Prosecution Insights
Last updated: October 25, 2026
Application No. 17/792,169

METHOD FOR PRODUCING A HIGH-PRESSURE TREATED PLANT SEED BASE PRODUCT, AND PLANT SEED BASE PRODUCT

Non-Final OA §103
Filed
Jul 12, 2022
Priority
Jan 14, 2020 — EU PCT/EP2020/050767 +1 more
Examiner
LACHICA, ERICSON M
Art Unit
1792
Tech Center
1700 — Chemical & Materials Engineering
Assignee
Döhler GmbH
OA Round
5 (Non-Final)
30%
Grant Probability
At Risk
5-6
OA Rounds
0m
Est. Remaining
65%
With Interview

Examiner Intelligence

Grants only 30% of cases
30%
Career Allowance Rate
158 granted / 531 resolved
-35.2% vs TC avg
Strong +35% interview lift
Without
With
+35.2%
Interview Lift
resolved cases with interview
Typical timeline
3y 3m
Avg Prosecution
76 currently pending
Career history
613
Total Applications
across all art units

Statute-Specific Performance

§101
0.9%
-39.1% vs TC avg
§103
50.5%
+10.5% vs TC avg
§102
5.6%
-34.4% vs TC avg
§112
37.5%
-2.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 531 resolved cases

Office Action

§103
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 . 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 August 6, 2026 has been entered. Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102 of this title, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. Claims 17, 28-29, and 34-37 are rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864. Regarding Claim 17, Vessio et al. discloses a method for producing a plant seed base product (base ingredient derived from cereals and/or legume seeds) (‘922, Paragraphs [0019]-[0021]). The method comprises soaking a plant seed feedstock in water (‘922, Paragraphs [0024] and [0028]) mixed with at least one enzyme (‘922, Paragraphs [0042]-[0043]). The plant seed feedstock comprises plant seeds (‘922, Paragraph [0019]) to produce a soaked plant seed feedstock (‘922, Paragraphs [0027]-[0028]). The soaked plant seed feedstock is liquefied (hydrolyzed) under the action of the at least one enzyme to produce a liquefied plant seed feedstock (‘922, Paragraph [0042]). The soaked plant seed feedstock comprises dietary fibers (‘922, Paragraphs [0028] and [0038]). The liquefied plant seed feedstock is subjected to high pressure treatment at a pressure of between 50 and 1500 bar for purposes of reducing the particle size of the seeds in a micronization step (‘169, Paragraph [0028]), which overlaps the claimed pressure ranges of between 800 bar and 3000 bar. Where the claimed pressure ranges for purposes of reducing particle size overlaps pressure ranges for purposes of reducing particle sizes disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Vessio et al. also discloses the plant seed base product (‘922, Paragraph [0001]) using whole grain seeds that keep the bran and the germ (‘922, Paragraphs [0014] and [0027]-[0028]), which whole grain seeds reads on the limitations regarding not removing any components of the plant seeds used so that the resulting plant seed base product consists of water (‘922, Paragraphs [0027]-[0028]) and essentially all components of the plant seeds or their degradation products (‘922, Paragraphs [0014] and [0042]). Vessio et al. discloses a micronization step in which seeds are placed in water occurring at a pressure of between 50 and 1500 bar (‘922, Paragraph [0028]). However, Vessio et al. does not characterize the micronization step to be a homogenization step. Vessio et al. is also silent regarding the at least one enzyme comprising β-glucanase and/or cellulase having a hydrolytic activity towards dietary fiber components of the soaked plant seed feedstock for a time sufficient to reduce total dietary fiber content of the soaked plant seed feedstock to produce the liquefied plant seed feedstock. Herrmann-Buerk et al. discloses a method for producing a plant seed base product (recipe component) (‘529, Paragraph [0017]). The method comprises soaking a feedstock (almond flour) in water (‘529, Paragraph [0046]) wherein the feedstock is derived from nut seeds to produce a soaked feedstock (‘529, Paragraph [0013]) wherein the feedstock comprises dietary fibers (‘529, Paragraph [0009]). Herrmann- Buerk et al. further discloses subjecting the liquefied feedstock to high pressure homogenization at a pressure of between 100 bar and 3000 bar (‘529, Paragraph [0025]), which overlaps the claimed high pressure homogenization pressure range of 800 bar and 3000 bar. Vessio et al. discloses a vegan food or beverage product (‘922, Paragraph [0056]) comprising a base ingredient being derived from nuts of peanuts (‘922, Paragraphs [0019]-[0020]). Herrmann-Buerk et al. also discloses a vegan food or beverage product (‘529, Paragraph [0006]). Both Vessio et al. and Herrmann-Buerk et al. are directed towards the same field of endeavor of vegan/milk substitute food and beverage products comprising a liquefied feedstock derived from nuts subjected to a high pressure that overlaps the claimed high pressure . It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of Vessio et al. and utilize a high pressure processing parameter with the claimed pressure ranges in the context of a high pressure homogenization pressure conditions since Hermann-Buerk et al. teaches that the high pressure homogenization pressure ranges were known and conventional pressure ranges for reducing the particle sizes of food particles while homogenizing said food particles. Furthermore, where the claimed pressure ranges for purposes of reducing particle size overlaps pressure ranges for purposes of reducing particle sizes disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Further regarding Claim 17, Vessio et al. discloses the liquefied plant seed feedstock mixture of wholegrain seeds being treated through an enzyme process using amylase treatments that hydrolyze the starches (‘922, Paragraphs [0042] and [0044]) wherein the wholegrain seeds keep the bran and are rich in fiber (‘922, Paragraphs [0014] and [0028]). The seeds are derived from wholegrain rice seeds (‘922, Paragraphs [0017]-[0018]). However, Vessio et al. modified with Hermann-Buerk et al. is silent regarding the at least one enzyme comprising β-glucanase and/or cellulase having a hydrolytic activity towards dietary fiber components of the soaked plant seed feedstock for a time sufficient to reduce total dietary fiber content of the soaked plant seed feedstock to produce the liquefied plant seed feedstock. Gay discloses a partially or totally deoiled soya bean and/or other plant material like legume beans, and cereals which has or has not been thermally treated (‘015, Column 3, lines 59-68) wherein a considerable fraction of the carbohydrates of soya and/or other plant material containing both proteins and carbohydrates are metabolized using alimentary yeasts whose action of hydrolyzing and modifying such carbohydrates in such a manner that those hydrolyzed and modified carbohydrates are then metabolized by yeasts by cellulases and amylases and beta glucanases in order to obtain a product low in carbohydrates and whose proportion of protein is greater than that of the original soya and/or other plant material (‘015, Column 3, lines 20-35). Carder et al. provides evidence that it was known in the art that a method of controlling a hydrolysis reaction by activating and deactivating an enzyme that catalyzes a hydrolysis reaction to start and stop the hydrolysis reaction (‘864, Paragraph [0002]) involves a fibrolytic enzyme or endo glucanase such as endo cellulase hydrolyzes insoluble fiber like cellulose and soluble fiber like beta glucan and endo-beta-glucanase hydrolyzes soluble fiber (‘864, Paragraph [0034]), which indicates that glucanase and cellulase enzymes are known in the art to have a hydrolytic activity towards dietary fiber components. Both modified Vessio et al. and Gay are directed towards the same field of endeavor of methods of processing food grains enzymatically using an enzyme and applying the process to rice cereals (‘922, Paragraph [0011]) (‘015, Column 2, lines 63-64). Both food processing methods of modified Vessio et al. and Gay use an enzymatic treatment involving amylase (‘922, Paragraph [0042]) (‘015, Column 3, lines 20-35). It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and liquefy the soaked plant seed feedstock using at least one enzyme comprising β-glucanase and/or cellulase (which are enzymes that necessarily have a hydrolytic activity towards dietary fiber components as evidenced by Carder et al.) as taught by Gay since the selection of a known material based on its suitability for its intended use supports a prima facie obviousness determination in view of Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945) (MPEP § 2144.07). Gay teaches that it was known in the food and beverage art to utilize one or more enzymes including beta glucanases and celluloses to hydrolyze and modify carbohydrates by action of metabolizing by yeast containing these enzymes of