PRODUCTION OF SOLUBLE PROTEIN SOLUTIONS FROM PULSES

Abstract

A pulse protein product, which may be an isolate, produces heat-stable solutions at low pH values and is useful for the fortification of acidic beverages such as soft drinks and sports drinks without precipitation of protein. The pulse protein product is obtained by extracting a pulse protein source material with an aqueous calcium salt solution to form an aqueous pulse protein solution, separating the aqueous pulse protein solution from residual pulse protein source, adjusting the pH of the aqueous pulse protein solution to a pH of about 1.5 to about 4.4 to produce an acidified pulse protein solution, which may be dried, following optional concentration and diafiltration, to provide the pulse protein product.

Claims

1. A method of producing a pulse protein product having a protein content of at least about 60 wt % (N×6.25) on a dry weight basis, which comprises: (a) extracting a pulse protein source with an aqueous calcium salt solution to cause solubilization of pulse protein from the protein source and to form an aqueous pulse protein solution, (b) at least partially separating the aqueous pulse protein solution from residual pulse protein source, (c) diluting the aqueous pulse protein solution to provide a diluted aqueous pulse protein solution, (d) adjusting the pH of the diluted aqueous pulse protein solution to a pH of about 1.5 to about 4.4 to produce an acidified aqueous pulse protein solution, (e) concentrating the acidified aqueous pulse protein solution formed in step (d) while maintaining the ionic strength substantially constant by a selective membrane technique to provide a concentrated pulse protein solution, (f) diafiltering the concentrated pulse protein solution to provide a concentrated and diafiltered pulse protein solution, and (g) drying the concentrated and diafiltered pulse protein solution, wherein said acidified pulse protein solution has a conductivity of less than about 95 mS.

2. The method of claim 1 wherein said aqueous calcium salt solution is an aqueous calcium chloride solution.

3. The method of claim 2 wherein said aqueous calcium chloride solution has a concentration less than about 1.0 M.

4. The method of claim 3 wherein said concentration is about 0.10 to about 0.15 M.

5. The process of claim 1 wherein said extraction step (a) is effected at a temperature of about 1° to about 100° C.

6. The process of claim 1 wherein said extraction with aqueous calcium salt solution is conducted at a pH of about 4.5 to about 11.

7. The process of claim 6 wherein said pH is about 5 to about 7.

8. The process of claim 1 wherein said aqueous pulse protein solution has a protein concentration of about 5 to about 50 g/L.

9. The process of claim 8 wherein said protein concentration is about 10 to about 50 g/L.

10. The process of claim 1 wherein said aqueous calcium salt solution contains an antioxidant.

11. The process of claim 1 wherein, following said separation step (b) and prior to said dilution step (c) or prior to said dilution step (c), said aqueous pulse protein solution is treated with an adsorbent to remove colour and/or odour compounds from the aqueous pulse protein solution.

12. The process of claim 1 wherein said aqueous pulse protein solution is diluted in step (c) to a conductivity of less than about 90 mS.

13. The process of claim 12 wherein said aqueous pulse protein solution is diluted in step (c) with about 0.5 to about 10 volumes of aqueous diluent to provide a conductivity of said pulse protein solution of about 4 to about 18 mS.

14. The process of claim 12 wherein said aqueous diluent has a temperature of about 1° to about 100° C.

15. The process of claim 14 wherein said temperature is about 15° to about 65° C.

16. The process of claim 15 wherein said temperature is about 50° to about 60° C.

17. (canceled)

18. The process of claim 1 wherein said conductivity is about 4 to about 23 mS.

19. The process of claim 1 wherein the pH of said aqueous pulse protein solution is adjusted in step (d) to about pH 2 to about 4.

20. The process of claim 1 wherein the acidified pulse protein solution is subjected to step (e).

21.-29. (canceled)

30. The process of claim 1 wherein said acidified aqueous pulse protein solution is dried to provide a pulse protein product having a protein content of at least about 60 wt % (N×6.25) d.b.

31. The process of claim 1 wherein said acidified aqueous pulse protein solution formed in step (d) is subjected to step (e) to produce a concentrated acidified pulse protein solution having a protein concentration of about 50 to about 300 g/L and the concentrated acidified pulse protein solution is subjected to step (f).

32. The process of claim 31 wherein said concentrated acidified pulse protein solution has a protein concentration of about 100 to about 200 g/L.

33. The process of claim 31 wherein said concentration step (e) is effected by ultrafiltration using a membrane having a molecular weight cut-off of about 3,000 to about 1,000,000 Daltons.

34. The process of claim 33 wherein said membrane has a molecular weight cut-off of about 5,000 to about 100,000 Daltons.

35. The process of claim 31 wherein step (f) is effected using water, acidified water, dilute saline or acidified dilute saline on the acidified pulse protein solution before or after partial or complete concentration thereof.

36. The process of claim 35 wherein said diafiltration step (f) is effected using about 1 to about 40 volumes of diafiltration solution.

37. The process of claim 36 wherein said diafiltration step (f) is effected using about 2 to about 25 volumes of diafiltration solution.

38. The process of claim 35 wherein said diafiltration step (f) is effected until no significant further quantities of contaminants or visible colour are present in the permeate.

39. The process of claim 35 wherein said diafiltration step (f) is effected until the retentate has been sufficiently purified so as, when dried, to provide a pulse protein isolate with a protein content of at least about 90 wt % (N×6.25) d.b.

40. The process of claim 35 wherein said diafiltration step (f) is effected using a membrane having a molecular weight cut-off of about 3,000 to about 1,000,000 Daltons.

41. The process of claim 40 wherein said membrane has a molecular weight cut-off of about 5,000 to about 100,000 Daltons.

42. The process of claim 35 wherein an antioxidant is present in the diafiltration medium during at least part of the diafiltration step (f).

43. The process of claim 31 wherein said concentration step (e) and diafiltration step (f) are carried out at a temperature of about 2° to about 65° C.

44. The process of claim 43 wherein said temperature is about 50° to about 60° C.

45. The process of claim 31 wherein partially concentrated or concentrated and diafiltered acidified pulse protein solution is subjected to a heat treatment step to inactivate heat-labile anti-nutritional factors, including heat-labile trypsin inhibitors.

