WO2006052003A1 - エンドウホエー由来の可溶性ポリペプチド、発泡剤及びその製造方法 - Google Patents
エンドウホエー由来の可溶性ポリペプチド、発泡剤及びその製造方法 Download PDFInfo
- Publication number
- WO2006052003A1 WO2006052003A1 PCT/JP2005/021064 JP2005021064W WO2006052003A1 WO 2006052003 A1 WO2006052003 A1 WO 2006052003A1 JP 2005021064 W JP2005021064 W JP 2005021064W WO 2006052003 A1 WO2006052003 A1 WO 2006052003A1
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- WO
- WIPO (PCT)
- Prior art keywords
- molecular weight
- whey
- polypeptide
- foaming
- concentrate
- Prior art date
Links
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 54
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 54
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 54
- 239000005862 Whey Substances 0.000 title claims abstract description 35
- 102000007544 Whey Proteins Human genes 0.000 title claims abstract description 35
- 108010046377 Whey Proteins Proteins 0.000 title claims abstract description 35
- 239000004088 foaming agent Substances 0.000 title claims abstract description 22
- 238000000034 method Methods 0.000 title abstract description 14
- 239000012528 membrane Substances 0.000 claims abstract description 39
- 239000012141 concentrate Substances 0.000 claims abstract description 24
- 102000004169 proteins and genes Human genes 0.000 claims description 27
- 108090000623 proteins and genes Proteins 0.000 claims description 27
- 239000012466 permeate Substances 0.000 claims description 15
- 238000004458 analytical method Methods 0.000 claims description 12
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 8
- 239000004480 active ingredient Substances 0.000 claims description 6
- 238000009295 crossflow filtration Methods 0.000 claims description 6
- 229920002401 polyacrylamide Polymers 0.000 claims description 6
- 239000000843 powder Substances 0.000 claims description 5
- 238000001962 electrophoresis Methods 0.000 claims description 4
- 239000000047 product Substances 0.000 claims description 2
- 239000006260 foam Substances 0.000 abstract description 37
- 238000005187 foaming Methods 0.000 abstract description 35
- 238000001035 drying Methods 0.000 abstract description 9
- 239000007788 liquid Substances 0.000 abstract description 9
- 230000008034 disappearance Effects 0.000 abstract description 4
- 235000018102 proteins Nutrition 0.000 description 26
- 239000000243 solution Substances 0.000 description 13
- 230000000052 comparative effect Effects 0.000 description 10
- 239000011550 stock solution Substances 0.000 description 10
- 238000000108 ultra-filtration Methods 0.000 description 10
- 239000007864 aqueous solution Substances 0.000 description 9
- 239000012510 hollow fiber Substances 0.000 description 9
- 235000013305 food Nutrition 0.000 description 7
- 238000001914 filtration Methods 0.000 description 6
- 238000005374 membrane filtration Methods 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 4
- 239000003599 detergent Substances 0.000 description 4
- 235000014103 egg white Nutrition 0.000 description 4
- 210000000969 egg white Anatomy 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 239000007921 spray Substances 0.000 description 4
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 3
- 102000009027 Albumins Human genes 0.000 description 3
- 108010088751 Albumins Proteins 0.000 description 3
- 102000002322 Egg Proteins Human genes 0.000 description 3
- 108010000912 Egg Proteins Proteins 0.000 description 3
- 208000025174 PANDAS Diseases 0.000 description 3
- 208000021155 Paediatric autoimmune neuropsychiatric disorders associated with streptococcal infection Diseases 0.000 description 3
- 240000004718 Panda Species 0.000 description 3
- 235000016496 Panda oleosa Nutrition 0.000 description 3
- 108010073771 Soybean Proteins Proteins 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 235000019710 soybean protein Nutrition 0.000 description 3
- 238000001694 spray drying Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 235000013365 dairy product Nutrition 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 101150109949 endou gene Proteins 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 244000105624 Arachis hypogaea Species 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- 101100421200 Caenorhabditis elegans sep-1 gene Proteins 0.000 description 1
- 101100156448 Caenorhabditis elegans vps-33.1 gene Proteins 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 241000207836 Olea <angiosperm> Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 235000012174 carbonated soft drink Nutrition 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 235000011850 desserts Nutrition 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005360 mashing Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 210000003097 mucus Anatomy 0.000 description 1
- 238000001728 nano-filtration Methods 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 235000014571 nuts Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 235000020232 peanut Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 235000020238 sunflower seed Nutrition 0.000 description 1
- 235000019465 surimi Nutrition 0.000 description 1
- 238000002834 transmittance Methods 0.000 description 1
- 238000007738 vacuum evaporation Methods 0.000 description 1
Classifications
-
- 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
- A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
-
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2300/00—Processes
- A23V2300/34—Membrane process
Definitions
- the present invention relates to a soluble polypeptide derived from Endo whey exhibiting unique foaming characteristics, a foaming agent, and a method for producing the same.