beta glucanases and cellulases (‘015, Column 3, lines 20-35). Regarding Claim 28, Hermann-Buerk et al. discloses keeping a temperature of the resulting plant seed base product in the range of from between 72°C and 138°C after high pressure homogenization (‘529, Paragraph [0027]), which overlaps the claimed temperature maintenance after high pressure homogenization of the liquefied plant seed feedstock of from 65°C to 95°C, in order to form large rough almond protein agglomerates (‘529, Paragraph [0027]). The temperature is maintained at this level for a heat holding time of between 30 seconds and 25 minutes (‘529, Paragraph [0027]), which falls within the claimed high pressure homogenization time of up to 50 minutes. Where the claimed maintenance temperature after homogenization and holding times overlaps maintenance temperature after homogenization and holding times disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Furthermore, differences in the maintenance temperature after homogenization and holding time will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such maintenance temperature and holding time is critical. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation in view of In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP § 2144.05.II.A.). One of ordinary skill in the art would adjust the maintenance temperature after homogenization in order to form large rough protein agglomerates. Regarding Claim 29, Hermann-Buerk et al. discloses the pressure during the high pressure homogenization being between 100 bar and 3000 bar (‘529, Paragraph [0025]), which overlaps the claimed high pressure homogenization pressure range of 2000 bar and 3000 bar. Vessio et al. discloses a vegan food or beverage product (‘922, Paragraph [0056]) comprising a base ingredient being derived from nuts of peanuts (‘922, Paragraphs [0019]-[0020]). Herrmann-Buerk et al. also discloses a vegan food or beverage product (‘529, Paragraph [0006]). Both Vessio et al. and Herrmann-Buerk et al. are directed towards the same field of endeavor of vegan/milk substitute food and beverage products comprising a liquefied feedstock derived from nuts subjected to a high pressure that overlaps the claimed high pressure. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of Vessio et al. and utilize a high pressure processing parameter with the claimed pressure ranges in the context of a high pressure homogenization pressure conditions since Hermann-Buerk et al. teaches that the high pressure homogenization pressure ranges were known and conventional pressure ranges for reducing the particle sizes of food particles while homogenizing said food particles. Furthermore, where the claimed pressure ranges for purposes of reducing particle size overlaps pressure ranges for purposes of reducing particle sizes disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Regarding Claim 34, Vessio et al. discloses the particles being micronized to a size of less than about 27 microns (‘922, Paragraph [0028]), which falls within the claimed particles included in the resulting plant seed base product being occupied by particle which are smaller than 130 micrometers. Hermman-Buerk et al. also discloses the particles having a particle size distribution of between 10 microns and 44 microns (‘529, Paragraph [0025]), which indicates that a majority of the volume of particles in the resulting plant seed base product occupied by particles are smaller than 130 micrometers. It would have been obvious to one of ordinary skill in the art at the time of the invention to use high pressure processing parameters that reduces the particle sizes of the food particles to the claimed particle sizes since Vessio et al. and Hermann-Buerk et al. both teach that using high pressure processing were known and conventional pressure ranges for reducing the particle sizes of food particles to the claimed particle sizes. Furthermore, where the claimed particle size range overlaps particle size ranges disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Regarding Claim 35, Herrmann-Buerk et al. discloses the viscosity of the liquid mixture is significantly reduced by means of the facultative cold high pressure homogenization step with a corresponding reduction of viscosity to further process the liquid mixture to pump it through devices used even if the proportion by weight of protein is higher (‘529, Paragraph [0022]). Applicant discloses high pressure homogenization