WO2003043439A1 - Continuous process for production of oil seed protein isolate - Google Patents
Continuous process for production of oil seed protein isolate Download PDFInfo
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- WO2003043439A1 WO2003043439A1 PCT/CA2002/001775 CA0201775W WO03043439A1 WO 2003043439 A1 WO2003043439 A1 WO 2003043439A1 CA 0201775 W CA0201775 W CA 0201775W WO 03043439 A1 WO03043439 A1 WO 03043439A1
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- protein
- oil seed
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- seed meal
- aqueous
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- 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
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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
- 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
Definitions
- the present invention relates to improved methods for manufacturing oil seed protein isolate.
- the defatted protein solution then is concentrated to increase the protein concentration while maintaining the ionic strength substantially constant, after which the concentrated protein solution may be subjected to a further fat removal step.
- the concentrated protein solution then is diluted to cause the formation of a cloud-like mass of highly aggregated protein molecules as discrete protein droplets in micellar form.
- the protein micelles are allowed to settle to form an aggregated, coalesced, dense amorphous, sticky gluten-like protein isolate mass, termed "protein micellar mass" or PMM, which is separated from residual aqueous phase and dried.
- the protein isolate has a protein content, on a dry weight basis, (as determined by Kjeldahl N 6.25) of at least about 90 wt%, is substantially undenatured (as determined by differential scanning calorimetry) and has a low residual fat content.
- protein content refers to the quantity of protein in the protein isolate expressed on a dry weight basis.
- the yield of protein isolate obtained using this procedure, in terms of the proportion of protein extracted from the oil seed meal which is recovered as dried protein isolate was generally less than 40 wt %, typically around 20 wt %.
- USP 4,208,323 itself was designed to be an improvement on the process described in US Patents Nos. 4,169,090 and 4,285,862 (Murray IA) by the introduction of the concentration step prior to dilution to form the PMM. The latter step served to improve the yield of protein isolate from around 20 wt % for the Murray IA process.
- the oil seed meal is extracted with an aqueous food grade salt solution.
- the resulting protein extract solution after an initial treatment with colorant adsorbant, if desired, is reduced in volume using ulfrafiltration membranes to provide a concentrated protein solution having a protein content in excess of about 200 g/L.
- the concentrated protein solution then is diluted into cold water, resulting in the formation of a white cloud of protein micelles which are allowed to separate. Following removal of the supernatant, the precipitated, viscous sticky mass (PMM) is dried.
- the supernatant from the PMM settling step is processed to remove a protein isolate comprising dried protein from wet PMM and supernatant.
- This procedure may be effected by initially concentrating the supernatant using ultrafiltration membranes, mixing the concentrated supernatant with the wet PMM and drying the mixture.
- the resulting canola protein isolate has a high purity of at least about 90 wt%, preferably at least about 100 wt%, protein (Nx 6.25).
- the supernatant from the PMM settling step is processed to recover a protein from the supernatant.
- This procedure may be effected by initially concentrating the supernatant using ultrafiltration membranes and drying the concentrate.
- the resulting canola protein isolate has a high purity of at least about 90 wt%, preferably at least about 100 wt%, protein (Nx 6.25).
- the continuous operation disclosed herein may be employed using the concentration and dilution conditions described in the Murray I and II patents but preferably, for the benefits described therein, the continuous operation described herein is preferably effected under the concentration and dilution conditions described in the aforementioned US Patent Applications Nos. 60/288,415, 60/326,987, 60/331,066, 60/333,494, 60/374,801 and 10/137,391.
- a process of preparing a protein isolate which comprises (a) continuously extracting an oil seed meal at a temperature of at least about 5°C to cause solubilization of protein in the oil seed meal and to form an aqueous protein solution having a pH of about 5 to about 6.8, (b) continuously separating the aqueous protein solution from residual oil seed meal, (c) continuously conveying the aqueous protein solution through a selective membrane operation to increase the protein concentration of the aqueous protein solution to at least about 50 g/L while maintaining the ionic strength substantially constant to provide a concentrated protein solution, (d) continuously mixing the concentrated protein solution with chilled water having a temperature of below about 15°C to cause the formation of protein micelles in the aqueous phase, (e) continuously flowing the resulting mixture into a settling vessel while permitting supernatant to overflow the vessel, (f) continuously permitting the protein micelles to settle in the settling vessel while continuing to overflow supernatant from the vessel until
- supernatant from the settling step is concentrated, batch-wise, semi-continuously or continuously, and the resulting concentrated supernatant is dried to provide a protein isolate having a protein content of at least about 90 wt% (Nx 6.25) on a dry weight basis.
