015101435A1 (en) * | 2013-12-30 | 2015-07-09 | Koninklijke Philips N.V. | A method of making soymilk |
| CN105939618A (zh) * | 2014-01-29 | 2016-09-14 | 预层析股份有限公司 | 豌豆蛋白的新型分离方法 |
| CN103933548A (zh) * | 2014-04-17 | 2014-07-23 | 中国药科大学 | 露那辛多肽在防治白内障药物中的应用 |
| US11291221B2 (en) | 2015-10-30 | 2022-04-05 | Beth Israel Deaconess Medical Center, Inc. | Methods for determination of bioactivity, quantity, removal, or inactivation of cereal amylase trypsin inhibitors in cereals, flours, plants, and complex foods |
| US10858390B2 (en) * | 2016-09-02 | 2020-12-08 | Cem Corporation | Use of excess carbodiimide for peptide synthesis at elevated temperatures |
| EP3599881A4 (en) | 2017-03-31 | 2021-02-17 | J.R. Simplot Company | POTATO PROTEIN POWDER |
| CN107488226A (zh) * | 2017-09-06 | 2017-12-19 | 成都晟博源生物工程有限公司 | 一种大豆胰蛋白酶抑制剂的提取方法 |
| CN110872140B (zh) * | 2018-09-03 | 2022-06-21 | 中国石油化工股份有限公司 | 危化品分离回收系统 |
| CN110104754B (zh) * | 2019-04-03 | 2022-03-29 | 江苏农林职业技术学院 | 一种豆制品废水废渣处理甲基橙染料废水的方法 |
| CN110551209A (zh) * | 2019-08-27 | 2019-12-10 | 合肥天汇孵化科技有限公司 | 一种基于大豆深加工废液以豆清水为原料粗提sbti蛋白工艺 |
| EP4061826A1 (en) * | 2019-11-20 | 2022-09-28 | CSL Behring AG | Method for extracting a protein from a precipitate and method for precipitating impurities |
| US20210259281A1 (en) * | 2020-02-26 | 2021-08-26 | Eat Just, Inc. | Pulse Protein Isolation by Ultrafiltration |
| JP2023528657A (ja) * | 2020-06-12 | 2023-07-05 | ビーエーエスエフ ソシエタス・ヨーロピア | 発酵ブロスの改善された脱塩及び例えばオリゴ糖のファインケミカルの精製 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0285204A (ja) * | 1988-04-11 | 1990-03-26 | Monsanto Co | 昆虫毒素効果の増強法 |
| JPH1066572A (ja) * | 1996-08-29 | 1998-03-10 | Showa Sangyo Co Ltd | 高純度の大豆トリプシンインヒビターの製造方法 |
| US20030018990A1 (en) * | 2001-03-30 | 2003-01-23 | Stewart C. Neal | Cabbage proteinase inhibitor gene confers resistance against plant pests |
| US20050153399A1 (en) * | 2003-11-06 | 2005-07-14 | Hans De Nobel | Expression in filamentous fungi of protease inhibitors and variants thereof |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4368151A (en) * | 1981-08-10 | 1983-01-11 | A. E. Staley Manufacturing Company | 7S And 11S vegetable protein fractionation and isolation |
| US5288856A (en) * | 1986-11-20 | 1994-02-22 | Pierre Amiguet | Method of isolating acid-stable, biologically active proteins |
| US4808314A (en) * | 1987-09-18 | 1989-02-28 | Scripps Clinic And Research Foundation | Method for reducing bacterial endotoxin contamination in solutions of macromolecules |
| US5250515A (en) * | 1988-04-11 | 1993-10-05 | Monsanto Company | Method for improving the efficacy of insect toxins |
| JPH06145198A (ja) * | 1992-03-30 | 1994-05-24 | Shokuhin Sangyo High Separeeshiyon Syst Gijutsu Kenkyu Kumiai | 大豆トリプシンインヒビターの製造方法 |
| DK46793D0 (da) * | 1993-04-26 | 1993-04-26 | Novo Nordisk As | Enzym |
| US6313273B1 (en) * | 1999-08-25 | 2001-11-06 | Abbott Laboratories | Soy proteins and methods for their production |
| US7175869B2 (en) * | 2000-11-30 | 2007-02-13 | Kraft Foods Holdings, Inc. | Method of deflavoring soy-derived materials using electrodialysis |