46. The process of claim 45 wherein said heat treatment is effected at a temperature of about 70° to about 160° C. for about 10 seconds to about 60 minutes.

47. The process of claim 46 wherein the heat treated pulse protein solution is cooled to a temperature of about 2° to about 65° C. for further processing.

48. (canceled)

49. The process of claim 31 wherein said concentrated and optionally diafiltered acidified pulse protein solution is treated with an adsorbent to remove colour and/or odour compounds.

50. The process of claim 31 wherein said concentrated and diafiltered acidified pulse protein solution is pasteurized prior to drying.

51. The process of claim 50 wherein said pasteurization step is effected at a temperature of about 55° to about 70° C. for about 30 seconds to about 60 minutes.

52. The process of claim 51 wherein said pasteurization step is effected at a temperature of about 60° to about 65° C. for about 10 to about 15 minutes.

53. The process of claim 39 wherein said concentrated and diafiltered acidified pulse protein solution is subjected to step (h) to provide a pulse protein isolate having a protein content of at least about 90 wt % (N×6.25) d.b.

54. The process of claim 53 wherein said pulse protein isolate has a protein content of at least about 100 wt % (N×6.25) d.b.

55. The process of claim 31 wherein the concentration and diafiltration step are operated in a manner favourable to the removal of trypsin inhibitors.

56. The process of claim 1 wherein a reducing agent is present during the extraction step (a) to disrupt or rearrange the disulfide bonds of trypsin inhibitors to achieve a reduction in trypsin inhibitor activity.

57. The process of claim 31 wherein a reducing agent is present during the concentration and diafiltration steps (e) and (f) to disrupt or rearrange the disulfide bonds of trypsin inhibitors to achieve a reduction in trypsin inhibitor activity.

58. The process of claim 1 wherein a reducing agent is added to the concentrated and diafiltered pulse protein solution prior to the drying step (g) and/or the dried pulse protein product to disrupt or rearrange the disulfide bonds of trypsin inhibitors to achieve a reduction in trypsin inhibitor activity.

59-65. (canceled)

66. The process of claim 1 wherein steps (a) to (g) are effected without high-shear mixing after step (d).

59. A pulse protein product having a protein content of at least about 60 wt % (N×6.25) d.b. which is water soluble and produces heat stable solutions at acid pH values of less than about 4.4.

60. The pulse protein product of claim 59 having a protein content of at least about 90 wt % (N×6.25) d.b.

61. The protein product of claim 59 having a protein content of at least about 100 wt % (N×6.25) d.b.

62. The protein product of claim 59 which is blended with water-soluble powdered materials for the production of aqueous solutions of the blend.

63. The blend of claim 62 which is a powdered beverage.

64. An aqueous solution of the pulse protein product of claim 59 which is heat stable at a pH of less than about 4.4.

65. The aqueous solution of claim 64 which is a beverage.

Description

EXAMPLES

Example 1

[0061] This Example evaluates the protein extractability of lentils, chickpeas and dry peas and the effect of acidification on the clarity of protein solutions resulting from the extraction step.

[0062] Dry lentils, chickpeas, yellow split peas and green split peas were purchased in whole form and ground using a Bamix chopper until in the form of a relatively fine powder. The extent of grinding was not controlled by time or particle size. Ground material (10 g) was extracted with 0.15M CaCl.sub.2 (100 ml) for 30 minutes on a magnetic stirrer at room temperature. The extract was separated from the spent material by centrifugation at 10,200 g for 10 minutes and then further clarified by filtration with a 0.45 μm pore size syringe filter. The ground starting material and the clarified extract were tested for protein content using a Leco FP 528 Nitrogen Determinator. The clarity of the extract at full strength and diluted with 1 volume of reverse osmosis purified (RO) water was determined by measuring the absorbance at 600 nm (A600). The full strength and diluted solutions were then adjusted to pH 3 with HCl and the A600 measured again. In this and other Examples where solution clarity was assessed by A600 measurement, water was used to blank the spectrophotometer.

[0063] The protein contents and apparent extractabilities determined for each protein source are shown in Table 1.

TABLE-US-00001 TABLE 1 Protein content and apparent extractability of protein sources protein source protein content (%) apparent extractability (%) lentil 24.20 47.5 chickpeas 18.97 52.2 yellow split peas 23.07 59.4 green split peas 22.38 64.3

[0064] As may be seen from the results in Table 1, the apparent extractability of all the protein sources was quite good.

[0065] Clarity of the full strength and diluted extract samples before and after acidification are shown in Table 2.

TABLE-US-00002 TABLE 2 Effect of acidification on clarity of diluted and undiluted extract samples - calcium chloride extraction undiluted diluted initial initial final final initial initial final final sample pH A600 pH A600 pH A600 pH A600 lentils 5.22 0.093 3.04 0.253 5.30 1.196 2.96 0.037 chickpeas 5.15 0.189 3.07 0.228 5.25 2.714 2.79 0.099 yellow split 5.21 0.250 3.14 0.828 5.28 2.334 3.11 0.250 peas green split peas 5.23 0.288 3.18 0.577 5.31 2.248 2.97 0.161

[0066] As may be seen from the results of Table 2, full strength extract solutions from lentil, chickpea and split peas were clear to slightly hazy. Acidification without dilution increased the haze level in the samples. Dilution of the filtered extract with an equal volume of water resulted in notable precipitation and a corresponding increase in the A600 value. Acidification of the diluted solution largely re-solubilized the precipitate and resulted in a clear solution for lentils and chickpeas and a slightly hazy solution for the yellow and green split peas.

Example 2

[0067] This Example contains an evaluation of the clarity of acidified, diluted or undiluted green split pea extracts with water and sodium chloride replacing the calcium chloride solution of Example 1 as the extraction solution.

[0068] Dry green split peas were purchased in whole form and ground to a fine powder using a KitchenAid mixer grinder attachment. The extent of grinding was not controlled by time or particle size. Ground material (10 g) was extracted with 0.15M NaCl (100 ml) or RO water (100 ml) for 30 minutes on a magnetic stirrer at room temperature. The extract was separated from the spent material by centrifugation at 10,200 g for 10 minutes and then further clarified by filtration with a 0.45 μm pore size syringe filter. The clarity of the filtrates at full strength and diluted with 1 volume of RO water was determined by measuring the absorbance at 600 nm. The full strength and diluted solutions were then adjusted to pH 3 with HCl and the A600 measured again.