- supernatant from the settling step is concentrated, batch-wise, semi-continuously or continuously, the resulting concentrated supernatant is mixed with the protein micellar mass prior to drying the same, and the resulting mixture is dried to provide a protein isolate having a protein content of at least about 90 wt% (Nx 6.25) on a dry weight basis.
- supernatant from the resulting step is concentrated, batch-wise, semi-continuously continuously, and a portion only of the resulting concentrated supernatant is mixed with at least a portion of the protein micellar mass prior to drying the same to provide other novel protein isolates according to the invention having a protein content of at least about 90 wt% (Nx 6.25) on a dry weight basis.
- the protein isolate produced according to the process herein may be used in conventional applications of protein isolates, such as, protein fortification of processed foods, emulsification of oils, body formers in baked goods and foaming agents in products which entrap gases.
- the protein isolate may be formed into protein fibers, useful in meat analogs, may be used as an egg white substitute or extender in food products where egg white is used as a binder.
- the canola protein isolate may be used as nutritional supplements. Other uses of the canola protein isolate are in pets foods, animal feed and in industrial and cosmetic applications and in personal care product.
- Figure 1 is a schematic flow sheet of a continuous procedure for producing an oil seed protein isolate in accordance with one embodiment of the invention.
- the initial step of the process of this invention involves solubilizing proteinaceous material from oil seed meal, particularly canola meal, although the process may be applied to other oil seed meals, such as soybean, traditional rapeseed, traditional flax, linola, sunflower and mustard oil seed meals.
- the invention is more particularly described herein with respect to canola seed meal, which may be low temperature desolventized meal.
- the proteinaceous material recovered from canola seed meal may be the protein naturally occurring in canola seed or other oil seed or the proteinaceous material may be a protein modified by genetic manipulation but possessing characteristic hydrophobic and polar properties of the natural protein.
- the canola meal may be any canola meal resulting from the removal of canola oil from canola seed with varying levels of non-denatured protem, resulting, for example, from hot hexane extraction or cold oil extrusion methods.
- Canola oil seed is also known as rapeseed or oil seed rape.
- a salt solution is used in the protein solubilization, and the salt usually is sodium chloride, although other salts suitable for protein extraction, such as, potassium chloride, may be used.
- the salt solution has an ionic strength of at least about 0.10, preferably at least about 0.15, to enable solubilization of significant quantities of protein to be effected.
- the ionic strength of the salt solution increases, the degree of solubilization of protein in the source material initially increases until a maximum value is achieved. Any subsequent increase in ionic strength does not increase the total protein solubilized.
- the ionic strength of the food grade salt solution which causes maximum protein solubilization varies depending on the salt concerned and the protein source chosen.
- ionic strength value less than about 0.8, and more preferably a value of about 0.15 to about 0.6.
- the salt solubilization step is effected rapidly, in a time of generally up to about 10 minutes, preferably to effect the solubilization to extract substantially as much protein from the source material as is practicable, so as to provide an overall high product yield.
- the solubilization preferably is effected at elevated temperatures, preferably above about 35 °C, generally up to about 65°C.
- the aqueous salt solution and the oil seed meal have a natural pH of about 5 to about 6.8 to enable the protein isolate to be formed by the micellar route, as described in more detail below.
- the optimum pH value for maximum yield of protein isolate varies depending on the protein source material chosen.
- the pH of the salt solution may be adjusted to any desired value within the range of about 5 to about 6.8 for use in the extraction step by the use of any convenient acid, usually hydrochloric acid, or alkali, usually sodium hydroxide, as required.
- any convenient acid usually hydrochloric acid, or alkali, usually sodium hydroxide, as required.
- concentration of protein source material in the salt solution during the solubilization step may vary widely. Typical concentration values are about 5 to about 15% w/v.
- the protein extraction step with the aqueous salt solution has the additional effect of solubilizing fats which may be present in the canola meal, which then results in the fats being present in the aqueous phase.
- the protein solution resulting from the extraction step generally has a protein concentration of about 5 to about 40 g/L, preferably about 10 to about 30 g/L.