- JP-A-5 2-1 5 1 2 0 0 discloses foam isolated from protein sources including extracts from soybeans, whey, egg whites, rapeseed, peanuts, sunflower seeds, palm nuts or olives. It is disclosed that it is useful as an agent.
- Japanese Patent Application Laid-Open No. Hei 4 (1990) 1 9 0 7 6 6 discloses that when foaming protein such as soybean protein or wheat protein is mixed with polysaccharide mucus in the meat, bubbles are appropriately dispersed inside. It is disclosed to give a texture.
- Japanese Patent Application Laid-Open No. 2000-069-920 discloses a polypeptide that separately hydrolyzes 7 S component and 11 S component in soybean protein and contains both hydrolysates. It is disclosed that it is excellent as a foaming agent or an emulsifier.
- Patent Document 1 Japanese Patent Application Laid-Open No. 52-1515 1200 (Claim 1 1)
- Patent Document 2 Japanese Patent Application Laid-Open No. Hei 41 1 9 0 7 6 6 (Claim 1, page 2, upper right column)
- Patent Document 3 Japanese Patent Application Laid-Open No. 2000-69-920 (Claim 1)
- conventional foaming agents such as soybean protein and egg white are foams that do not easily disappear after the foaming. Most have good stability. In recent years, there has been a wide variety of consumer needs for food, The power that is high and the foam disappears relatively early and the low foam stability is also demanded. Conventional foaming agents cannot meet such needs.
- an object of the present invention is to provide a novel polypeptide, a foaming agent, and a method for producing a polypeptide that exhibit high foaming properties with high initial foaming properties and low foam stability that eliminates foam relatively early. It is to provide. Disclosure of the invention
- the present inventors have conducted intensive studies. As a result, in the analysis by SDS polyacrylamide, the soluble whey derived from endow whey having a molecular weight of 3,000 to 25,000. However, the present inventors have found that a foaming characteristic with a high initial foaming property and a low foam stability in which the foam disappears relatively early is developed, and the present invention has been completed.
- the present invention provides a soluble polypeptide derived from endow whey characterized by having a molecular weight of 3,00 or more and less than 17, 500 in the analysis by SDS polyacrylamide electrophoresis. Is provided.
- the present invention provides a soluble polypeptide derived from endhu whey, characterized in that the molecular weight is from 3,00 to 1,0,00 in analysis by SDS polyacrylamide electrophoresis. Is.
- the present invention provides a foaming agent comprising the above-mentioned soluble polypeptide derived from endhoe as an active ingredient.
- the present invention also includes a first step of treating the endow whey with a cross-flow filtration membrane having a molecular weight cut-off of 3, 00 to 4, 00 to obtain a concentrate and a permeate, and the concentration
- the present invention provides a method for producing a soluble polypeptide derived from endow whey, comprising a second step of drying the liquid to obtain a powdered polypeptide.
- the foaming agent containing the soluble polypeptide derived from the endow whey of the present invention as an active ingredient has a high initial foaming property, and can exhibit foaming characteristics with a low foam stability in which the foam disappears relatively early.
- the method for producing the soluble polypeptide derived from the end whey of the present invention can be produced by a simple method and on an industrial scale.
- Fig. 1 shows the results of SDS-PAGE analysis of the undiluted solution and concentrate in Example 1.
- Fig. 2 shows the results of foaming tests in Examples and Comparative Examples.