[0069] Clarity of the full strength and diluted extract samples before and after acidification are shown in Table 3.

TABLE-US-00003 TABLE 3 Effect of acidification on clarity of diluted and undiluted extract samples - water and sodium chloride extractions undiluted diluted extraction initial initial final final initial initial final final solution pH A600 pH A600 pH A600 pH A600 water 6.56 0.113 3.14 >3.0 6.62 0.050 3.00 2.647 0.15M NaCl 6.19 0.021 2.96 >3.0 6.28 0.870 2.87 2.851

[0070] As may be seen from the results in Table 3, extracts prepared with water or sodium chloride solution were very cloudy when acidified regardless of whether a dilution step was employed.

Example 3

[0071] This Example evaluates the protein extractability of several types of dry beans and the effect of acidification on the clarity of protein solutions resulting from the extraction step.

[0072] Pinto beans, small white beans, small red beans, romano beans, great northern beans and lima beans were purchased in whole, dry form and ground using a Bamix chopper until in the form of a relatively fine powder. The extent of grinding was not controlled by time or particle size. Black bean flour was also purchased. Ground material or flour (10 g) was extracted with 0.15M CaCl.sub.2) (100 ml) for 30 minutes on a magnetic stirrer at room temperature. The extract was separated from the spent material by centrifugation at 10,200 g for 10 minutes and then further clarified by filtration with a 0.45 μm pore size syringe filter. The ground starting material or flour and the clarified extract were tested for protein content using a Leco FP 528 Nitrogen Determinator. The clarity of the extract at full strength and diluted with 1 volume of RO water was determined by measuring the absorbance at 600 nm. The full strength and diluted solutions were then adjusted to pH 3 with HCl and the A600 measured again.

[0073] The protein contents and apparent extractabilities determined for each type of dry bean are shown in Table 4.

TABLE-US-00004 TABLE 4 Protein content and apparent extractability of various dry beans type of bean protein content (%) apparent extractability (%) black bean 24.00 77.9 pinto bean 21.45 66.2 small white bean 24.41 63.5 small red bean 20.18 76.8 romano bean 18.07 86.9 great northern bean 21.77 85.9 lima bean 21.43 71.9

[0074] As may be seen from the results in Table 4, the protein in all of the types of beans was readily extracted.

[0075] Clarity of the full strength and diluted extract samples before and after acidification are shown in Table 5.

TABLE-US-00005 TABLE 5 Effect of acidification on clarity of diluted and undiluted extract samples - calcium chloride extraction undiluted diluted 1 + 1 initial initial final final initial initial final final sample pH A600 pH A600 pH A600 pH A600 black bean 4.69 0.100 2.99 0.154 4.76 0.025 3.15 0.031 pinto bean 5.08 0.014 3.02 0.072 5.34 0.003 3.00 0.017 small white 5.08 0.026 3.03 0.092 5.23 0.022 3.03 0.019 bean small red bean 5.06 0.028 3.07 0.093 5.33 0.014 2.97 0.021 romano bean 4.96 n.d. 3.07 0.023 5.21 0.005 2.86 0.008 gr. northern 4.93 0.026 3.10 0.045 5.16 0.008 3.11 0.013 bean lima bean 5.13 n.d. 3.07 0.089 5.37 0.020 3.04 0.013 n.d. = not determined

[0076] As may be seen from the results of Table 5, full strength extract solutions from all of the beans were quite clear. Acidification without dilution slightly increased the haze level in the samples but they remained quite clear. Dilution of the filtered extract with an equal volume of water did not result in the formation of any precipitate. This is in contrast to the precipitation seen upon dilution for the pulses tested in Example 1. The diluted bean protein solutions stayed clear when acidified.

Example 4

[0077] This Example contains an evaluation of the clarity of acidified, diluted or undiluted small white bean extracts with water and sodium chloride replacing the calcium chloride solution of Example 3 as the extraction solution.

[0078] Dry small white beans were purchased in whole form and ground to a fine powder using a Bamix chopper. The extent of grinding was not controlled by time or particle size. Ground material (10 g) was extracted with 0.15M NaCl (100 ml) or RO water (100 ml) for 30 minutes on a magnetic stirrer at room temperature. The extract was separated from the spent material by centrifugation at 10,200 g for 10 minutes and then further clarified by filtration with a 0.45 μm pore size syringe filter. The protein content of the filtrates was determined using a Leco FP528 Nitrogen Determinator. The clarity of the extracts at full strength and diluted with 1 volume of RO water was determined by measuring the absorbance at 600 nm. The full strength and diluted solutions were then adjusted to pH 3 with HCl and the A600 measured again.

[0079] Extraction with water and sodium chloride solution provided apparent extractabilities of 45.9% and 61.5% respectively. Clarity of the full strength and diluted extract samples before and after acidification are shown in Table 6.

TABLE-US-00006 TABLE 6 Effect of acidification on clarity of diluted and undiluted extract samples - water and sodium chloride extractions undiluted diluted extraction initial initial final final initial initial final final solution pH A600 pH A600 pH A600 pH A600 water 6.48 0.079 2.95 >3.0 6.51 0.051 3.03 2.771 0.15M NaCl 6.13 0.116 3.01 >3.0 6.22 0.212 3.02 >3.0

[0080] As may be seen from the results in Table 6, extracts prepared with water or sodium chloride solution were very cloudy when acidified regardless of whether a dilution step was employed.

Example 5

[0081] This Example illustrates the production of green pea protein isolate at benchtop scale.

[0082] 180 g of dry green split peas were finely ground using a KitchenAid mixer grinder attachment. 150 g of finely ground green split pea flour was combined with 1,000 ml of 0.15 M CaCl.sub.2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed and the resulting protein solution was clarified by centrifugation and filtration to produce a filtered protein solution having a protein content of 1.83% by weight. 655 ml of the filtered protein solution was added to 655 ml of RO water and the pH of the sample lowered to 3.03 with HCl solution.

