WO2010127414A1 - Emulsifiant de type huile dans l'eau - Google Patents
Emulsifiant de type huile dans l'eau Download PDFInfo
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- WO2010127414A1 WO2010127414A1 PCT/AU2010/000625 AU2010000625W WO2010127414A1 WO 2010127414 A1 WO2010127414 A1 WO 2010127414A1 AU 2010000625 W AU2010000625 W AU 2010000625W WO 2010127414 A1 WO2010127414 A1 WO 2010127414A1
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- Prior art keywords
- composition
- lupin
- proteins
- oil
- molecular weight
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Classifications
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- 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
-
- 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
- A23J1/148—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 by treatment involving enzymes or microorganisms
-
- 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
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/10—Foods or foodstuffs containing additives; Preparation or treatment thereof containing emulsifiers
Definitions
- the invention relates to protein extracts, concentrates and isolates, especially those obtainable from plant sources that are useful in the manufacture of foods and food products, especially as emulsifiers, creaming agents and the like.
- Vegetable and plant proteins have been used for some time in the manufacture of food products. In some applications these sources of proteins are used for nothing more than increasing the nutritive quality of food products. For example, soy protein may be added to meat products to increase protein content.
- the protein sources are added to modify a quality or characteristic of a food product, or otherwise to provide a quality or characteristic to a mixture of ingredients which then leads to the formation of a food product.
- protein sources that are used as emulsifiers, gelling agents, thickeners, whipping agents, creaming agents and whitening agents.
- Vegetable protein isolates and concentrates have been described for use in stabilising oil-in-water emulsions. These are essentially colloidal dispersions where oil forms a discrete phase and water forms a continuous phase. Depending on factors including relative amount of oil to water, the type of oil, the amount of solids, polysaccharides, pH, ionic strength and type and concentration of salt, these oil-in-water emulsions may be provided in the form of a liquid, a semi liquid in the form of a gel or paste, or a solid. Examples of oil-in-water emulsions that are liquids, semi liquids and solids include milk, low fat mayonnaise and cheese, respectively.
- Most protein isolates that are useful for stabilising oil-in-water emulsions work by unfolding at the interface of the oil and water phases to provide the requisite degree of hydrophobicity for stabilising the emulsion.
- the hydrophobic portions of the proteins are understood to at least partially dissolve into the discrete phase, leaving the more aqueous soluble portions to dissolve into the continuous phase.
- the degree of unfolding and surface hydrophobicity may be enhanced by thermal denaturation of the protein prior to emulsification, by chemical modification of the protein or by enzymatic modification of the protein.
- the latter are understood to increase an entangled network of protein molecules at the interface of the oil and water phases.
- thermal denaturation of lupin proteins is the most effective modification for improving emulsifying properties of lupin proteins.
- the invention seeks to improve or at least to minimise one or more of the above problems or limitations and in one embodiment provides a composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product, the composition including: - lupin proteins in an amount of about 70 to 98 % by dry weight of the composition,
- composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product including:
- said lupin proteins being substantially free of attached fibre.
- composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product the composition produced by a process including:
- composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product the composition produced by a process including:
- a food product including oil or fat, water and a composition useful as an emulsifier for stabilising an oil-in-water emulsion.
- the food product is provided in the form of an oil-in-water emulsion such as a milk, cheese or like product, an ice cream, or mayonnaise, salad dressing, sauce, confectionery filling or like product.
- the food product is a low fat food product.
- the food product is provided in the form of a creaming agent, a dispersant or a surfactant.
- Figure 1 Size exclusion profile of the composition of the invention.
- Figure 2 Matrix Assisted Laser Desorption/lonisation - Time of Flight (MALDI-TOF) profile of the composition of the invention.
- Figure 3 Typical effect of different ratios of oil to water on the emulsion activity of the composition.
- Figure 4 Typical effect of different ratios of water to oil on the emulsion activity of the composition.
- Figure 5 Typical effect of pH on emulsion activity of the oil-in-water emulsifier.
- the inventors sought to provide improved oil in water emulsifiers, and in particular emulsifiers for stabilising low fat oil-in-water emulsions and food products formed therefrom.
- lupin protein extracts, concentrates or isolates that predominantly consist of proteins having a higher molecular weight are useful for stabilising oil-in-water emulsions, and in particular for stabilising oil in water emulsions having a low oil content relative to water.