- Fig. 3 shows the results of Examples and Comparatives.
- Fig. 4 shows the results of SDS-PAGE analysis of the undiluted solution and concentrate in Example 2
- Fig. 5 shows the results of foaming test in Example 2.
- FIG. 6 shows the foamability test results in Comparative Example 3.
- the endow whey as a raw material is manufactured by a known method.
- Endo whey is a clarified product obtained by dispersing the whole particle of endo in an aqueous solution and leaving it for a certain period of time to extract components dissolved in the aqueous solution into the solution, and then removing proteins and other components insoluble in the aqueous solution. Says an aqueous solution.
- Insoluble components differ depending on the conditions of the aqueous solution, so for example, by changing the pH of the aqueous solution, changing the temperature, adding a salt to the aqueous solution, or adding an organic solvent to the component dissolved under a certain condition Or by deliberately precipitating insoluble components by changing the solubility of the dissolved components. it can.
- the clear water after intentionally removing insoluble components from the aqueous solution in this way is also called whey. Centrifugation, membrane filtration, etc. can be used as a method for separating insoluble components and clarified water.
- Endo whey from Endo An example of obtaining Endo whey from Endo is shown. That is, the dried and peeled endou beans are pulverized, an aqueous alkaline solution (pH 9.0) is added, and the protein is extracted at room temperature. The extract is filtered to remove residues and unnecessary components such as starch, and then the pH is adjusted to 3.5 to 6.0 to cause isoelectric point aggregation of the protein. The aggregate is then centrifuged to obtain a supernatant (whey). Remove globulin residues (impurities) in advance before treating endofe adjusted to pH 3.5 to 6.0 with a cross-flow filtration membrane. It is preferable in that it can be improved. Examples of the impurity removal method include a centrifugal separation method and a membrane filtration method.
- the cross-flow type filtration membrane is not particularly limited, and examples thereof include an ultrafiltration membrane and an NF membrane (nanofiltration membrane). Among these, an ultrafiltration membrane is preferable.
- the temperature at which the green whey is treated with the cross-flow filter membrane is not particularly limited, but is preferably 20 ° C. or lower and 2 to 14 ° C. If the temperature is too low, the transmittance will be poor, and if the temperature is too high, protein denaturation, pacteria growth, etc. will be undesirable.
- the cross-flow type filtration membrane used in the present invention has a molecular weight cut-off of 3,000 to 4,00,0, and preferably a molecular weight cut-off of 3,000.
- the concentrated solution obtained by this membrane filtration is albumin having a molecular weight of 3,00 or more, and the foaming agent containing this as an active ingredient has a high initial foaming property, and the foam disappears relatively early. Low foaming characteristics can be developed.
- Endofhoe is treated with a cross-flow filtration membrane with a molecular weight cut-off of 3, 00 0 to 4, 0 0 0.
- a cross-flow filtration membrane having a molecular weight cut off of, for example, 100,000 is used to obtain a permeate containing a polypeptide having a molecular weight range of 100,000 or less, and this permeate is separated. It may be treated with a cross-flow type filtration membrane having a molecular weight of 3,000 to 4,00. As a result, a concentrated solution having a molecular weight range of 3,000 or more and 10,000 or less can be obtained.
- the shape of the cross-flow type filtration membrane used in the present invention is not particularly limited, and examples thereof include a hollow fiber type, a flat membrane type, a tubular type, and a spiral type.
- the hollow fiber type has a concentration ratio. It is preferable in that it is large, has a simple structure, and allows reverse permeation cleaning.
- the operating pressure of the cross-flow filter membrane used in the present invention is not particularly limited, and is, for example, in the range of 0.1 4 to 0.5 MPa (1.4 to 5. O kgf / cm 2 ). As appropriate. Endo whey is treated with a cross-flow filtration membrane to obtain a concentrate and permeate.
- the concentration factor is not particularly limited, and is 2 to 50 times, particularly 2 to 5 times.
- the permeate is not required in the present invention and is appropriately disposed of.
- the second step is a step of obtaining a powdery polypeptide by drying the concentrated liquid obtained in the first step. Since the pH of the concentrate obtained in the first step is usually 4 to 4.5, neutralize with a neutralizing agent in advance before entering the drying step. As a result, protein denaturation due to heat of drying can be prevented.