- the extraction of the protein from the oil seed meal is carried out in any convenient manner consistent with effecting a continuous extraction of protein from the oil seed meal, such as by passing the mixture of oil seed meal and food grade salt solution through a conduit having a length and at a flow rate for a residence time sufficient to effect the desired extraction in accordance with the above-described parameters.
- the extraction procedure may be effected in a stirred tank into which the mixture of oil seed meal and salt solution is continuously fed and from which the aqueous protein solution is continuously removed.
- the procedure may be effected in a semi-continuous manner equivalent to continuous wherein a mixture of oil seed meal salt solution is ⁇ fed into a first stirred vessel in which the extraction is effected to form the aqueous protein solution while aqueous protein solution is continuously fed from a second stirred vessel to the residual meal separation step described below.
- the first vessel then becomes the first vessel and vice versa.
- the aqueous phase resulting from the extraction step then may be separated from the residual canola meal in any convenient manner, such as by employing vacuum filtration, followed by centrifugation and/or filtration to remove residual meal.
- the separated residual meal may be dried for disposal.
- the colour of the final protein isolate can be improved in terms of light colour and less intense yellow by the mixing of powdered activated carbon or other pigment adsorbing agent with the separated aqueous protein solution and subsequently removing the adsorbent, conveniently by filtration, to provide a protein solution. Diafiltration of the separated aqueous protein solution also may be used for pigment removal.
- Such pigment removal step may be carried out under any convenient conditions, generally at the ambient temperature of the separated aqueous protein solution, employing any suitable pigment adsorbing agent.
- any suitable pigment adsorbing agent for powdered activated carbon, an amount of about 0.025 to about 5 w/v, preferably about 0.05 to about 2 w/v, is employed.
- such extraction may be made using water alone, although the utilization of water alone tends to extract less protein from the oil seed meal than the aqueous salt solution.
- the salt in the concentrations discussed above, is added to the protein solution after separation from the residual oil seed meal in order to maintain the protein in solution during the concentration step.
- the salt generally is added after completion of such operations.
- Another alternative procedure is to extract the oil seed meal with the salt solution at a relatively high pH value above about pH 6.8, generally up to about 9.9.
- the pH of the salt solution may be adjusted in pH to the alkaline value by the use of any convenient alkali, such as aqueous sodium hydroxide solution.
- the oil seed meal may be extracted with the salt solution at a relatively low pH below about pH 5, generally down to about pH 3.
- the pH of the salt solution may be adjusted in pH to the acidic value by the use of any convenient acid, such as hydrochloric acid.
- the aqueous phase resulting from the oil seed meal extraction step then is separated from the residual canola meal, in any convenient manner, such as by employing vacuum filtration, followed by centrifugation and/or filtration to remove residual meal.
- the separated residual meal may be dried for disposal.
- the aqueous protein solution resulting from the high or low pH extraction step then is pH adjusted to the range of about 5 to about 6.8, preferably about 5.3 to about 6.2, as discussed above, prior to further processing as discussed below.
- pH adjustment may be effected using any convenient acid, such as hydrochloric acid, or alkali, such as sodium hydroxide, as appropriate.
- the aqueous protein solution then is concentrated to increase the protein concentration thereof while maintaining the ionic strength thereof substantially constant. Such concentration may be effected to provide a concentrated protein solution having a protein concentration of at least about 50 g/L.
- concentration is effected preferably to provide a concentrated protein solution having a protein concentration of at least about 200 g/L, more preferably at least about 250 g/L.
- the concentration step may be effected in any convenient manner consistent with a continuous operation, such as by employing any convenient selective membrane technique, such as ultrafiltration, using membranes, such as hollow-fibre membranes or spiral-wound membranes, with a suitable molecular weight cut-off, such as from about 3000 to about 50,000 daltons, having regard to differing membrane materials and configurations, and dimensioned to permit the desired degree of concentration of the aqueous protein solution as the aqueous protein solution passes through the membranes.
- any convenient selective membrane technique such as ultrafiltration
- membranes such as hollow-fibre membranes or spiral-wound membranes
- a suitable molecular weight cut-off such as from about 3000 to about 50,000 daltons
- the concentration step may be effected at any convenient temperature, generally about 20° to about 60°C, and for the period of time to effect the desired degree of concentration.