- Stabilisation of oil-in-water emulsions is particularly important when these emulsions are used in low fat products which require stability to maintain quality during their shelf life.
- compositions described herein find particular application in the production of low fat food products formed from low fat containing oil-in-water emulsions.
- compositions of the invention described herein are capable of stabilising oil-in-water emulsions across a wide range of oil to water ratios, pH, salt and temperature conditions.
- emulsifier compositions of the invention described herein is that these emulsifying characteristics do not require additional thermal denaturation or chemical or enzymatic modification.
- composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product including:
- proteins having a greater molecular weight may be provided in a low relative abundance.
- An emulsion is generally understood as a mixture of two or more immiscible liquids, e.g. oil and water, in which one liquid forms a discrete phase and another a continuous phase. Liquids are said to be immiscible if they are not able to mix, in any proportions, to form a homogenous solution. Generally, a solution is homogenous if the liquids that make up the solution are uniformly dispersed throughout the solution.
- compositions of the present invention are capable of stabilising mixtures of aqueous solutions and oils by forming a suspension of the oil phase in the aqueous phase (i.e. the oil phase forms a discrete phase and the aqueous phase forms a continuous phase), thereby preventing or minimising phase separation of the oil phase from the aqueous phase and increasing the homogeneity of the mixture. This results in an even distribution of the oil phase throughout the mixture. Phase separation may occur by the coalescence of the discrete oil droplets into larger droplets or creaming, where the oil migrates to the surface of the aqueous phase. Minimising can mean any of reducing, diminishing, lessening, curtailing or decreasing phase separation.
- An oii-in-water emulsion is generally understood as meaning an emulsion wherein oil forms the discrete phase and water forms the continuous phase.
- a low fat oil-in-water emulsion is generally understood as meaning an oil-in-water emulsion in a low-fat product.
- An emulsifier is generally understood as meaning a substance which stabilizes an emulsion by increasing its kinetic stability.
- the emulsifier minimises phase separation so that the relevant discrete and continuous phases forming the emulsion are maintained.
- the composition includes lupin protein whereby about 70 to 98 % of the dry weight of the composition is lupin protein.
- the composition includes lupin proteins in an amount of about 75 to 98 %, 80 to 98 %, 85 to 98 %, or 90 to 98 %.
- useful oil-in-water emulsifiers can be provided by removing attached and/or entrapped fibre from lupin proteins.
- An example of attached fibre is O- and N- linked carbohydrates. The removal of fibre improves the emulsion activity.
- composition useful as an emulsifier for stabilising an oil-in-water emulsion to form a food product including:
- said lupin proteins being substantially free of attached fibre.
- about 85 to 95% of the lupin proteins have a molecular weight greater than 20 kDa.
- composition of the invention typically in the composition of the invention about 30 to 35 % of the lupin proteins have a molecular weight from about 25 to 55 kDa.
- lupin proteins typically have a molecular weight from about 60 to 80k Da.
- lupin proteins typically have a molecular weight from about 200 to 250 kDa.
- the relative abundances of the molecular weight range of lupin protein in the composition are as shown in Table 5 or Table 6.
- the lupin proteins may include ⁇ - and ⁇ -conglutin and fragments thereof.
- composition further includes lipid in an amount of from about 10 to 30 % by dry weight of the composition.
- lipids may contain unsaturated fatty acid chains.
- lipid about 80 to 90 % of the fatty acid chains in the lipid are C18 (i.e. having 18 carbon atoms).
- lipid is lupin lipid.
- the lipid component of the composition is stable, In particular, the lipid within the composition has been observed to have a shelf life of up to 12 months.
- the stability of the lipid component is believed to facilitate maintenance of oil-in-water emulsions.
- the lipid component may dissolve into the discrete oil phase and in doing so be particularly effective for stabilising an oil-in-water emulsion over a longer term, thereby providing a product with improved shelf life.
- composition of the invention derived from lupin forms a useful source of plant-derived lipid having long shelf life for use in food technology applications where addition of lipid is required to fulfil a nutritional or functional need.
- the composition of the invention has an ANS hydrophobicity value of about 0.75 to 0.85 at pH 7.4.
