DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Receipt is acknowledged of the Request for Continued Examination (RCE) under 1.114, the Amendment and Response, all filed 01/22/26.
Claims 1, 2, 4-8, 11-13, and 17-20 are pending and are rejected in this action. Claims 3, 9, 10, 14-16 were previously cancelled. Claim 20 is new.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 1/22/26 has been entered.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 2, 5, 7, 11, and 17-20 are rejected under 35 U.S.C. 103 as being unpatentable over Vlasie et al. (WO 2017/009100).
Regarding Claims 1, 17-19: Vlasie discloses a method of using peptidyl arginine deiminase (PAD) to improve a physical property of the protein or to improve the solubility of the protein [abstract]. Vlasie discloses improving the properties of plant proteins and specifically discloses rapeseed as a suitable plant protein in addition to soy, wheat, and pea proteins [pg. 3, lines 1-7]. Vlasie discloses the activity of the PAD as one unit of PAD expressed as 1µmol of citrulline formed/min/mg of protein [pg. 7, lines 14-22]. Vlasie discloses dosing the PAD at .1% v/w on dry matter [pg. 8, Ex. 1]. Vlasie discloses that the plant protein is a solution and that the solution can be a beverage and that the beverage can be a type of milk derived from a plant protein source [pg. 12, claims 9-11]. Vlasie discloses incubating protein with PAD at a pH of between 6.2 and 6.8 and at a temperature between 35 and 45°C [pg. 3, lines 1-15]. Vlasie discloses inactivating PAD by heat shock at 85°C for 15 min [pg. 11, Ex. 4].
The fact that applicant has recognized another advantage (“decreasing the sweetness, licorice flavor, astringency, and/or length of aftertaste”) which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985).
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Further although Vlasie does not disclose 2 units PAD per liter of solution to 60 units PAD per liter of solution, is added in an amount of 2 units PAD per liter of solution; added in an amount of 20 units PAD per liter of solution; added in an amount of 60 units PAD per liter of solution, Vlasie does disclose that the activity is the same as claimed and discloses adding the enzyme at .1%.
It would have been obvious to one having ordinary skill in the art at the time of the invention to adjust the amount of PAD for the intended application, since it has been held that discovering an optimum value of a result effective variable involves only routine skill in the art. In re Boesch, 617 F.2d 272.
Although Vlasie does not disclose wherein the incubating reduces trypsin inhibitory activity (TIA) of the rapeseed protein solution by at least 40% as measured by a-N-benzoyl-L- arginine-ethyl ester (BAEE) or AzoCasein assay, and, relative to an otherwise identical rapeseed protein solution not incubated with PAD, decreases at least one of sweetness, liquorice flavor, astringency, or length of aftertaste by at least 10 points on a 0-100 unstructured quantitative descriptive analysis (QDA) scale, Vlasie discloses the same protein, enzyme, and incubation conditions, it would have been obvious to one of ordinary skill in the art that Vlasie would have had the same features and results as recited.
The Office is not equipped to manufacture prior art products and compare them for patentability. Applicant is reminded that where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
"When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
Regarding Claim 2: Vlasie discloses as discussed above in claim 1. Vlasie discloses that the treated protein may be used as a food ingredient [page 2, lines 31-35].
Regarding Claim 5: Vlasie discloses as discussed in claim 1 above. Vlasie discloses that the peptidyl arginine deiminase (PAD) is of microbial origin since the PAD used is secreted by Fusarium graminearum [pg. 3, lines 19-28].
Regarding Claims 7 and 11: Vlasie discloses as discussed above in claim 1. Vlasie discloses that the treated protein may be used as a food ingredient [page 2, lines 31-35].
Regarding Claim 20: Vlasie discloses as discussed above in claim 1. Vlasie discloses in an example, treating protein with PAD at a pH of 6.5, at 45°C for 16 hours [pg. 8, Ex. 1].
Although Vlasie does not disclose treating for 2 to 3 hours, it would have been obvious to one having ordinary skill in the art at the time of the invention to adjust the incubation time for the intended application, since it has been held that discovering an optimum value of a result effective variable involves only routine skill in the art. In re Boesch, 617 F.2d 272.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Vlasie et al. (WO 2017/009100) as applied to claim 1 above and in further view of JP 2012513772 Machine Translation June 2012.
Regarding Claim 4: Vlasie discloses as discussed above in claim 1.
Vlasie does not disclose further dissolving flour to obtain a protein solution.
JP 772 discloses taking plant proteins and namely canola (rapeseed), soy, wheat, and pea flours, adding water to the flours to make a slurry solution and then treating with an enzyme [abstract; pg. 3, I. Method a.)i.); pg. 5, 2nd , and 4th paragraphs; pg. 9, 3rd full paragraph]. JP’772 discloses the protein hydrolysate as suitable for infant formulas [pg. 11, 1st paragraph].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to further modify the method of Vlasie to include the rapeseed in a flour form and dissolving in water as in JP’772 in order to distribute the protein and aid in the even distribution of the enzyme in the deamination of the protein.