[0083] The diluted and acidified protein extract solution was reduced in volume from 1250 ml to 99 ml by concentration on a PES membrane having a molecular weight cutoff of 10,000 Daltons. An aliquot of 96 ml of concentrated protein solution was then diafiltered on the same membrane with 480 ml of RO water. The resulting acidified, diafiltered, concentrated protein solution had a protein content of 7.97% by weight and represented a yield of 65.5 wt % of the initial filtered protein solution that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 95.69% (N×6.25) d.b. The product was termed GP701-01 protein isolate.

[0084] 8.30 g of GP701-01 was produced. A solution of GP701-01 was prepared by dissolving sufficient protein powder to provide 0.48 g protein in 15 ml RO water and the pH measured with a pH meter and the colour and clarity assessed using a HunterLab Color Quest XE instrument operated in transmission mode. The results are shown in the following Table 7.

TABLE-US-00007 TABLE 7 pH and HunterLab scores for solution of GP701-01 sample pH L* a* b* haze GP701-01 3.17 89.46 1.10 14.98 63.3

[0085] As may be seen from the results in Table 7, the solution of GP701-01 was translucent and had a light colour.

[0086] The solution of GP701-01 was heated to 95° C., held at this temperature for 30 seconds and then immediately cooled to room temperature in an ice bath. The clarity was re-measured with the HunterLab instrument and the results are shown in Table 8.

TABLE-US-00008 TABLE 8 HunterLab scores for solution of GP701-01 after heat treatment sample L* a* b* haze GP701-01 95.56 −0.06 9.65 47.0

[0087] As may be seen from the results in Table 8, heat treatment was found to improve the lightness and reduce the haze level of the solution while making it greener and less yellow. Although the level of haze in the solution was reduced, the protein solution was still translucent rather than transparent.

Example 6

[0088] This Example illustrates the production of green pea protein isolate at benchtop scale but with the filtration step moved to after dilution and acidification of the extract.

[0089] 180 g of dry green split peas were finely ground using a KitchenAid mixer grinder attachment. 150 g of finely ground green split pea flour was combined with 1,000 ml of 0.15 M CaCl.sub.2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed by centrifugation to produce a centrate having a protein content of 2.49% by weight. 800 ml of centrate was added to 800 ml of water and the pH of the sample lowered to 3.00 with diluted HCl. The diluted and acidified centrate was further clarified by filtration to provide a clear protein solution with a protein content of 1.26% by weight. By filtering the solution after dilution and acidification, the A600 of the solution before membrane processing in this trial was 0.012, compared to 0.093 for the diluted and acidified filtrate in Example 5.

[0090] The filtered protein solution was reduced in volume from 1292 ml to 157 ml by concentration on a PES membrane having a molecular weight cutoff of 10,000 Daltons. An aliquot of 120 ml of concentrated protein solution was then diafiltered on the same membrane with 600 ml of RO water. The resulting acidified, diafiltered, concentrated protein solution had a protein content of 7.70% by weight and represented a yield of 42.5 wt % of the initial centrate that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 94.23% (N×6.25) d.b. The product was termed GP701-02 protein isolate.

[0091] 8.55 g of GP701-02 was produced. A solution of GP701-02 was prepared by dissolving sufficient protein powder to provide 0.48 g protein in 15 ml of RO water and the pH measured with a pH meter and the colour and clarity assessed using a HunterLab Color Quest XE instrument operated in transmission mode. The results are shown in the following Table 9.

TABLE-US-00009 TABLE 9 pH and HunterLab scores for solution of GP701-02 sample pH L* a* b* haze GP701-02 3.23 90.78 0.77 14.00 47.2

[0092] As may be seen from the results in Table 9, the GP701-02 solution was translucent and had a light colour. The level of haze was lower than that determined for the solution of GP701-01 in Example 5.

[0093] The solution of GP701-02 was heated to 95° C., held at this temperature for 30 seconds and then immediately cooled to room temperature in an ice bath. The clarity was then re-measured with the HunterLab and the result is shown in Table 10 below.

TABLE-US-00010 TABLE 10 HunterLab scores for solution of GP701-02 after heat treatment sample L* a* b* haze GP701-02 96.24 −0.48 9.74 2.2

[0094] As may be seen from the results in Table 10, heat treatment of the GP701-02 solution resulted in an extremely clear solution.

Example 7

[0095] This Example illustrates the production of small white bean protein isolate at benchtop scale.

[0096] About 150 g of small white beans were finely ground using a KitchenAid mixer grinder attachment. 120 g of finely ground small white bean flour was combined with 1,000 ml of 0.15 M CaCl.sub.2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed and the resulting protein solution was clarified by centrifugation and filtration to produce a filtered protein solution having a protein content of 2.02% by weight. 600 ml of the filtered protein solution was added to 600 ml of RO water and the pH of the sample lowered to 3.01 with diluted HCl. Some wispy particulates were visible in the sample after the pH adjustment and these were removed by passing the sample through 25 μm pore size filter paper.

[0097] A sample of the diluted and acidified protein extract solution was then reduced in volume from 1110 ml to 82 ml by concentration on a PES membrane having a molecular weight cutoff of 10,000 Daltons. An aliquot of 79 ml of the retentate was then diafiltered on the same membrane with 395 ml of RO water. The resulting acidified, diafiltered, concentrated protein solution had a protein content of 10.37% by weight and represented a yield of 67.6 wt % of the initial filtered protein solution that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 93.75% (N×6.25) d.b. The product was termed SWB701 protein isolate.

[0098] 8.26 g of SWB701 was produced. A solution of SWB701 was prepared by dissolving sufficient protein powder to provide 0.48 g protein in 15 ml RO water and the pH measured with a pH meter and the colour and clarity assessed using a HunterLab Color Quest XE instrument operated in transmission mode. The results are shown in the following Table 11.

TABLE-US-00011 TABLE 11 pH and HunterLab scores for solution of SWB701 sample pH L* a* b* haze SWB701 3.09 97.42 0.22 5.29 73.2

[0099] As may be seen from the results in Table 11, the solution of SWB701 was translucent and had a light colour.

[0100] The solution of SWB701 was heated to 95° C., held at this temperature for 30 seconds and then immediately cooled to room temperature in an ice bath. The clarity was re-measured with the HunterLab instrument and the results are shown in Table 12.