- the relatively high hydrophobicity of the compositions of the invention means that the compositions are more likely to dissolve into an oil phase than aqueous phase, thereby stabilising oil-in-water emulsions, and in particular low fat oil-in-water emulsions.
- An ANS hydrophobicity value or score is a measure of the hydrophobicity of a given protein- containing composition.
- the value represents the degree of binding of ANS dye to hydrophobicity regions of proteins.
- the ANS value is influenced by the solubility of the composition in the given solvent in which the ANS hydrophobicity assay is conducted.
- the ANS value for the composition of the invention is lower at more acidic pH reflecting the limited solubility of the composition at acidic pH. It will be understood that the ANS value is a measure of hydrophobicity of the composition of the invention as it exists after the treatment that is provided to the composition in the ANS assay steps as in Example 3.
- the ANS hydrophobicity assay is also described in Howe A et al. 2008 Pharma. Res. 25: 1487- 1499.
- the composition is generally partially insoluble in an aqueous solution having a pH of about 5.5. It is more soluble below pH 5.2 and above pH 5.8.
- the relative abundance of the amino acids in the composition of the invention is as described in Table 10 herein.
- composition of the invention does not include a fermentation product such as lactic acid, or lecithin.
- composition according to the invention may be produced by a number of processes.
- the composition is produced by a process including:
- carbohydrase is a pectinase cellulase and/ or hemicellulase.
- the process includes the following steps:
- the extract of lupin proteins may be provided in the form of a lupin protein-containing slurry.
- the lupin protein-containing slurry may be formed from milling of de-hulled lupins to form a slurry. Prior to milling, the de-hulled lupins may have been steeped in water. The water may be heated to temperatures of no more than about 7O 0 C. In certain embodiments the lupins have not been de-oiled with an organic solvent such as hexane for removing lupin oils or fats, although in other embodiments de-oiling is possible.
- an organic solvent such as hexane for removing lupin oils or fats
- the lupin protein-containing slurry generally has a pH in the range of 8 to 9, preferably about 8.4.
- the adjustment of the pH may be provided by an alkali, NaOH being one example.
- a protein-containing supernatant and fibre-containing pellet is formed.
- the protein-containing supernatant may then be separated from the fibre-containing pellet. This can be done by, for example, decanting the supernatant from the pellet.
- the lupins are of genus Lupinus. Particularly preferred species are Angustifolius, Luteus, Mutablis and other low alkaloid varieties of species including Albus. In one embodiment the lupin is not a pea, especially not a member of genus Pisum.
- the protein- containing supernatant is a mixture of higher and lower molecular weight proteins and residual lupin fibre, the latter remaining after alkaline treatment.
- the inventors recognised that by treating this fibre component of the protein-containing supernatant, it then becomes possible to separate the lower molecular weight proteins from the higher molecular weight proteins. From this, the inventors were able to observe that the composition having higher molecular weight proteins is useful as an oil-in-water emulsifier.
- the treatment according to the invention involves the use of fibre-hydrolysing enzymes.
- the fibre-hydrolysing enzyme is a carbohydrase.
- the carbohydrase may be a pectinase, celfulase or hemicellulase.
- the carbohydrase is an enzymatic composition of cellulase and pectinase.
- the carbohydrase treatment digests soluble fibre.
- the fibre may or may not be attached to protein prior to digestion.
- the quantity of enzyme used is dependent on the specific activity of the enzyme at the pH and temperature of the incubation period.
- the treatment might be designed to be completed in one hour with the enzymic reaction being carried out at a pH range of from about 6 to 8.
- the enzymes After the completion of the enzymic reaction it may be desirable to deactivate the enzymes. This can be done by, for example, changing the pH of the supernatant and/or heat treatment of the supernatant.
- the inventors have found that the decrease in specific gravity of the soluble protein fraction enables better separation of protein fractions through a clarifier which uses centrifugal force to separate the insoluble from the soluble protein fractions.
- the higher molecular weight proteins in the enzyme-treated, protein-containing supernatant are separated from the lower molecular weight proteins. This can be achieved by adjusting the pH of the supernatant to the isoelectric point of the higher molecular weight proteins in the supernatant to precipitate the higher molecular weight proteins.
- the pH range may be from about 5 to 6, preferably about 5.5.