Claims 6, 13, and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Vlasie et al. (WO 2017/009100) as applied to claim 1 above and in further view of Edens et al. (WO 2008/000714).
Regarding Claim 6: Vlasie discloses as discussed above in claim 1. Vlasie does not discloses that the deiminase has at least 80% sequence identity to Seq Id 1.
Edens discloses as discussed above in claim 1. Edens discloses arginine deiminase (SEQ ID NO: 6) which is 100% identical to SEQ ID NO: 1 as instantly claimed [page 3, line 28].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the method of Vlasie to include the PAD with SEQ ID 6 of Edens since both inventions seek to treat vegetable proteins to a PAD enzyme for the modification of the protein and for the inclusion of the modified protein in food and beverage products. Edens discloses the enzyme as effective across plant types. It would have been expected that the enzyme would have been effective in treating the rapeseed of Vlasie.
Regarding Claim 13: Vlasie discloses as discussed above in claim 7. Vlasie does not explicitly disclose wherein the drink is medicinal or a sport drink.
Edens further discloses that the composition is a dietary or nutraceutical or pharmaceutical beverage [pg. 10, lines 16-25].
At the effective filing date of the invention it would have been obvious to one of ordinary skill to modify the method of Vlasie to include medicinal or sports drinks as in Edens in or to offer the modified protein in a greater array of beverage products.
Regarding Claim 20: Vlasie discloses as discussed above in claim 1. Vlasie discloses in an example, treating protein with PAD at a pH of 6.5, at 45°C for 16 hours [pg. 8, Ex. 1].
Edens further discloses using PAD at a pH of 6.5 at 45°C for 3 hours to test the effectivity of the enzyme [pg. 51, lines 31-34].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the method of Vlasie to incubate the enzyme for 3 hours as in Edens since Edens discloses the effective conversion of arginine to citrulline in that time frame [pg. 52, Table 1].
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Vlasie et al. (WO 2017/009100) as applied to claim 7 above and in view of Canella et al. (HU 185829 Machine Translation).
Regarding Claim 8: Vlasie as modified discloses as discussed above in claim 7.
Vlasie does not disclose the production of a plant protein milk or a fermented plant protein product.
Canella discloses the production of a fermented rapeseed protein [pg. 2, 1st full paragraph].
At the effective filing date of the invention it would have been obvious to those of ordinary skill in the art to utilize the rapeseed protein of modified Edens to include fermented rapeseed protein as in Canella in order to produce fermented rapeseed beverages.
Claim 20 is rejected under 35 U.S.C. 103 as being unpatentable over Vlasie et al. (WO 2017/009100) as applied to claim 1 above and in view of .
Regarding Claim 20: Vlasie as modified discloses as discussed above in claim 1.
Vlasie does not disclose the production of a plant protein milk or a fermented plant protein product.
Canella discloses the production of a fermented rapeseed protein [pg. 2, 1st full paragraph].
At the effective filing date of the invention it would have been obvious to those of ordinary skill in the art to utilize the rapeseed protein of modified Edens to include fermented rapeseed protein as in Canella in order to produce fermented rapeseed beverages.
Claims 1, 2, 5-7, 11-13, and 17-20 are rejected under 35 U.S.C. 103 as being unpatentable over Edens et al. (WO 2008/000714) in view of Vlasie et al. (WO 2017/009100).
Regarding Claims 1, 17-19: Edens discloses a process for citrullination of proteins and peptides using a peptidyl arginine deiminase. The modified proteins are used in foodstuff. The process converts at least 80% of arginine in the protein substrate to a citrulline residue [Abstract]. Edens states that proteins or peptides incorporating large amounts of citrulline can be used in infant nutrition or nutritional supplements for special consumer groups. Additionally these proteins and peptides offer an organoleptic benefit because proteins and peptides comprising citrulline residues do not exhibit bitter taste [page 11, lines 26-31]. Edens also discloses that the composition does not exhibit impaired taste which is often an effect of extensive hydrolyzation [pg. 12, lines 19-21]. Edens discloses the type of food proteins that may be treated with PAD comprise animal and plant proteins, e.g. casein or egg protein, soy protein, pea protein, wheat gluten, etc. [page 8, lines 6-15]. Edens discloses that the enzymes of the invention is used at a pH of 6.5 and at 45°C [pg. 51, lines 31-34].