- the method for drying the concentrate is not particularly limited, and examples thereof include spray drying, freeze drying, and 'vacuum evaporation drying. Of these, spray drying is preferable because it can be carried out by a simple method and the drying efficiency is high. Spray drying can be done by known methods.
- the powdered polypeptide obtained in the second step is analyzed by SDS polyacrylamide gel electrophoresis (hereinafter also referred to as SDS-PAGE).
- the molecular weight is 3,000 to 25,000.
- Polypeptides with a molecular weight of less than 3,000 are difficult to concentrate, making industrial production impossible, and those with a molecular weight of more than 2,500 are low in content and efficient production. At the same time, it is impossible to develop foaming characteristics with high initial foamability and low foam stability in which foam disappears relatively early.
- the molecular weight of the polypeptide of the present invention is 3,000 or more and less than 17,500, the above-mentioned initial initial foaming property can be further enhanced.
- the molecular weight of the polypeptide of the present invention is 3,000 or more and 10,000 or less, the initial foaming property is highly developed, and the foaming property with even lower foam stability is exhibited that the foam disappears early. Can be made.
- Analysis by SDS_P AGE can measure the molecular weight of each polypeptide from the mobility of a standard molecular weight marker, and can also determine its content by quantification with a densitometer.
- the polypeptide of the present invention has at least two bands in the molecular weight range of 3,500 to 1,4,300 in the analysis by SDS polyacrylamide electrophoresis. One panda exists at 1, 0 0 0, and one panda exists between 2 1,0 00 and 2 9000 or less.
- the polypeptide of the present invention has an area area of 80% or more of a polypeptide having a molecular weight in the range of 300 to 8,000 with respect to the total area of the polypeptide of the present invention.
- the foaming agent of the present invention contains the above-mentioned soluble polypeptide derived from enduro whey as an active ingredient.
- the foaming agent of the present invention has a high initial foaming property and expresses foaming characteristics with low foam stability in which foam disappears relatively early. Therefore, the foaming agent can be used alone or in combination with other foaming agents.
- As food to mix There are no particular restrictions, and examples include surimi foods such as happoshu, brewed sake, dairy products, and hampen, and desserts that enjoy foam.
- the amount of the foaming agent of the present invention to be mixed with food is appropriately determined according to the type and purpose of the food, but for example, those in the range of 0.05 to 3.0% by weight. Many.
- the foaming agent of the present invention is applied to detergents, it is usually used in combination with other foaming agents. The amount to be added to the detergent is 0.05 to 3.0 weight in the same way. / Determined appropriately from 0 .
- Circulation pump Magnet pump, capacity 50 1 / min, head 14 m • Membrane filtration operating temperature 6-14 ° C
- the powdered polypeptide obtained in Example 1 was mixed with pure water at 0.3 wt% and 1.5 wt%, respectively. This was stirred for 30 seconds in a mill & mixer TML 15 (manufactured by TOSCOM). Immediately after stirring, the entire amount of the liquid was transferred to a graduated cylinder, and the volume ratio (%) of the foam over time was measured. The volume ratio of the foam was a value obtained by dividing the volume of the foam by the total amount of the liquid including the foam. The results of 0.3 wt% are shown in Fig. 2, and the results of 1.5 wt% are shown in Fig. 3.
- Example 2 shows the result of 1.0% by volume. The results for 4.0% by weight are shown in FIG.
- the endoglobulin protein is prepared by mashing dried and peeled endou beans, adding an alkaline aqueous solution (pH 9.0), extracting the protein at room temperature, filtering the extract, and removing residues and starch. After removing unnecessary components, the pH is adjusted to 3.5 to 6.0, and the protein obtained by isoelectric focusing is sterilized, neutralized, and dried into powder o 0
- Example 2 The same method as in the foamability test of Example 1 was performed, except that egg white was used instead of the powdered polypeptide obtained in Example 1. The results for 0.3% by weight are shown in FIG. 2, and the results for 1.5% by weight are shown in FIG.