can be performed more easily since the liquefaction enables to lower the viscosity (Specification, Page 4, lines 12-15). Applicant also discloses hydrolytic breakdown of dietary fibers wherein breaking down dietary fibers reduces the viscosity of the mixture of seed feedstock and water (Specification, Page 14, lines 7-17). Therefore, the method of the combination of Vessio et al. modified with Hermann-Buerk et al. and Gay as further evidenced by Carder et al. necessarily reads on the step of liquefying the soaked plant seed feedstock under the action of the at least one enzyme lowering the viscosity of the soaked plant seed feedstock in view of applicant’s disclosure. Regarding Claims 36-37, Vessio et al. modified with Hermann-Buerk et al. and Gay as further evidenced by Carder et al. is silent regarding the at least one enzyme being present at a concentration of about 0.5 kg/MT or about 1.0 kg/MT of plant feedstock. However, Gay discloses the at least one enzyme of beta glucanases and cellulases being part of a yeast that hydrolyzes and modifies carbohydrates to adjust the carbohydrate and protein content of the original plant material (‘015, Column 3, lines 20-35). The claims recite a step of soaking a plant seed feedstock in water mixed with at least one enzyme without specifying any particular volumes of water used in the soaking step. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and adjust the concentration of at least one enzyme comprising at least beta glucanases and/or cellulases present in a plant seed feedstock in an unspecified volume of water since differences in the concentration of the at least one enzyme in an unspecified volume of water will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such degree of concentration of the at least one enzyme in an unspecified volume of water is critical. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation in view of In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP § 2144.05.II.A.). One of ordinary skill in the art would adjust the concentration of the at least one enzyme containing at least beta glucanases and/or cellulases that is generically recited in an amount effective to adjust the carbohydrate and protein content of the original plant material to the desired carbohydrate and protein levels (‘015, Column 3, lines 20-35). Claim 19 is rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), Gay US 3,958,015, and Carder et al. US 2019/0233864 as applied to claim 17 as further evidenced by Janiak “Of starch and spit” (published 2019) (herein referred to as “Janiak”) and Triantafyllou US 2019/0110501. Regarding Claim 19, Vessio et al. discloses the at least one enzyme further comprising amylase and liquefying the soaked plant seed feedstock (‘922, Paragraphs [0038] and [0042]) and the enzyme treatments hydrolyzing the starches in the sugars (‘922, Paragraph [0044]). Janiak provides evidence that it was known in the art that alpha amylase is the enzyme that breaks down starchy food (Janiak, Page 1). Triantafyllou also provides evidence that alpha and beta amylase are types of starch degrading enzymes (‘501, Paragraph [0051]), i.e. alpha and beta amylases break down starches. Furthermore, products of identical chemical composition (plant seed feedstocks comprising at least one enzyme comprising amylase) can not have mutually exclusive properties in view of In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (MPEP § 2112.01.II.). Therefore, the amylase of the food and beverage composition of modified Vessio et al. would be expected to behave in the same manner as claimed, i.e. break down starch with the amylase. Claims 21-24 are rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 as applied to claim 17 above in further view of Nelson et al. US 4,041,187. Regarding Claim 21, Vessio et al. discloses processing soybeans (‘922, Paragraph [0020]). However, Vessio et al. modified with Herrmann-Buerk et al. and Gay as further evidenced by Carder et al. is silent regarding deactivating the at least one enzyme before the high pressure homogenization of the liquefied plant seed feedstock. Nelson et al. discloses a method for producing a plant seed base product (soybean dispersion beverage base) (‘187, Column 12, lines 64-68). The method comprises soaking a plant seed feedstock (soybean) in water mixed with at least one enzyme wherein the plant seed feedstock comprises plant seeds (soybean) to produce a soaked plant seed feedstock (ground slurry of soybeans), liquefying the soaked plant seed feedstock under the action of the at least one enzyme to produce a liquefied plant seed feedstock (‘187, Column 10, lines 7-35), and subjecting the liquefied plant seed feedstock to high pressure homogenization (‘187, Column 11, lines 1-20). Nelson et al. further discloses deactivating the at least one enzyme before the high pressure homogenization of the liquefied plant seed feedstock (‘187, Column 4, lines 6-26). Both modified Vessio et al. and Nelson et al. are directed towards the same field of endeavor of methods of processing soybean. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and deactivate the at least one enzyme before the high pressure homogenization of the liquefied plant seed feedstock as taught by Nelson et al. in order to prevent off flavor and off odor of the final product (‘187, Column 5, lines 29-39) (‘187, Column 7, lines 23-44). Regarding Claim 22, Nelson et al. discloses the deactivating the at least one enzyme being achieved by heating the liquefied plant seed feedstock (‘187, Column 7, lines 23-44). Regarding Claims 23-24, Nelson et al. discloses the deactivating being performed at about a boiling temperature for a duration of about 20 to 40 minutes (‘187, Column 7, lines 23-44), which falls within the claimed enzyme deactivation duration of up to one hour. The disclosure of the deactivating temperature occurring at about a boiling temperature of water reads on the claimed the deactivating being performed at temperatures of up to one hour. Where the claimed enzyme deactivation time and temperature ranges overlaps enzyme deactivation time and temperature ranges disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Claim 22 is rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 in further view of Nelson et al. US 4,041,187 as applied to claim 21 above in further view of Carder et al. US 2019/0233864. Regarding Claim 22, Nelson et al. discloses the deactivating of the at least one enzyme being achieved by heating (‘187, Column 7, lines 54-61). However, Vessio et al. modified with Herrmann-Buerk et al., Gay, and Nelson et al. is silent regarding the deactivating being achieved also by altering a pH value. Carder et al. discloses a food composition comprising a hydrolyzed composition (‘864, Paragraph [0041]) comprising a fiber hydrolysis catalyzing enzyme or a starch hydrolysis catalyzing enzyme (alpha-amylase) (‘864, Paragraph [0097]) comprising deactivating a second enzyme of alpha-amylase (‘864, Paragraph [0095]) by heating (‘864, Paragraph [0122]) or by altering a pH value (by adding an acid) (‘864, Paragraph [0123]). Hammond discloses a method for enzymatically stabilizing rice bran and products produced from a stabilized and unstabilized rice bran (‘537, Column 1, lines 5-8) wherein the starch in the liquid phase can be converted into dextrins and dextroses by application of acid, heat, and/or amylases (‘537, Column 2, lines 6-14). Both modified Vessio et al. and Carder et al. directed towards the same field of endeavor of methods of deactivating at least one enzyme of a food composition containing enzyme. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and deactivate the at least one enzyme by altering a pH value as taught by Carder et al. or by enzymatic hydrolysis resulting in converting starches into dextrins by application of acid, heat, and/or amylases as taught by Hammond since the simple substitution of one known element (using only heating to inactivate enzymes) for another (using both heating and altering pH values to inactivate enzymes) to yield predictable results (to inactivate enzymes) is prima facie obvious (MPEP § 2143.I). Hammond discloses one method known in the art includes enzymatic conversion of grains in the form of rice bran by application of acid, heat, and/or amylases (‘537, Column 2, lines 6-14). Claims 25-26 are rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 in further view of Nelson et al. US 4,041,187 as applied to claim 22 above in further view of Triantafyllou US 2002/0081367 or alternatively Claims 25-26 are rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 in further view of Nelson et al. US 4,041,187 and Carder et al. US 2019/0233864 as applied to claim 22 above in further view of Triantafyllou US 2002/0081367. Regarding Claim 25, Vessio et al. modified with Herrmann-Buerk et al., Gay, and Nelson et al. or alternatively Vessio et al. modified with