- these higher molecular weight proteins can be recovered by any technique that enables the precipitated proteins to be separated from lower molecular weight protein of less than about 30 kDa, including centrifugation and/or membrane filtration.
- the recovered proteins can also be further treated by, for example, adjusting the pH, washing and/or spray drying.
- a food product or ingredient for formation of a food product including water, and oil and/or fat and an emulsifier composition of the invention, as previously discussed.
- the food product may be provided in the form of an oil-in-water emulsion, or it may be homogenised to create an emulsion. In the latter embodiments the emulsion may be stabilised by a composition as described above.
- the food product or ingredient is a low fat product formed that contains an oil- in water emulsion.
- Particularly useful oils for use in a food product or ingredient of the invention are those that are edible, e.g. animal and plant oils.
- Examples of food products or ingredients according to the invention include dairy and related products, mayonnaises, salad dressings, sauces, confectionery fillings and the like.
- the composition may be applied in the form of a liquid or a powder for formation of a food product or ingredient for forming a food product, which requires the formation of an oil-in-water emulsion.
- a liquid or a powder for formation of a food product or ingredient for forming a food product, which requires the formation of an oil-in-water emulsion.
- Example 1 Chemical analysis data of the major components of the oil-in-water composition
- Table 1 Chemical analysis data of the major components of the composition according to the invention showing the range of values
- DSB refers to composition calculated on a dry solids basis.
- a sample oil-in-water emulsifier composition according to the invention was analysed and found to be composed of the following:
- DSB refers to composition calculated on a dry solids basis.
- Example 2 Molecular level analysis data for the protein component of the oil in water composition
- Cysteine analysis was performed using performic acid oxidation followed by 24 hr acid hydrolysis with 6 mol/kg HCI at 110 0 C.
- For tryptophan analysis samples underwent 24 hr base hydrolysis in 5 mol/kg NaOH at 110 0 C. After hydrolysis all amino acids were analysed using the Waters AccQTag Ultra chemistry. Samples were analysed in duplicate and results are expressed as an average.
- Table 4 Typical amino acid composition for serum albumin, soy protein and lupin protein
- Example 2.2 Size exclusion chromatographic analysis of the protein component of the composition
- a Phenomenex BIOSEP-SEC 4000 column was used for the analysis.
- a running time of 10 min was used (flow rate 2 mL/min) instead of the Standard 35 min run (0.5 mL/min).
- the eluent used was aqueous acetonitrile (ACN) buffer (0.05 % trifluoroactic acid (TFA) in water and 0.05 % in ACN).
- the proteins were detected at a wavelength of 214 nm.
- Example 2.3 MALDI-TOF analysis data of protein component of oil-in-water emulsifier composition
- Samples were dissolved in 60 ⁇ m ACN/H 2 O (v/v, 50:50) containing 0.05 % v/v TFA for 1 hour.
- Sample preparation was carried out according to the dried droplet method using sinapinic acid (SA) as matrix.
- SA sinapinic acid
- the matrix solution was prepared by dissolving SA in ACN/H 2 O (50:50 v/v) with 0.05 % v/v TFA at a concentration of 10 mg/mL.
- a sample/ matrix solution mixture (1 :10 v/v) was deposited (2 ⁇ L) on to a 96-sample MALDI probe tip, and dried at room temperature.
- MALDI-TOF mass spectrometric experiments were carried out on a Voyager DE-PRO TOF mass spectrometer (Applied Biosystems, Foster City, CA, USA) equipped with UV nitrogen laser (337 nm). The instrument was used with the following parameters: laser intensity 2 500, mass range 50-100 kDa, acceleration voltage 25 kV, grid voltage 93% guide wire 0.2 %, delay time 850 ns. Spectra were obtained in positive (inear ion mode and were averaged from 50 laser shots to improve the S/N level. All the samples were automatically accumulated in a random pattern over the sample spot to provide the final spectrum. Human transferrin (79 549 Da) as external standards for mass assignment.