- the temperature and other conditions used to some degree depend upon the membrane equipment used to effect the concentration and the desired protein concentration of the solution.
- ultrafiltration and similar selective membrane techniques permit low molecular weight species to pass therethrough while preventing high molecular weight species from so doing.
- the low molecular weight species include not only the ionic species of the food grade salt but also low molecular weight materials extracted from the source material, such as, carbohydrates, pigments and anti-nutritional factors, as well as any low molecular weight forms of the protein.
- the molecular weight cut-off of the membrane is usually chosen to ensure retention of a significant proportion of the protein in the solution, while permitting contaminants to pass through having regard to the different membrane materials and configurations.
- the concentrated protein solution may be warmed to a temperature of about 20° to about 60°C, preferably about 25° to about 35°C, to decrease the viscosity of the concentrated protein solution to facilitate the subsequent dilution step and micelle formation.
- the concentrated protem solution should not be heated beyond a temperature above which the temperature of the concentrated protein solution does not permit micelle formation on dilution into chilled water.
- the concentrated protein solution may be subject to a further defatting operation, if required, as described in the aforementioned USPs 5,844,006 and 6,005,076.
- the concentrated protein solution resulting from the concentration step and optional defatting step then is diluted to effect micelle formation by mixing the concentrated protein solution with chilled water having the volume required to achieve degree of dilution desired.
- the degrees of dilution may be varied. With higher dilution levels, in general, a greater proportion of the canola protein remains in the aqueous phase.
- the concentrated protein solution is diluted by less than about 15 fold, more preferably about 10 fold or less.
- the dilution operation may be carried out by continuously passing the concentrated protein solution to one inlet of a T-shaped pipe while the diluting water is fed to the other inlet of the T-shaped pipe, permitting mixing in the pipe.
- the diluting water is fed into the T-shaped pipe at a rate sufficient to achieve the desired degree of dilution.
- the diluting water has a temperature of less than about 15°C, generally about 3° to about 15°C, preferably less than about 10°C, since improved yields of protein isolate in the form of protein micelles are attained with these colder temperatures at the dilution factors used.
- the mixing of the concentrated protein solution and the diluting water in the pipe initiates the formation of protem micelles and the mixture is continuously fed from the outlet from the T-shaped pipe into a settling vessel, from which, when full, supernatant is pennitted to overflow.
- the settling vessel may be initially charged full with chilled water which gradually is displaced by the inflowing mixture from the exit to the pipe.
- the mixture is fed into the body of liquid in the settling vessel in a manner which minimizes turbulence within the body of liquid to permit proper settling of the micelles.
- the mixture usually is fed from the outlet to the T- shaped pipe below the surface of the body of liquid in the settling vessel.
- the outlet may be configured and structured so that the liquid flows out of the pipe in a radial direction in the upper levels of the settling vessel.
- the protein micelles are allowed to settle in the settling vessel to form an aggregated, coalesced, dense amorphous gluten-like protein micellar mass (PMM) and the procedure is continued until a desired quantity of the PMM has accumulated in the bottom of the settling vessel, whereupon the accumulated PMM is removed from the settling vessel.
- the protein micellar mass may be subjected to centrifugation to decrease the liquid content of the mass prior to removal of accumulated PMM from the settling vessel. Centrifugation may decrease the moisture content of the protein micellar mass from about 70 wt% to about 95 wt% to a value of generally about 50% by weight to about 80 wt% of the total micellar mass. Decreasing the moisture content of the protein micellar mass in this way also decreases the occluded salt content of the protein micellar mass, and hence the salt content of dried isolate.
- the settling step may be effected under continuous centrifugation.
- the recovered PMM may be used in wet form or may be dried, by any convenient technique, such as spray drying, freeze drying or vacuum drum drying, to a dry form.
- the dry PMM has a high protein content of at least about 90 wt%, usually in excess of about 100 wt% protein (calculated as Kjeldahl Nx 6.25), and is substantially undenarured (as determined by differential scanning calorimetry).
- the dry PMM isolated from fatty oil seed meal also has a low residual fat content, when the procedure of the aforementioned US Patents Nos. 5,844,086 and 6,005,026 is employed, which may be below about 1 wt%.
- the supernatant from the PMM formation step may be processed to recover further protein therefrom.
- Such procedure may include an initial concentration of the supernatant.