Edens does not disclose “decreasing the sweetness, licorice flavor, astringency, and/or length of aftertaste”. However, claim 1 is a recitation of the intended use of the claimed invention and in order to patentably distinguish the claimed invention from the prior art, the recitation must result in a structural difference between the claimed invention and the prior art. MPEP 2103 states that intended use language "does not limit a claim to a particular structure does not limit the scope of a claim". The above mentioned phrase does not limit the claim to any particular structure, so it is not interpreted to limit the scope of the claims. If the prior art structure is capable of performing the intended use, then it meets the claim.
Edens does not disclose that the protein is rapeseed protein.
Edens does not disclose wherein the PAD is added in an amount of 2 units PAD per liter of solution to 60 units PAD per liter of solution, wherein one unit of PAD is expressed as 1 umol of citrulline formed/min/mg of rapeseed protein (claim 1); wherein in step a) the PAD is added in an amount of 2 units PAD per liter of solution (claim 17); wherein in step a) the PAD is added in an amount of 20 units PAD per liter of solution (claim 18); wherein in step a) the PAD is added in an amount of 60 units PAD per liter of solution (claim 19).
Vlasie discloses a method of using PAD to improve a physical property of the protein or to improve the solubility of the protein [abstract]. Vlasie discloses improving the properties of plant proteins and specifically discloses rapeseed as a suitable plant protein in addition to soy, wheat, and pea proteins [pg. 3, lines 1-7]. Vlasie discloses the activity of the PAD as one unit of PAD expressed as 1µmol of citrulline formed/min/mg of protein [pg. 7, lines 14-22]. Vlasie discloses dosing the PAD at .1% v/w on dry matter [pg. 8, Ex. 1]. Vlasie discloses that the plant protein is a solution and that the solution can be a beverage and that the beverage can be a type of milk derived from a plant protein source [pg. 12, claims 9-11]. Vlasie discloses incubating protein with PAD at a pH of between 6.2 and 6.8 and at a temperature between 35 and 45°C [pg. 3, lines 1-15]. Vlasie discloses inactivating PAD by heat shock at 85°C for 15 min [pg. 11, Ex. 4].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the method of Edens to include hydrolysis of rapeseed protein as disclosed in Vlasie since Vlasie also discloses rapeseed as a suitable plant protein source that can be treated with PAD, since Edens is directed towards the hydrolysis of plant protein, since rapeseed is a plant protein, and since the proteins applicable to both Edens and Vlasie are overlapping in their disclosures of at least soy, pea, and wheat proteins.
Further it would have been obvious to modify Edens to provide the PAD in amounts as in Vlasie that would provide the desired level of increased solubility of the protein and deamination/citrullination.
Further although Vlasie does not disclose 2 units PAD per liter of solution to 60 units PAD per liter of solution, is added in an amount of 2 units PAD per liter of solution; added in an amount of 20 units PAD per liter of solution; added in an amount of 60 units PAD per liter of solution, Vlasie does disclose that the activity is the same as claimed and discloses adding the enzyme at .1%.
It would have been obvious to one having ordinary skill in the art at the time of the invention to adjust the amount of PAD for the intended application, since it has been held that discovering an optimum value of a result effective variable involves only routine skill in the art. In re Boesch, 617 F.2d 272.
The fact that applicant has recognized another advantage (“decreasing the sweetness, licorice flavor, astringency, and/or length of aftertaste”) which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985).
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Although Vlasie does not disclose wherein the incubating reduces trypsin inhibitory activity (TIA) of the rapeseed protein solution by at least 40% as measured by a-N-benzoyl-L- arginine-ethyl ester (BAEE) or AzoCasein assay, and, relative to an otherwise identical rapeseed protein solution not incubated with PAD, decreases at least one of sweetness, liquorice flavor, astringency, or length of aftertaste by at least 10 points on a 0-100 unstructured quantitative descriptive analysis (QDA) scale, Edens as modified discloses treating the same protein, enzyme, and incubation conditions, it would have been obvious to one of ordinary skill in the art that Edens would have had the same features and results as recited.
The Office is not equipped to manufacture prior art products and compare them for patentability. Applicant is reminded that where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).
"When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
Regarding Claim 2: Edens discloses as discussed above in claim 1. Edens discloses that the treated protein may be used as food, feed, nutraceutical or medicament [page 3, lines 16-20].
Regarding Claim 5: Edens discloses as discussed in claim 1 above. Edens disclose that the peptidyl arginine deiminase (PAD) is of microbial origin since the PAD used is secreted by Fusarium graminearum [pg. 6, lines 20-25].
Regarding Claim 6: Edens discloses as discussed above in claim 1. Edens discloses arginine deiminase (SEQ ID NO: 6) which is 100% identical to SEQ ID NO: 1 as instantly claimed [page 3, line 28].