TABLE-US-00012 TABLE 12 HunterLab scores for solution of SWB701 after heat treatment sample L* a* b* haze SWB701 98.57 −0.17 4.05 50.0

[0101] As may be seen from the results in Table 12, heat treatment was found to improve the lightness and reduce the haze level of the solution while making it greener and less yellow. Although the level of haze in the solution was reduced, the protein solution was still translucent rather than transparent.

Example 8

[0102] This Example contains an evaluation of the solubility in water of the GP701-02 produced by the method of Example 6 and the SWB701 produced by the method of Example 7. Solubility was tested using a modified version of the procedure of Morr et al., J. Food Sci. 50:1715-1718.

[0103] Sufficient protein powder to supply 0.5 g of protein was weighed into a beaker and then approximately 45 ml of reverse osmosis (RO) purified water was added. The contents of the beaker were slowly stirred for 60 minutes using a magnetic stirrer. The pH was determined immediately after dispersing the protein and was adjusted to the appropriate level (2, 3, 4, 5, 6 or 7) with diluted NaOH or HCl. A sample was also prepared at natural pH. For the pH adjusted samples, the pH was measured and corrected periodically during the 60 minutes stirring. After the 60 minutes of stirring, the samples were made up to 50 ml total volume with RO water, yielding a 1% w/v protein dispersion. The protein content of the dispersions was measured using a Leco FP528 Nitrogen Determinator. Aliquots of the dispersions were then centrifuged at 7,800 g for 10 minutes, which sedimented insoluble material. The protein content of the supernatant was then determined by Leco analysis.

[0104] The solubility of the protein was then calculated using the following equation:

Solubility (%)=(% protein in supernatant/% protein in initial dispersion)×100

[0105] The natural pH values of the protein isolates produced in Examples 6 and 7 are shown in the following Table 13:

TABLE-US-00013 TABLE 13 Natural pH of samples prepared in water at 1% w/v protein sample Natural pH GP701-02 3.23 SWB701 3.09

[0106] The solubility results obtained are set forth in the following Table 14:

TABLE-US-00014 TABLE 14 Solubility of products at different pH values Solubility (%) sample pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH GP701-02 100 100 100 31.1 35.7 37.8 100 SWB701 95.2 95.3 100 88.8 55.4 77.5 94.0

[0107] As can be seen from the results of Table 14, both of the 701 products were extremely soluble over the pH range 2 to 4.

Example 9

[0108] This Example contains an evaluation of the clarity in water of the GP701-02 produced by the method of Example 6 and the SWB701 produced by the method of Example 7.

[0109] The clarity of the 1% w/v protein dispersions prepared as described in Example 8 was assessed by analyzing the samples on a HunterLab ColorQuest XE instrument operated in transmission mode to provide a percentage haze reading. A lower score indicated greater clarity.

[0110] The clarity results are set forth in the following Table 15:

TABLE-US-00015 TABLE 15 Clarity of solutions at different pH values as assessed by HunterLab analysis HunterLab haze reading (%) sample pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH GP701-02 11.9 16.3 17.4 91.8 92.1 92.0 14.0 SWB701 0.0 38.0 64.6 91.7 92.4 82.9 43.9

[0111] As can be seen from the results of Table 15, the solutions of GP701-02 were substantially clear or slightly hazy in the pH range 2 to 4. The solutions of GP701-02 were cloudy at the higher pH values where the solubility was reduced. The solution of SWB701 had no detectable haze at pH 2, but was noticeably hazier as the pH increased. Note that the protein solubility was still very high in the pH range 3 to 4 even though the solutions were not clear.

Example 10

[0112] This Example illustrates the production of black bean protein product at benchtop scale.

[0113] 50 g of black bean flour was combined with 500 ml of 0.15 M CaCl.sub.2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed and the resulting protein solution was clarified by centrifugation and filtration to produce a filtered protein solution having a protein content of 1.18% by weight. 450 ml of the filtered protein solution was added to 450 ml of RO water and the pH of the sample lowered to 3.09 with diluted HCl.

[0114] The diluted and acidified protein extract solution was then reduced in volume from 900 ml to 50 ml by concentration on a PES membrane having a molecular weight cutoff of 10,000 Daltons. An aliquot of 40 ml of the retentate was then diafiltered on the same membrane with 200 ml of RO water. The resulting acidified, diafiltered, concentrated protein solution had a protein content of 6.23% by weight and represented a yield of approximately 46.9 wt % of the initial filtered protein solution that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 86.33% (N×6.25) d.b. The product was termed BB701.

[0115] 2.19 g of BB701 was produced. A solution of BB701 was prepared by dissolving sufficient protein powder to provide 0.48 g protein in 15 ml of RO water and the pH measured with a pH meter and the colour and clarity assessed using a HunterLab Color Quest XE instrument operated in transmission mode. The results are shown in the following Table 16.

TABLE-US-00016 TABLE 16 pH and HunterLab scores for solution of BB701 sample pH L* a* b* haze BB701 3.14 95.20 0.88 8.22 54.6

[0116] As may be seen from the results in Table 16, the solution of BB701 was translucent and had a light colour.

[0117] The solution of BB701 was heated to 95° C., held at this temperature for 30 seconds and then immediately cooled to room temperature in an ice bath. The clarity was re-measured with the HunterLab instrument and the results are shown in Table 17

TABLE-US-00017 TABLE 17 HunterLab scores for solution of BB701 after heat treatment sample L* a* b* haze BB701 95.89 0.54 7.81 25.2

[0118] As may be seen from the results in Table 17, heat treatment was found to improve the lightness and reduce the haze level of the solution while making it less red and less yellow. Although the level of haze in the solution was reduced, the protein solution was still hazy rather than transparent.

Example 11

[0119] This Example illustrates the production of yellow pea protein isolate at pilot scale.

[0120] 20 kg of yellow split pea flour was combined with 200 L of 0.15 M CaCl.sub.2 solution at ambient temperature and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed by centrifugation to produce a centrate having a protein content of 1.53% by weight. 180.4 L of centrate was added to 231.1 L of RO water and the

[0121] The filtered protein solution was reduced in volume from 431 L to 28 L by concentration on a PES membrane, having a molecular weight cutoff of 100,000 Daltons, operated at a temperature of about 30° C. At this point the acidified protein solution, with a protein content of 6.35% by weight, was diafiltered with 252 L of RO water, with the diafiltration operation conducted at about 30° C. The resulting diafiltered solution was then further concentrated to provide 21 kg of acidified, diafiltered, concentrated protein solution with a protein content of 7.62% by weight, which represented a yield of 58.0 wt % of the initial centrate that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 103.27 wt % (N×6.25) d.b. The product was termed YP01-D11-11A YP701 protein isolate.