- concentration is effected using any convenient selective membrane technique, such as ultrafiltration, using membranes with a suitable molecular weight cut-off permitting low molecular weight species, including salt and other non-proteinaceous low molecular weight material extracted from the protein source material, to pass through the membrane, while retaining canola protein in the solution.
- Ultrafiltration membranes having a molecular weight cut-off of about 3000 to about 10,000, having regard to differing membrane materials and configuration, may be used.
- the concentration preferably is effected continuously on the continuously overflowing supernatant, although a batch procedure on collected volumes of the overflowing supernatant may be employed, if desired.
- the membranes are dimensioned to permit the desired degree of concentration of the supernatant as the supernatant passes through the membranes.
- the supernatant generally is concentrated to a protein concentration of about 100 to about 400 g/L, preferably about 200 to about 300 g/L, prior to drying.
- the concentrated supernatant may be dried in any convenient manner, such as by spray drying, freeze drying or vacuum drum drying, to a dry form, to provide a , further canola protein isolate having a protein content of at least about 90 wt%, preferably at least about 100 wt%, (Nx 6.25), and which is substantially undenatured (as determined by differential scanning calorimetry).
- the concentrated supernatant may be mixed with the wet PMM and the resulting mixture dried, to provide a further canola protein isolate having protein content of at least about 90 wt%, preferably at least about 100 wt% (Nx 6.25) and which is substantially undenatured (as determined by differential scanning calorimetry).
- the remainder of the concentrated supernatant may be dried as may any of the remainder of the PMM. Further, dried PMM and dried supernatant also may be dry mixed in any desired relative proportions, as discussed above.
- FIG. 1 there is illustrated schematically a flow sheet of one embodiment to the invention.
- Canola oil seed meal and aqueous extraction medium are fed by lines 10 and 12 respectively to a blender 14 wherein the oil seed meal and aqueous extraction medium are mixed and the mixture is passed by line 16 to a mixing pipe 18.
- the oil seed meal is extracted and an aqueous protein solution is formed.
- the slurry of aqueous protein solution and residual oilseed meal is passed by line 20 to a vacuum filter belt 22 for separation of the residual oil seed meal which is removed by line 24.
- the aqueous protein solution then is passed by line 26 to a clarification operation 28 wherein the aqueous protem solution is centrifuged and filtered to remove fines, which are recovered by line 30.
- the clarified aqueous protein solution is pumped by line 32 through ultrafiltration membranes 34 sized to provide the desired degree of concentration of the aqueous protein solution to produce a concentrated protein solution as the retentate in line 36 with the permeate being recovered by line 38.
- the concentrated protein solution is passed into the inlet of a mixing tee 40, with cold water being fed thereto by line 42 in a volume sufficient to achieve the desired degree of dilution.
- the resulting solution is fed by line 44 to a settling tank 46 to permit the protein micellar mass to settle. Protein micellar mass settled in the settling vessel 46 is removed by line 48 from time to time and passed tlirough a spray dryer 50 to provide dry canola protein isolate 52.
- Supernatant from the settling tank is removed by line 54 and pumped through ultrafiltration membranes 52 to produce a concentrated protein solution as the retentate i line 58 with the permeate being removed by line 60.
- the concentrated protein solution is passed through a spray dryer 62 to provide further dry canola protein isolate 64.
- the concentrated protein solution in line 58 may be passed by line 66 to mix with the protein micellar mass before the mixture then is dried in spray dryer 50.
- Example 1 This Example illustrates . a continuous process for the production of canola protein isolate in accordance with one embodiment of the invention.
- 200 g of canola meal was added to 1350 ml (15 % w/v) of a 0.15M sodium chloride solution at 50°C.
- the resulting mixture was passed through tubing of a sufficient length to give 5 minutes total residence time of the mixture in the tubing. Analysis of the extract leaving the tubing showed a protein content of 20.5 g/L.
- salt solubilization (0.15 M NaCl) of a 15% w/v solution of canola meal achieved a protein content of 18.3 g/1 after 30 minutes of mixing at 24°C (Run BW-AH014-H29-01A).
- the mixture then passed from the outlet from the T-shaped connection pipe into a 50 litre settling vessel filled with 4°C water where the mixture exited the pipe through a outlet designed to minimize turbulence in the settling vessel.