| US6787173B2 (en) * | 2000-11-30 | 2004-09-07 | Kraft Foods Holdings, Inc. | Method of deflavoring soy-derived materials |
| CN1150831C (zh) * | 2001-01-19 | 2004-05-26 | 北京中联捷思科技发展有限公司 | 超滤提取大豆乳清蛋白的方法 |
| US7214394B2 (en) * | 2002-05-31 | 2007-05-08 | Archer-Daniels-Midland Company | Policosanol compositions, extraction from novel sources, and uses thereof |
| CN100506062C (zh) * | 2002-08-28 | 2009-07-01 | 不二制油株式会社 | 酸性大豆蛋白质凝胶食物及其生产方法 |
| WO2004104036A1 (ja) * | 2003-05-21 | 2004-12-02 | Fuji Oil Company, Limited | 大豆ホエー蛋白及び大豆ホエー蛋白分解物の製造法 |
| US20070277269A1 (en) * | 2006-04-17 | 2007-11-29 | Ceres, Inc. | Nucleotide sequences and polypeptides encoded thereby useful for modifying plant characteristics |
| CN1901811A (zh) * | 2003-11-05 | 2007-01-24 | 凯里集团服务国际有限公司 | 酸稳定大豆蛋白与强化食品或饮料 |
| ATE482972T1 (de) * | 2003-11-06 | 2010-10-15 | Danisco Us Inc | Tgf-beta1-bindende und geträgerte peptide |
| CN1615722A (zh) * | 2003-11-14 | 2005-05-18 | 哈高科大豆食品有限责任公司 | 超滤膜分离技术制备大豆分离蛋白的方法 |
| CN1921770A (zh) * | 2004-02-26 | 2007-02-28 | 不二制油株式会社 | 含大豆蛋白的溶液和凝胶 |
| WO2005082389A1 (ja) * | 2004-02-27 | 2005-09-09 | Fuji Oil Company, Limited | 癌転移抑制組成物 |
| US20060057275A1 (en) * | 2004-09-16 | 2006-03-16 | Shaowen Wu | Process for the preparation of glycinin-rich and beta-conglycinin-rich protein fractions |
| US9084734B2 (en) * | 2005-05-05 | 2015-07-21 | Danisco Us Inc. | Peptide personal care compositions and methods for their use |
| US20070054031A1 (en) * | 2005-09-02 | 2007-03-08 | Keshun Liu | Methods of extracting, concentrating and fractionating proteins and other chemical components |
| TWI257723B (en) * | 2005-09-15 | 2006-07-01 | Epitech Technology Corp | Vertical light-emitting diode and method for manufacturing the same |
| US20080182002A1 (en) * | 2007-01-26 | 2008-07-31 | Solae, Llc | Processes for Removing Bitter Components from Soy Protein Isolates |
| BRPI0811788A2 (pt) * | 2007-07-03 | 2014-10-07 | Solae Llc | Composição de proteína vegetal, processo para a fabricação de uma composição de proteína vegetal e produto alimentício |
| CN101367018A (zh) * | 2007-09-13 | 2009-02-18 | 中国海洋大学 | 壳聚糖树脂固定化酶纯化大豆乳清废水中胰蛋白酶抑制剂的工艺 |
| BRPI0823193A2 (pt) * | 2008-10-15 | 2019-09-24 | Danisco Us Inc | inibidores de protease de bowman birk variantes modificados |
-
2010
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2015
- 2015-06-11 JP JP2015118467A patent/JP2015157873A/ja not_active Abandoned
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0285204A (ja) * | 1988-04-11 | 1990-03-26 | Monsanto Co | 昆虫毒素効果の増強法 |
| JPH1066572A (ja) * | 1996-08-29 | 1998-03-10 | Showa Sangyo Co Ltd | 高純度の大豆トリプシンインヒビターの製造方法 |
| US20030018990A1 (en) * | 2001-03-30 | 2003-01-23 | Stewart C. Neal | Cabbage proteinase inhibitor gene confers resistance against plant pests |
| US20050153399A1 (en) * | 2003-11-06 | 2005-07-14 | Hans De Nobel | Expression in filamentous fungi of protease inhibitors and variants thereof |
Non-Patent Citations (2)
| Title |
|---|
| JPN6015009685; Ａｎａｌｙｔｉｃａｌ Ｂｉｏｃｈｅｍｉｓｔｒｙ Ｖｏｌ．３００， Ｎｏ．１, 2002, ｐ．１１-１４ * |
| JPN6015009687; Ｅｕｒｏｐｅａｎ Ｊｏｕｒｎａｌ ｏｆ Ｂｉｏｃｈｅｍｉｓｔｒｙ Ｖｏｌ．３２, 1973, ｐ．４１７-４３１ * |
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