- the foaming characteristics of the soluble polypeptide derived from endow whey in Example 1 are unique in that the initial foaming property is high and the foam disappears relatively early and the foam stability is low. Indicates.
- the endoglobulin protein of Comparative Example 1 shows almost no foaming property.
- the foaming characteristics of the egg white of Comparative Example 2 are excellent in foam stability in which the foam does not easily disappear with the passage of time, although the initial foamability is not so much.
- a permeate containing a polypeptide having a molecular weight range of 10 or less was obtained by treatment with a hollow fiber type ultrafiltration membrane having a molecular weight of 10 or 0.00. Further, this permeate was concentrated with a hollow fiber type ultrafiltration membrane having a fractional molecular weight of 3,00 0 to obtain a concentrated solution of a polypeptide having a molecular weight range of 3,00 0 to 10 0,000. Further, the concentrate was circulated to obtain a concentrate having a concentration factor of 5 times.
- Membrane module of hollow fiber type ultrafiltration membrane device fractional molecular weight 1 0, 0 0 0, effective membrane area 0.1 2 m 2 “Microza UF SLP 1 0 5 3” (Asahi Kasei Chemicals)
- Circulation pump Magnet pump, capacity 50 liters / min, head 14 m • Membrane filtration operating temperature: 2 to 14 ° C
- Circulation pump Magnet pump, capacity 50 liters / min, head 14 m • Membrane filtration operating temperature: 2 to 14 ° C
- the dried powder (standard corresponding to lane B in Fig. 4) containing a polypeptide having a molecular weight range of 3,000 to 100,000 obtained in Example 2 was added to pure water. They were blended at 0.5% by weight and 1.0% by weight, respectively. This was stirred for 30 seconds in a mixer MX-B 30 G (manufactured by Toshiba). Immediately after stirring, the entire amount of the liquid was transferred to the graduated cylinder, and the volume ratio (%) of the foam over time was measured. The volume ratio of the foam was a value obtained by dividing the volume of the foam by the total amount of liquid including the foam. The results are shown in Fig. 5.
- Example 2 instead of the dry powder of the concentrated solution containing the polypeptide having a molecular weight range of 3,00,000, etc., 100, 00 obtained in Example 2, the dry powder of the concentrated solution of the stock solution (No. 4 The test was performed in the same manner as in the foamability test of Example 2, except that the sample corresponding to lane A in FIG. The result is shown in Fig. 6.
- the foaming agent comprising the soluble polypeptide derived from the endow whey of the present invention as an active ingredient has a high initial foaming property and expresses a unique foaming characteristic with a low foam stability in which the foam disappears relatively early. When used in combination with other foaming agents in foods and detergents, it can produce quaint foam that can meet various needs in recent years.
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- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Botany (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
- Dairy Products (AREA)
Abstract
Description
Claims
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
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JP2006545108A JPWO2006052003A1 (ja) | 2004-11-11 | 2005-11-10 | エンドウホエー由来の可溶性ポリペプチド、発泡剤及びその製造方法 |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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JP2004-327221 | 2004-11-11 | ||
JP2004327221 | 2004-11-11 |
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WO2006052003A1 true WO2006052003A1 (ja) | 2006-05-18 |
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PCT/JP2005/021064 WO2006052003A1 (ja) | 2004-11-11 | 2005-11-10 | エンドウホエー由来の可溶性ポリペプチド、発泡剤及びその製造方法 |