- Table 6 MALDI - TOF analysis data of the molecular size ranges for the protein component of the composition
- Example 3 Characterisation of lipid component of oil-in-water emulsifier composition
- Table 8 Typical lipid composition for oil-in-water emulsifier
- Table 9 Fatty acid ranges for oil-in-water emulsifier
- Table 10 Typical fatty acid composition for oil-in-water emulsifier
- Example 4.1 Solubility of oil-in-water emulsifier composition
- Solubility (%) (Solids in Supernatant x 100)/Total solids
- solubilities determined for the samples shown in Tables 11 and 12 are exemplary of the compositions according to the invention defined herein. Solubility is dependent on processing steps for manufacture of the composition including for example the parameters for drying. Accordingly, the composition of the invention may have solubilities outside the ranges generally shown in Tables 11 and 12.
- Example 4.2 Determination of hydrophobicity value for oil-in-water emulsifier composition
- the principle of the method is measuring the binding of a fluorescent dye (ANS) to the hydrophobic regions of the proteins.
- ANS fluorescent dye
- the resulting values are inversely proportional to hydrophobicity thus a lower value indicates a greater hydrophobicity.
- Buffer 1 0.1 mol/kg phosphate buffer from KH 2 PO 4 and Na 2 HPO 4 pH 7.4. 2. Prepare a stock protein solution: 0.05 % (m/m) protein solution in Buffer 1 (40 mL).
- Table 15 Typical values for ANS Hydrophobicity for protein components of lupin, soy, dairy and beef sera (atpH 7.4)
- the oil-in-water emulsifier is more hydrophobic than soy protein and much more hydrophobic than sodium caseinate and bovine serum albumin.
- EA (%) (emulsified layer (top) (cm ⁇ x 100)/ Total layer (cm)
- Table 17 Typical effect of re-hydration medium for oil-in-water emulsifier on emulsion activity
- the highest emulsion activity for a 3.6% concentration of the oil- in-water composition occurs when the ratio of oil to water is 5:3.
- the highest emulsion activity for a 3.6% concentration of oil-in- water composition occurs when the ratio of water to oil is 3:5.
- the oil-in-water emulsifier is affected by the pH with higher emulsions forming above and below pH 5.5.
- Table 18 Typical effect of freezing and thawing on emulsion activity
- the oil-in-water emulsifier does not lose emulsion activity after repeated freezing and thawing.
- the oil-in-water emulsifier does not lose emulsion activity after chilling.
- Example 6 Meat emulsion for sliceable sandwich meat (Laboratory model meat mix)
- Example 7 Enhancement of the functional performance of the base oil-in-water emulsifier
- the following methods can be used to improve performance of the oil-in-water emulsifier.
- Proteases which break the protein, peptide or amino acid linkages eg: exo-proteases can be used to change the protein structure of the oil-in-water emulsifier.
- the composition of the invention is one that has not been digested with an endopeptidase or related protease.
- Heating to temperatures greater than 90 0 C can change the agglomeration of the proteins and alter the performance characteristics of the oil-in-water emulsifier.
- Processes that use high shear and increased pressure such as using a homogeniser can structurally change the oil-in-water emulsifier by reducing the size of aggregates.
- Spray drying parameters including spray nozzle size, feed inlet pressures and instantising processes can affect the aggregation and hence solubility and performance of the oil-in-water emulsifier.
- Example 7.4 Modification using chemical agents
- Chemical agents that change the covalent and non-covalent bonds between amino acids in the proteins can change the structure of the protein.
- the conformational change influences the surface characteristics of the proteins.
- Examples of chemical agents include carboxylic anhydrides, ionic salts and redox reagents.