Example 12

[0122] This Example contains an evaluation of the protein and phytic acid content as well as the trypsin inhibitor activity of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB).

[0123] Protein content was determined by a combustion method using a LecoTruSpec N Nitrogen Determinator. Phytic acid content was determined using the method of Latta and Eskin (J. Agric. Food Chem., 28: 1313-1315). Trypsin inhibitor activity (TTA) was determined using AOCS method Ba 12-75 for the commercial protein sample and a modified version of this method for the YP701 product, which has a lower pH when rehydrated.

[0124] The results obtained are set forth in the following Table 18:

TABLE-US-00018 TABLE 18 Protein content, phytic acid content and trypsin inhibitor activity of protein products % protein % phytic TIA (TIU/mg (N × 6.25) acid protein Batch Product d.b. d.b. (N × 6.25)) YP01-D11-11A YP701 103.27 0.27 4.6 Propulse 82.33 2.72 3.3

[0125] As may be seen from the results presented in Table 18, the YP701 was very high in protein and low in phytic acid compared to the commercial product. The trypsin inhibitor activity in both products was very low.

Example 13

[0126] This Example contains an evaluation of the dry colour and colour in solution of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB).

[0127] The colour of the dry powders was assessed using a HunterLab ColorQuest XE instrument in reflectance mode. The colour values are set forth in the following Table 19:

TABLE-US-00019 TABLE 19 HunterLab scores for dry protein products Sample L* a* b* YP01-D11-11A YP701 86.27 2.21 9.73 Propulse 82.39 3.29 20.94

[0128] As may be seen from Table 19, the YP01-D11-11A YP701 powder was lighter, less red and less yellow in colour compared to the commercial yellow pea protein product.

[0129] Solutions of the yellow pea protein products were prepared by dissolving sufficient protein powder to supply 0.48 g of protein in 15 ml of RO water. The pH of the solutions was measured with a pH meter and the colour and clarity assessed using a HunterLab Color Quest XE instrument operated in transmission mode. Hydrochloric acid solution was added to the Propulse sample to lower the pH to 3 and then the measurement repeated. The results are shown in the following Table 20.

TABLE-US-00020 TABLE 20 pH and HunterLab scores for solutions of yellow pea protein products sample pH L* a* b* haze YP01-D11-11A YP701 3.45 93.97 0.54 12.70 5.0 Propulse 6.15 35.33 12.61 48.79 96.6 Propulse (pH adjusted) 3.00 37.83 11.55 47.87 96.9

[0130] As may be seen from the results in Table 20, the YP01-D11-11A YP701 solution was transparent while the Propulse solution was very cloudy regardless of pH. The YP01-D11-11A YP701 solution was also much lighter, less red and less yellow than the Propulse solution regardless of its pH.

Example 14

[0131] This Example contains an evaluation of the heat stability in water of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB).

[0132] 2% w/v protein solutions of YP01-D11-11A YP701 and Propulse were prepared in RO water. The natural pH of the solutions was determined with a pH meter. The samples were each split into two portions and the pH of one portion was lowered to 3.00 with HCl solution. The clarity of the control and pH adjusted solutions was assessed by haze measurement with the HunterLab Color Quest XE instrument operated in transmission mode. The solutions were then heated to 95° C., held at this temperature for 30 seconds and then immediately cooled to room temperature in an ice bath. The clarity of the heat treated solutions was then measured again.

[0133] The clarity of the protein solutions before and after heating is set forth in the following Table 21:

TABLE-US-00021 TABLE 21 Effect of heat treatment on clarity of 2% w/v protein solutions of yellow pea protein products haze before heat haze after heat Sample pH treatment (%) treatment (%) YP01-D11-11A YP701 3.70 3.6 1.4 YP01-D11-11A YP701 (pH adjusted) 3.00 2.8 1.3 Propulse 6.24 96.1 96.4 Propulse (pH adjusted) 3.00 96.6 96.6

[0134] As can be seen from the results in Table 21, the solutions of YP01-D11-11A YP701 were transparent before and after heating at both pH levels. The solutions of Propulse were highly cloudy before and after heating at both pH levels.

Example 15

[0135] This Example contains an evaluation of the solubility in water of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB). Solubility was tested based on protein solubility (termed protein method, a modified version of the procedure of Morr et al., J. Food Sci. 50:1715-1718) and total product solubility (termed pellet method).

[0136] Sufficient protein powder to supply 0.5 g of protein was weighed into a beaker and then a small amount of reverse osmosis (RO) purified water was added and the mixture stirred until a smooth paste formed. Additional water was then added to bring the volume to approximately 45 ml. The contents of the beaker were then slowly stirred for 60 minutes using a magnetic stirrer. The pH was determined immediately after dispersing the protein and was adjusted to the appropriate level (2, 3, 4, 5, 6 or 7) with diluted NaOH or HCl. A sample was also prepared at natural pH. For the pH adjusted samples, the pH was measured and corrected periodically during the 60 minutes stirring. After the 60 minutes of stirring, the samples were made up to 50 ml total volume with RO water, yielding a 1% w/v protein dispersion. The protein content of the dispersions was measured using a Leco TruSpec N Nitrogen Determinator. Aliquots (20 ml) of the dispersions were then transferred to pre-weighed centrifuge tubes that had been dried overnight in a 100° C. oven then cooled in a desiccator and the tubes capped. The samples were centrifuged at 7,800 g for 10 minutes, which sedimented insoluble material and yielded a clear supernatant. The protein content of the supernatant was measured by Leco analysis and then the supernatant and the tube lids were discarded and the pellet material dried overnight in an oven set at 100° C. The next morning the tubes were transferred to a desiccator and allowed to cool. The weight of dry pellet material was recorded. The dry weight of the initial protein powder was calculated by multiplying the weight of powder used by a factor of ((100−moisture content of the powder (%))/100). Solubility of the product was then calculated two different ways:

Solubility (protein method) (%)=(% protein in supernatant/% protein in initial dispersion)×100  1)

Solubility (pellet method) (%)=(1−(weight dry insoluble pellet material/((weight of 20 ml of dispersion/weight of 50 ml of dispersion)×initial weight dry protein powder)))×100  2)

[0137] The natural pH values of the protein isolate produced in Example 11 and the commercial yellow pea protein product in water (1% protein) are shown in Table 22:

TABLE-US-00022 TABLE 22 Natural pH of YP01-D11-11A YP701 and Propulse solutions prepared in water at 1% protein Batch Product Natural pH YP01-D11-11A YP701 3.56 Propulse 6.15

[0138] The solubility results obtained are set forth in the following Tables 23 and 24:

TABLE-US-00023 TABLE 23 Solubility of products at different pH values based on protein method Solubility (protein method) (%) Batch Product pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH YP01-D11-11A YP701 98.2 99.1 99.5 50.9 20.4 39.3 100 Propulse 14.9 3.6 2.6 5.3 10.3 7.0 8.0

TABLE-US-00024 TABLE 24 Solubility of products at different pH values based on pellet method Solubility (pellet method) (%) Batch Product pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH YP01-D11-11A YP701 99.6 99.3 99.1 74.7 34.7 39.1 99.0 Propulse 15.5 14.7 11.6 12.1 16.4 18.0 16.5

[0139] As can be seen from the results presented in Table 23 and 24, the YP01-D11-11A YP701 was highly soluble in the pH range of 2 to 4 and less soluble at higher pH values. The Propulse was very poorly soluble at all pH values tested.

Example 16

[0140] This Example contains an evaluation of the clarity in water of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB).

[0141] The clarity of the 1% w/v protein solutions prepared as described in Example 15 was assessed by measuring the absorbance at 600 nm, with a lower absorbance score indicating greater clarity. Analysis of the samples on a HunterLab ColorQuest XE instrument in transmission mode also provided a percentage haze reading, another measure of clarity.

[0142] The clarity results are set forth in the following Tables 25 and 26:

TABLE-US-00025 TABLE 25 Clarity of protein solutions at different pH values as assessed by A600 A600 Batch Product pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH YP01-D11-11A YP701 0.012 0.015 0.024 1.962 2.829 2.557 0.021 Propulse 2.576 2.579 2.693 2.685 2.588 2.560 2.590

TABLE-US-00026 TABLE 26 Clarity of protein solutions at different pH values as assessed by HunterLab haze analysis HunterLab haze reading (%) Batch Product pH 2 pH 3 pH 4 pH 5 pH 6 pH 7 Nat. pH YP01-D11-11A YP701 0.0 0.1 1.1 95.9 96.7 96.4 0.7 Propulse 96.2 96.3 96.7 96.7 96.2 96.4 96.4

[0143] As can be seen from the results of Tables 25 and 26, the solutions of YP01-D11-11A YP701 were transparent in the range of pH 2 to 4 but very cloudy at higher pH values. The solutions of Propulse were very cloudy regardless of pH.

Example 17

[0144] This Example contains an evaluation of the solubility in a soft drink (Sprite) and sports drink (Orange Gatorade) of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB). The solubility was determined with the protein added to the beverages with no pH correction and again with the pH of the protein fortified beverages adjusted to the level of the original beverages.

[0145] When the solubility was assessed with no pH correction, a sufficient amount of protein powder to supply 1 g of protein was weighed into a beaker and a small amount of beverage was added and stirred until a smooth paste formed. Additional beverage was added to bring the volume to 50 ml, and then the solutions were stirred slowly on a magnetic stirrer for 60 minutes to yield a 2% protein w/v dispersion. The protein content of the samples was analyzed using a Leco TruSpec N Nitrogen Determinator then an aliquot of the protein containing beverages was centrifuged at 7,800 g for 10 minutes and the protein content of the supernatant measured.

Solubility (%)=(% protein in supernatant/% protein in initial dispersion)×100.

[0146] When the solubility was assessed with pH correction, the pH of the soft drink (Sprite) (3.42) and sports drink (Orange Gatorade) (3.11) without protein was measured. A sufficient amount of protein powder to supply 1 g of protein was weighed into a beaker and a small amount of beverage was added and stirred until a smooth paste formed. Additional beverage was added to bring the volume to approximately 45 ml, and then the solutions were stirred slowly on a magnetic stirrer for 60 minutes. The pH of the protein containing beverages was determined immediately after dispersing the protein and was adjusted to the original no-protein pH with HCl or NaOH as necessary. The pH was measured and corrected periodically during the 60 minutes stirring. After the 60 minutes of stirring, the total volume of each solution was brought to 50 ml with additional beverage, yielding a 2% protein w/v dispersion. The protein content of the samples was analyzed using a Leco TruSpec N Nitrogen Determinator then an aliquot of the protein containing beverages was centrifuged at 7,800 g for 10 minutes and the protein content of the supernatant measured.

Solubility (%)=(% protein in supernatant/% protein in initial dispersion)×100

[0147] The results obtained are set forth in the following Table 27:

TABLE-US-00027 TABLE 27 Solubility of yellow pea protein products in Sprite and Orange Gatorade no pH correction pH correction Solubility (%) Solubility (%) in Solubility (%) Solubility (%) in Batch Product in Sprite Orange Gatorade in Sprite Orange Gatorade YP01-D11-11A YP701 98.1 100 96.6 100 Propulse 3.2 4.6 5.6 7.4

[0148] As can be seen from the results of Table 27, the YP01-D11-11A YP701 was highly soluble in the Sprite and the Orange Gatorade. As the YP701 is an acidified product, its addition did not significantly alter the pH of the beverages. The Propulse was very poorly soluble in the beverages tested. Addition of Propulse increased the pH of the drinks but the solubility of the protein was not improved by lowering the pH of the drink back to its original no-protein value.

Example 18

[0149] This Example contains an evaluation of the clarity in a soft drink and sports drink of the yellow pea protein isolate produced by the method of Example 11 and a commercial yellow pea protein product called Propulse (Nutri-pea, Portage la Prairie, MB).