- Supernatant was removed from the top of the settling vessel maintaining the vessel at a constant volume. The system ran for two hours.
- a boundary layer began to form between micelles and the supernatant. This layer moved upwards in the vessel for the first hour after winch it began to settle.
- a layer of precipitated, viscous sticky mass (PMM) was visible at the bottom of the settling vessel. As the run progressed, the PMM layer grew steadily in volume.
- the boundary layer between the settling micelles and the supernatant steadied at a level approximately even with the retentate/water outlet.
- the supernatant as it exited the settling vessel was clear and there were no visible micelles in the supernatant being removed.
- the PMM removed from the bottom of the vessel following the settling period had a solids content of 29.8 wt% and represented 49 wt% of the protein in the retentate.
- Example 2 [0069] This Example provides details of the batch procedures described in the preceding Example.
- This Example illustrates the application of the continuous extraction stage of the continuous process to mustard, non-GMO canola, high euricic acid rapeseed (H.E.A.R.), white flake canola meal and cold pressed canola meal.
- Oil seed meals were added to separate 500 ml aliquots of 55°C, 0.15 M
- Non-GMO Canola 10.7 mg/ml
- Example 4 This Example illustrates the application of the continuous dilution stage of the continuous process to mustard, non-GMO canola, high euricic acid rapeseed, white flake canola meal and cold pressed canola meal.
- Each clarified was concentrated on a Amicon mini stirred-cell concentration system using membranes of MWCO sufficient to retain the soluble protein while allowing water and contaminating small molecular weight material to pass through the permeate.
- Each protein solution was concentrated to 200 mg/ml or greater.
- the retentates were diluted in a continuous manner by using two peristaltic pumps and a t-shaped comiector.
- the pump speeds were adjusted to allow the first pump to move fluid at a rate 10 times faster than the first pump, to provide a dilution ratio of retentate to water of 1:10.
- the pumps were started simultaneously and the retentates and water were pumped into a common line through the t-shaped connector where they were mixed and micelle formation commenced.
- the resulting solutions were then passed into settling tanks where the precipitates were allowed to settle. Pellets of settled PMM were collected and freeze dried to calculate yield and protein content of each PMM formed.
- Tables HI and TV The results obtained for each seed are set forth in Tables HI and TV below:
- Protein content was determined as Kjeldahl nitrogen x 6.25. All PMM products formed were protein isolates.
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Priority Applications (14)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CA2467746A CA2467746C (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate |
MXPA04004731A MXPA04004731A (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate. |
BRPI0214313-5B1A BR0214313B1 (en) | 2001-11-20 | 2002-11-20 | continuous process for oilseed protein isolate production |
US10/496,071 US20070015910A1 (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate |
JP2003545128A JP4406286B2 (en) | 2001-11-20 | 2002-11-20 | Continuous production method of oilseed protein isolate |
KR1020047007750A KR100933766B1 (en) | 2001-11-20 | 2002-11-20 | Process for the Continuous Production of Oil Seed Protein Isolates |
DE60229283T DE60229283D1 (en) | 2001-11-20 | 2002-11-20 | CONTINUOUS METHOD FOR THE PRODUCTION OF OILSAAT PROTEIN ISOLATE |
DK02779080T DK1450621T3 (en) | 2001-11-20 | 2002-11-20 | Continuous process for producing oilseed protein isolate |
AU2002342482A AU2002342482B2 (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate |
NZ533541A NZ533541A (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate as opposed to a batch process |
EP02779080A EP1450621B1 (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate |
ZA2004/04707A ZA200404707B (en) | 2001-11-20 | 2004-06-14 | Continuous process for production of oil seed protein isolate |