Regarding Claims 7 and 11: Edens discloses as discussed above in claim 1. Edens discloses the type of food proteins that may be treated with PAD including soy protein. Edens explicitly states that the treated protein may be used in all kinds of foods [pg. 10, lines 1-15]. Further Edens discloses utilizing soy protein and pea protein [pg. 8, lines 8-15]. Edens discloses the production of a drink/beverage [pg. 10, lines 1-5]. Vlasie discloses beverages as discussed above.
Regarding Claim 12: Edens disclose as discussed above in claim 7. Edens further discloses that the composition can be in soda form and discloses the inclusion of acids and stabilizers [Ex 9]. It is well known in the art that sodas tend to have an acidic pH. Further it would have been obvious to provide the beverage with a neutral pH since it is easier on the digestive tract. Vlasie discloses beverages as discussed above.
Regarding Claim 13: Edens discloses as discussed above in claim 7. Edens further discloses that the composition is a dietary or nutraceutical or pharmaceutical beverage [pg. 10, lines 16-25].
Regarding Claim 20: Edens discloses as discussed above in claim 1. Edens further discloses using PAD at a pH of 6.5 at 45°C for 3 hours to test the effectivity of the enzyme [pg. 51, lines 31-34].
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Edens et al. (WO 2008/000714) and Vlasie et al. (WO 2017/009100) as applied to claim 1 above and in further view of JP 2012513772 Machine Translation June 2012.
Regarding Claim 4: Edens discloses as discussed above in claim 1. Edens teaches the subjecting food proteins to an incubation with PAD, the antigenicity or allergenicity of the resulting citrullinated protein or protein hydrolysate is reduced [page 12, lines 15-19]. Edens discloses that application of the active PAD according to the invention is the incorporation in all kinds of doughs to increase the taste and aroma of baked goods. (page 15, lines 7-9).
Edens does not disclose further dissolving flour to obtain a protein solution.
JP 772 discloses taking plant proteins and namely canola (rapeseed), soy, wheat, and pea flours, adding water to the flours to make a slurry solution and then treating with an enzyme [abstract; pg. 3, I. Method a.)i.); pg. 5, 2nd , and 4th paragraphs; pg. 9, 3rd full paragraph]. JP’772 discloses the protein hydrolysate as suitable for infant formulas [pg. 11, 1st paragraph].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to further modify the method of Edens to include the rapeseed in a flour form and dissolving in water as in JP’772 in order to distribute the protein and aid in the even distribution of the enzyme in the deamination of the protein.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Edens et al. (WO 2008/000714) and Vlasie et al. (WO 2017/009100) as applied to claim 7 above and in view of Canella et al. (HU 185829 Machine Translation).
Regarding Claim 8: Edens as modified discloses as discussed above in claim 7. Edens discloses the type of food proteins that may be treated with PAD including soy protein. Edens explicitly states that the treated protein may be used in all kinds of foods [pg. 10, lines 1-15]. Further, Edens discloses utilizing soy protein and pea protein [pg. 8, lines 8-15]. Edens discloses the production of a drink/beverage [pg. 10, lines 1-5].
However, Edens does not disclose the production of a plant protein milk or a fermented plant protein product.
Canella discloses the production of a fermented rapeseed protein [pg. 2, 1st full paragraph].
At the effective filing date of the invention it would have been obvious to those of ordinary skill in the art to utilize the rapeseed protein of modified Edens to include fermented rapeseed protein as in Canella in order to produce fermented rapeseed beverages.
Response to Arguments
The Applicants assert that neither Edens or Vlasie suggest the amended parameters regarding the reduction TIA, and the quantification of the flavor reduction (QDA). The Applicants also assert that the inactivation steps by heating are absent.
The Examiner maintains that since Edens as modified and Vlasie as a primary and secondary reference disclose the same protein treated at the same temperature and at the same pH level that the results and features of Edens as modified and Vlasie would have been the same or substantially similar. The Examiner also notes that Vlasie disclosed a heat inactivation step for 15 minutes at 85C. The Examiner maintains that the inactivating enzymes at high temperatures is known and common in the art and to do so at a desired time and temperature to achieve a desired level of reduction or complete inactivation would have been known to one of ordinary skill.
Regarding Claim 4, the Applicants assert that JP’772 does not teach the recited QDA outcome and that it does not cure the deficiencies of Edens and Vlasie.
The Examiner maintains that the references were not deficient for the reasons discussed above. The Examiner maintains that JP’772 was incorporated for the protein flour limitation.
Regarding Claim 8, the Applicants assert that Canella does not teach the recited QDA outcome and that it does not cure the deficiencies of Edens and Vlasie.
The Examiner maintains that the references were not deficient for the reasons discussed above. The Examiner maintains that Canella was incorporated for the fermented rapeseed protein limitation.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to FELICIA C TURNER whose telephone number is (571)270-3733. The examiner can normally be reached Mon-Thu 8:00-4:00 pm.
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/Felicia C Turner/Primary Examiner, Art Unit 1793
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