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Abstract
La présente invention concerne des extraits, des concentrés et des isolats protéiques, en particulier ceux pouvant être obtenus à partir de sources végétales qui sont utiles dans la fabrication d'aliments et de produits alimentaires, en particulier comme émulsifiants, agents de crémage et équivalents. En particulier, la présente invention concerne une composition utile comme émulsifiant destinée à stabiliser une émulsion de type huile dans l'eau afin de former un produit alimentaire, la composition comprenant des protéines de lupin en une quantité d'environ 70 à 98 % en poids sec de la composition, environ 85 à 95 % des protéines de lupin ayant un poids moléculaire supérieur à 20 kDa. La présente invention concerne également des procédés de production de cette composition.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2009902032A AU2009902032A0 (en) | 2009-05-08 | Oil-in-water emulsifier | |
| AU2009902032 | 2009-05-08 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2010127414A1 true WO2010127414A1 (fr) | 2010-11-11 |
Family
ID=43049860
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/AU2010/000625 Ceased WO2010127414A1 (fr) | 2009-05-08 | 2010-05-07 | Emulsifiant de type huile dans l'eau |
Country Status (1)
| Country | Link |
|---|---|
| WO (1) | WO2010127414A1 (fr) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20170105441A1 (en) * | 2014-06-30 | 2017-04-20 | Prolupin Gmbh | Emulsion with lupine protein |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040214300A1 (en) * | 2000-02-21 | 2004-10-28 | Andreas Wasche | Method for the production of protein preparations with essentially constant properties with regard to solubility and functionality within a ph range from about ph 3 to ph 10 |
| US20060127560A1 (en) * | 2002-10-16 | 2006-06-15 | Fraunhofergesellschaft Zur Forderung Der Angewandt Angewandten Forschung E.V. | Protein-containing preparation which can be biotechnologically produced, method for the production thereof, and use of the same as a food ingredient |
| US20060257453A1 (en) * | 2003-04-03 | 2006-11-16 | Funda Elger | Powderous formulations of fat-soluble active ingredients |
| CA2666510A1 (fr) * | 2006-10-26 | 2008-05-02 | Emsland-Starke Gmbh | Procede d'obtention de fractions proteiques de legumineuse d'un poids moleculaire moyen, fraction proteique de legumineuse et utilisation de ladite fraction proteique |
| US20080206439A1 (en) * | 2003-07-01 | 2008-08-28 | George Weston Foods Limited | Process for the Production of Lupin Extracts |
| US20080241343A1 (en) * | 2007-03-28 | 2008-10-02 | California Natural Products | Lupin food product base and processes |
| US20080305212A1 (en) * | 2007-04-16 | 2008-12-11 | Solae, Llc | Protein Hydrolysate Compositions Having Improved Sensory Characteristics and Physical Properties |
-
2010
- 2010-05-07 WO PCT/AU2010/000625 patent/WO2010127414A1/fr not_active Ceased
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040214300A1 (en) * | 2000-02-21 | 2004-10-28 | Andreas Wasche | Method for the production of protein preparations with essentially constant properties with regard to solubility and functionality within a ph range from about ph 3 to ph 10 |
| US20060127560A1 (en) * | 2002-10-16 | 2006-06-15 | Fraunhofergesellschaft Zur Forderung Der Angewandt Angewandten Forschung E.V. | Protein-containing preparation which can be biotechnologically produced, method for the production thereof, and use of the same as a food ingredient |
| US20060257453A1 (en) * | 2003-04-03 | 2006-11-16 | Funda Elger | Powderous formulations of fat-soluble active ingredients |
| US20080206439A1 (en) * | 2003-07-01 | 2008-08-28 | George Weston Foods Limited | Process for the Production of Lupin Extracts |
| CA2666510A1 (fr) * | 2006-10-26 | 2008-05-02 | Emsland-Starke Gmbh | Procede d'obtention de fractions proteiques de legumineuse d'un poids moleculaire moyen, fraction proteique de legumineuse et utilisation de ladite fraction proteique |
| US20080241343A1 (en) * | 2007-03-28 | 2008-10-02 | California Natural Products | Lupin food product base and processes |
| US20080305212A1 (en) * | 2007-04-16 | 2008-12-11 | Solae, Llc | Protein Hydrolysate Compositions Having Improved Sensory Characteristics and Physical Properties |
Non-Patent Citations (3)
| Title |
|---|
| MANRIQUE J. ET AL.: "The influence of isolation procedures on the yield and functional properties of the protein from Lupinus Leguminosae", PHD THESIS, 1977, UNIVERSITY OF NEW SOUTH WALES * |
| PAPALAMPROU, E. ET AL.: "Model salad dressing emulsion stability as affected by the type of the lupin seed protein isolate", JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, vol. 86, no. 12, 2006, pages 1932 - 1937 * |
| WASCHE, A. ET AL.: "New processing of lupin protein isolates and functional properties", NAHRUNG/FOOD, vol. 45, no. 6, 2001, pages 393 - 395 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20170105441A1 (en) * | 2014-06-30 | 2017-04-20 | Prolupin Gmbh | Emulsion with lupine protein |
| US11730182B2 (en) * | 2014-06-30 | 2023-08-22 | Prolupin Gmbh | Emulsion with lupine protein |
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