[0150] The clarity of the 2% w/v protein dispersions prepared in soft drink (Sprite) and sports drink (Orange Gatorade) in Example 17 were assessed using the A600 and HunterLab haze methods described in Example 16.

[0151] The results obtained are set forth in the following Tables 28 and 29:

TABLE-US-00028 TABLE 28 A600 readings for yellow pea protein products in Sprite and Orange Gatorade no pH correction pH correction A600 in A600 in A600 in Orange A600 in Orange Batch Product Sprite Gatorade Sprite Gatorade no protein 0.007 0.450 0.007 0.450 YP01-D11-11A YP701 0.048 0.338 0.043 0.345 Propulse 2.800 2.834 2.827 2.793

TABLE-US-00029 TABLE 29 HunterLab haze readings for yellow pea protein products in Sprite and Orange Gatorade no pH correction pH correction Haze Haze (%) Haze Haze (%) (%) in in Orange (%) in in Orange Batch Product Sprite Gatorade Sprite Gatorade no protein 0.0 78.6 0.0 786 YP01-D11-11A YP701 5.7 56.7 4.9 57.7 Propulse 97.1 97.5 96.3 96.3

[0152] As can be seen from the results of Tables 28 and 29, the addition of YP01-D11-11A YP701 to the soft drink and sports drink added little or no haziness, while the addition of the Propulse made the drinks very cloudy, even when the pH was corrected.

Example 19

[0153] This Example illustrates the production of yellow pea protein isolate at pilot scale.

[0154] 20 kg of yellow split pea flour was combined with 200 L of 0.15 M CaCl.sub.2 solution at 60° C. and agitated for 30 minutes to provide an aqueous protein solution. The residual solids were removed by centrifugation to produce a centrate having a protein content of 1.32% by weight. 186.5 L of centrate was added to 225.8 L of RO water at 60° C. and the pH of the sample lowered to 3.34 with diluted HCl. The diluted and acidified centrate was further clarified by filtration to provide a clear protein solution with a protein content of 0.58% by weight.

[0155] The filtered protein solution was reduced in volume from 400 L to 35 L by concentration on a polyethersulfone membrane, having a molecular weight cutoff of 100,000 Daltons, operated at a temperature of about 58° C. At this point the acidified protein solution, with a protein content of 4.94 wt %, was diafiltered with 350 L of RO water, with the diafiltration operation conducted at about 60° C. The resulting diafiltered solution was then further concentrated to provide 21.52 kg of acidified, diafiltered, concentrated protein solution with a protein content of 7.54% by weight, which represented a yield of 65.9 wt % of the initial centrate that was further processed. The acidified, diafiltered, concentrated protein solution was dried to yield a product found to have a protein content of 103.19 wt % (N×6.25) d.b. The product was termed YP01-E19-11A YP701 protein isolate.

Example 20

[0156] This Example illustrates a comparison of the flavor of the YP701, prepared as described in Example 19 with that of a commercial yellow pea protein product called Nutralys S85F (Roquette America, Inc. Keokuk, Iowa), with the evaluation done at low pH.

[0157] Samples were prepared for sensory evaluation by dissolving sufficient protein powder to supply 5 g of protein in 250 ml purified drinking water. The pH of the solution of YP701 was determined to be 3.78. Food grade HCl was added to the solution of Nutralys S85F to lower the pH from 7.25 to 3.78. An informal panel of seven panelists was asked to blindly compare the samples and indicate which sample had a cleaner flavour, and of which sample they preferred the flavour.

[0158] Seven out of seven panelists indicated that the YP701 had a cleaner flavour. Seven out of seven panelists preferred the flavour of the YP701.

Example 21

[0159] This Example illustrates a comparison of the flavour of the YP701, prepared as described in Example 19 with that of the commercial yellow pea protein product Nutralys S85F, with the evaluation done at near neutral pH.

[0160] Samples were prepared for sensory evaluation by dissolving sufficient protein powder to supply 5 g of protein in 250 ml purified drinking water. The pH of the solution of Nutralys S85F was determined to be 7.32. Food grade NaOH was added to the solution of YP701 to raise the pH from 3.67 to 7.32. An informal panel of eight panelists was asked to blindly compare the samples and indicate which sample had a cleaner flavour, and of which sample they preferred the flavour.

[0161] Six out of eight panelists indicated that the YP701 had a cleaner flavour. Six out of eight panelists preferred the flavour of the YP701.

Example 22

[0162] This Example illustrates a comparison of the flavour of the YP701, prepared as described in Example 19 with that a commercial yellow pea protein product called Propulse (Nutri-Pea, Portage la Prairie, MB), with the evaluation done at low pH.

[0163] Samples were prepared for sensory evaluation by dissolving sufficient protein powder to supply 5 g of protein in 250 ml purified drinking water. The pH of the solution of YP701 was determined to be 3.78. Food grade HCl was added to the solution of Propulse to lower the pH from 6.17 to 3.78. An informal panel of seven panelists was asked to blindly compare the samples and indicate which sample had a cleaner flavour, and of which sample they preferred the flavour.

[0164] Six out of seven panelists indicated that the YP701 had a cleaner flavour. Seven out of seven panelists preferred the flavour of the YP701.

Example 23

[0165] This Example illustrates a comparison of the flavour of the YP701, prepared as described in Example 19 with that of the commercial yellow pea protein product called Propulse, with the evaluation done at near neutral pH.

[0166] Samples were prepared for sensory evaluation by dissolving sufficient protein powder to supply 5 g of protein in 250 ml purified drinking water. The pH of the solution of Propulse was determined to be 6.18. Food grade NaOH was added to the solution of YP701 to raise the pH from 3.78 to 6.18. An informal panel of eight panelists was asked to blindly compare the samples and indicate which sample had a cleaner flavour, and of which sample they preferred the flavour.

[0167] Seven out of eight panelists indicated that the YP701 had a cleaner flavour. Six out of eight panelists preferred the flavour of the YP701.

SUMMARY OF THE DISCLOSURE

[0168] In summary of this disclosure, the present invention provides novel pulse protein products which are completely soluble and form heat stable, preferably transparent, solutions at acid pH and are useful in the protein fortification of aqueous systems, including soft drinks and sport drinks, without leading to protein precipitation. Modifications are possible within the scope of this invention.