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WO (1) | WO2006052003A1 (ja) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR3001362A1 (fr) * | 2013-01-31 | 2014-08-01 | Roquette Freres | Procede de fractionnement des solubles de pois, fractions obtenues et leur valorisation |
WO2018197822A1 (fr) | 2017-04-28 | 2018-11-01 | Roquette Freres | Albumines de pois ameliorees, procede d'obtention et leurs applications |
WO2019068999A1 (fr) | 2017-10-04 | 2019-04-11 | Roquette Freres | Composition de protéines de pois a qualité nutritionnelle améliorée |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
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JPH05230100A (ja) * | 1991-09-13 | 1993-09-07 | Pentapharm Ag | 蛋白分画、その単離法、該蛋白分画を含有する有効物質濃縮物、及び該蛋白分画を含有する、皮膚手入れ及び/又は炎症性皮膚病の治療用製剤 |
JPH0925225A (ja) * | 1995-05-09 | 1997-01-28 | Sansho Seiyaku Co Ltd | 皮膚外用剤およびその有効成分の製造方法 |
JP2001069920A (ja) * | 1998-07-29 | 2001-03-21 | Fuji Oil Co Ltd | 大豆蛋白加水分解物及びその製造法並びにそれを使用した製品 |
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2005
- 2005-11-10 JP JP2006545108A patent/JPWO2006052003A1/ja active Pending
- 2005-11-10 WO PCT/JP2005/021064 patent/WO2006052003A1/ja active Application Filing
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH05230100A (ja) * | 1991-09-13 | 1993-09-07 | Pentapharm Ag | 蛋白分画、その単離法、該蛋白分画を含有する有効物質濃縮物、及び該蛋白分画を含有する、皮膚手入れ及び/又は炎症性皮膚病の治療用製剤 |
JPH0925225A (ja) * | 1995-05-09 | 1997-01-28 | Sansho Seiyaku Co Ltd | 皮膚外用剤およびその有効成分の製造方法 |
JP2001069920A (ja) * | 1998-07-29 | 2001-03-21 | Fuji Oil Co Ltd | 大豆蛋白加水分解物及びその製造法並びにそれを使用した製品 |
Cited By (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP3308651A1 (fr) | 2013-01-31 | 2018-04-18 | Roquette Freres | Procede de fractionnement des solubles de pois |
EP3305093A1 (fr) | 2013-01-31 | 2018-04-11 | Roquette Freres | Procede de fractionnement des solubles de pois |
FR3001362A1 (fr) * | 2013-01-31 | 2014-08-01 | Roquette Freres | Procede de fractionnement des solubles de pois, fractions obtenues et leur valorisation |
EP3300610A1 (fr) * | 2013-01-31 | 2018-04-04 | Roquette Freres | Procede de fractionnement des solubles de pois |
DE202014011178U1 (de) | 2013-01-31 | 2018-05-23 | Roquette Frères S.A. | Im Wesentlichen aus Albuminen bestehendes Ultrafiltrationsretentat |
EP3305094A1 (fr) | 2013-01-31 | 2018-04-11 | Roquette Freres | Procédé de fractionnement des solubles de pois, fractions obtenues et leur valorisation |
EP3305092A1 (fr) | 2013-01-31 | 2018-04-11 | Roquette Freres | Procede de fractionnement des solubles de pois |
DE202014011179U1 (de) | 2013-01-31 | 2018-05-23 | Roquette Frères S.A. | Ultrafiltrationspermeat mit einem hohen Gehalt an PA1b-Fraktion |
CN104955341A (zh) * | 2013-01-31 | 2015-09-30 | 罗盖特公司 | 分级可溶性豌豆部分的方法,由此获得的部分及其增值 |
WO2014118449A1 (fr) * | 2013-01-31 | 2014-08-07 | Roquette Freres | Procédé de fractionnement des solubles de pois, fractions obtenues et leur valorisation |
EP2950662B1 (fr) | 2013-01-31 | 2018-04-18 | Roquette Freres | Procédé de fractionnement des fractions solubles de pois |
US11377472B2 (en) | 2013-01-31 | 2022-07-05 | Roquette Freres | Method for fractionating soluble fractions of peas, fraction thus obtained and upgrade thereof |
EP3305093B1 (fr) | 2013-01-31 | 2021-11-10 | Roquette Frères | Procede de fractionnement des solubles de pois |
EP3300610B1 (fr) | 2013-01-31 | 2021-11-10 | Roquette Frères | Procede de fractionnement des solubles de pois |
WO2018197822A1 (fr) | 2017-04-28 | 2018-11-01 | Roquette Freres | Albumines de pois ameliorees, procede d'obtention et leurs applications |
US11937619B2 (en) | 2017-04-28 | 2024-03-26 | Roquette Freres | Pea albumins, method for obtaining same and applications thereof |
WO2019068999A1 (fr) | 2017-10-04 | 2019-04-11 | Roquette Freres | Composition de protéines de pois a qualité nutritionnelle améliorée |
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