HK05110107A HK1077983A1 (en) | 2001-11-20 | 2005-11-11 | Continuous process for production of oil seed pro tein isolate |
US12/230,303 US7625588B2 (en) | 2001-11-20 | 2008-08-27 | Continuous process for production of oil seed protein isolate |
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
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US33164601P | 2001-11-20 | 2001-11-20 | |
US60/331,646 | 2001-11-20 | ||
US38380902P | 2002-05-30 | 2002-05-30 | |
US60/383,809 | 2002-05-30 |
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US10496071 A-371-Of-International | 2002-11-20 | ||
US12/230,303 Continuation US7625588B2 (en) | 2001-11-20 | 2008-08-27 | Continuous process for production of oil seed protein isolate |
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WO2003043439A1 true WO2003043439A1 (en) | 2003-05-30 |
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PCT/CA2002/001775 WO2003043439A1 (en) | 2001-11-20 | 2002-11-20 | Continuous process for production of oil seed protein isolate |
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US (4) | US20070015910A1 (en) |
EP (1) | EP1450621B1 (en) |
JP (1) | JP4406286B2 (en) |
KR (1) | KR100933766B1 (en) |
CN (1) | CN100334963C (en) |
AT (1) | ATE410071T1 (en) |
AU (1) | AU2002342482B2 (en) |
BR (1) | BR0214313B1 (en) |
CA (1) | CA2467746C (en) |
DE (1) | DE60229283D1 (en) |
DK (1) | DK1450621T3 (en) |
ES (1) | ES2315413T3 (en) |
HK (1) | HK1077983A1 (en) |
MX (1) | MXPA04004731A (en) |
NZ (1) | NZ533541A (en) |
PT (1) | PT1450621E (en) |
RU (1) | RU2314705C2 (en) |
WO (1) | WO2003043439A1 (en) |
ZA (1) | ZA200404707B (en) |
Cited By (22)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2005067729A1 (en) | 2004-01-20 | 2005-07-28 | Burcon Nutrascience (Mb) Corp. | Novel canola protein isolate |
WO2005077201A1 (en) * | 2004-02-17 | 2005-08-25 | Burcon Nutrascience (Mb) Corp. | Preparation of canola protein isolate and use in aquaculture |
WO2005107492A1 (en) | 2004-05-07 | 2005-11-17 | Burcon Nutrascience (Mb) Corp. | Protein isolation procedures for reducing phytic acid |
WO2007003044A1 (en) | 2005-07-01 | 2007-01-11 | Burcon Nutrascience (Mb) Corp. | Production of canola protein |
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US8128974B2 (en) | 2001-05-04 | 2012-03-06 | Burcon Nutrascience (Mb) Corp. | Production of mustard seed protein isolate |
US7794762B2 (en) | 2001-05-04 | 2010-09-14 | Burcon Nutrascience (Mb) Corp. | Production of oil seed protein isolate |
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JP2007508001A (en) * | 2003-06-20 | 2007-04-05 | バーコン ニュートラサイエンス (エムビー) コーポレイション | Oilseed meal preparation |
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US11882850B2 (en) | 2014-08-27 | 2024-01-30 | Burcon Nutrascience (Mb) Corp. | Preparation of soy protein products (S810) |
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Also Published As
Publication number | Publication date |
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KR100933766B1 (en) | 2009-12-24 |
BR0214313A (en) | 2004-11-03 |
ES2315413T3 (en) | 2009-04-01 |
US20070015910A1 (en) | 2007-01-18 |
KR20050044564A (en) | 2005-05-12 |
CA2467746A1 (en) | 2003-05-30 |
AU2002342482A2 (en) | 2003-06-10 |
EP1450621B1 (en) | 2008-10-08 |
CN100334963C (en) | 2007-09-05 |
EP1450621A1 (en) | 2004-09-01 |
ATE410071T1 (en) | 2008-10-15 |
DK1450621T3 (en) | 2009-02-09 |
ZA200404707B (en) | 2005-08-31 |
HK1077983A1 (en) | 2006-03-03 |
CN1615083A (en) | 2005-05-11 |
US20040039174A1 (en) | 2004-02-26 |
AU2002342482A1 (en) | 2003-06-10 |
JP4406286B2 (en) | 2010-01-27 |
AU2002342482B2 (en) | 2008-04-03 |
US20080319171A1 (en) | 2008-12-25 |
DE60229283D1 (en) | 2008-11-20 |
JP2005509428A (en) | 2005-04-14 |
PT1450621E (en) | 2009-01-14 |
NZ533541A (en) | 2006-04-28 |
US7704534B2 (en) | 2010-04-27 |
CA2467746C (en) | 2012-10-02 |
US7625588B2 (en) | 2009-12-01 |
RU2004118486A (en) | 2005-05-10 |
MXPA04004731A (en) | 2004-07-30 |
BR0214313B1 (en) | 2013-09-24 |
RU2314705C2 (en) | 2008-01-20 |
US20090076252A1 (en) | 2009-03-19 |
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