Herrmann-Buerk et al., Gay, Nelson et al., and Carder et al. is silent regarding adjusting the pH value in the range from 3 to 5 prior to heating. Triantafyllou discloses a method for producing a plant seed base product comprising the steps of mixing water with at least one enzyme and soaking a plant seed feedstock in the water (‘367, Paragraphs [0058] and [0082]). The plant seed feedstock comprises plant seeds (oat grain cereals) (‘367, Paragraph [0054]). The soaked plant seed feedstock is liquefied under the action of the at least one enzyme to produce a liquefied plant seed feedstock (‘367, Paragraphs [0058]-[0060]). The liquefied plant seed feedstock mixture (cereal meal suspension) is treated with beta-amylase in a first enzyme treatment step that generates maltose units and then the resulting suspension is treated with alpha-amylase in a second enzyme treatment step to generate maltose units (‘367, Paragraph [0085]) and using enzymatic hydrolysis of constituents in a cereal substrate suspension (‘367, Paragraph [0049]), which reads on the claimed at least one enzymes (amylase) having a hydrolytic activity towards dietary fibers. The liquefied plant feedstock is high pressure homogenized (‘367, Paragraph [0096]). Triantafyllou also discloses the pH value being adjusted to 4.7 (‘367, Paragraph [0070]), which falls within the claimed pH range of from 3 to 5. Vessio et al. discloses processing oats (‘922, Paragraph [0011]). Both modified Vessio et al. and Triantafyllou are directed towards the same field of endeavor of methods of processing oats using high pressure conditions. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and adjust the pH value to the claimed pH range of 3 to 5 as taught by Triantafyllou since where the claimed pH ranges overlaps pH ranges disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Furthermore, where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation in view of In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP § 2144.05.II.A.). Enzymes extracted from different sources may catalyze the same reaction at different pH conditions (‘367, Paragraph [0070]). The claims do not specify any particular enzyme for the deactivating step. Regarding Claim 26, Triantafyllou discloses the pH value being adjusted to 7.5 (‘367, Paragraph [0070]), which falls within the claimed pH range of from 6 to 8. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and adjust the pH value since where the claimed pH ranges overlaps pH ranges disclosed by the prior art, a prima facie case of obviousness exists in view of In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (MPEP § 2144.05.I.). Furthermore, where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation in view of In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP § 2144.05.II.A.). Enzymes extracted from different sources may catalyze the same reaction at different pH conditions (‘367, Paragraph [0070]). The claims do not specify any particular enzyme for the deactivating step. Further regarding Claim 26, Vessio et al. modified with Herrmann-Buerk et al., Gay, Nelson, and Triantafyllou or alternatively Vessio et al. modified with Herrmann-Buerk et al., Gay, Nelson et al., Carder et al., and Triantafyllou is silent regarding the pH adjustment step being conducted following the heating step. However, claims directed towards a process that reverses the order of the prior art process steps is prima facie obvious in view of Ex parte Rubin, 128 USPQ 440 (Bd. App. 1959) (MPEP § 2144.04.IV.C.). Claim 27 is rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 as applied to claim 17 above in further view of Kim et al. US 2019/0289870. Regarding Claim 27, Vessio et al. modified with Herrmann-Buerk et al. and Gay as further evidenced by Carder et al. is silent regarding a separate step of comminuting the plant seed feedstock and/or comminuting the liquefied plant seed feedstock before the step of high pressure homogenization of the liquefied plant seed feedstock. Kim et al. discloses a method for producing a plant seed base product comprising soaking a plant seed feedstock in water mixed with at least one enzyme to produce a soaked plant seed feedstock and liquefying the soaked plant seed feedstock under the action of the at least one enzyme to produce a liquefied plant seed feedstock, comminuting the plant seed feedstock before high pressure homogenization of the liquefied plant seed feedstock (‘870, Paragraph [0048]). Both modified Vessio et al. and Kim et al. are directed towards the same field of endeavor of methods of making milk/dairy substitutes using enzymes. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and incorporate a step of comminuting the plant seed feedstock before the high pressure homogenization step since Kim et al. teaches that it was known and conventional in the food art to process a milk/dairy substitute for milk using a comminuting step before the high pressure homogenization step. Claim 38 is rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 as applied to claim 17 above as further evidenced by Hammond US 5,292,537 (cited on Information Disclosure Statement filed July 12, 2022) and Enzymedica “Enzymes for Fat Digestion” <https://enzymedica.com/blogs/digest-this/enzymes-for-fat-digestion> (published November 29, 2017) (herein referred to as “Enzymes for Fat Digestion”). Regarding Claim 38, Vessio et al. discloses an enzyme treatment wherein the type of enzyme is not limited and can be variously used to obtain the desired food product (‘922, Paragraphs [0041]-[0043]). Vessio et al. also discloses the seeds being derived from whole grain seeds that keep the bran and the germ that are richer in fiber, fatty acids, and other precious substances for the body (‘922, Paragraph [0014]) wherein the whole grain seeds are rice (‘922, Paragraph [0011]). Hammond et al. provides evidence that it was known in the food and beverage art that rice bran has naturally occurring lipases which hydrolyze oil into glycerol and free fatty acids (‘537, Column 1, lines 20-43). Therefore, the whole grain rice cereal seeds that keep the bran and the germ disclosed by Vessio et al. necessarily comprises a lipase enzyme in the bran that breaks down fats with the lipase as evidenced by Hammond. Furthermore, products of identical chemical composition (plant seed feedstocks comprising at least one enzyme comprising lipase) can not have mutually exclusive properties in view of In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (MPEP § 2112.01.II.). Therefore, the lipase of the food and beverage composition of modified Vessio et al. would be expected to behave in the same manner as claimed, i.e. break down fats with the lipase. Additionally, Enzymes for Fat Digestion provides evidence that it was known in the art that lipase is the major enzyme that breaks down dietary fats into smaller molecules called fatty acids and glycerol wherein lipase hydrolyzes lipids, the ester bonds in triglycerides (Enzymes for Fat Digestion, Page 2). Claim 39 is rejected under 35 U.S.C. 103 as being unpatentable over Vessio et al. US 2013/0156922 in view of Herrmann-Buerk et al. US 2020/0100529 (cited on Information Disclosure Statement filed July 12, 2022), and Gay US 3,958,015 as further evidenced by Carder et al. US 2019/0233864 as applied to claim 17 above in further view of Hammond US 5,292,537 (cited on Information Disclosure Statement filed July 12, 2022) as further evidenced by Enzymedica “What is Protease” <https://enzymedica.com/blogs/ingredient-science/what-is-protease> (published June 4, 2018) (herein referred to as “What is Protease?”). Regarding Claim 39, Vessio et al. discloses an enzyme treatment wherein the type of enzyme is not limited and can be variously used to obtain the desired food product (‘922, Paragraphs [0041]-[0043]). Vessio et al. also discloses the seeds being derived from whole grain seeds that keep the bran and the germ that are richer in fiber, fatty acids, and other precious substances for the body (‘922, Paragraph [0014]) wherein the whole grain seeds are rice (‘922, Paragraph [0011]). However, Vessio et al. in view of Hermann-Buerk et al. and Gay as further evidenced by Carder et al. is silent regarding the at least one enzyme further comprising a protease. Hammond discloses a method for enzymatically stabilizing rice bran and products produced from a stabilized and unstabilized rice bran (‘537, Column 1, lines 5-8) wherein proteases are used to inactivate the naturally occurring lipase in the rice bran (‘537, Column 2, lines 60-68). Both modified Vessio et al. and Hammond are directed towards the same field of endeavor of methods of enzymatically treating rice bran products. It would have been obvious to one of ordinary skill in the art at the time of the invention to modify the process of modified Vessio et al. and use at least one enzyme further comprising a protease as taught by Hammond in order to inactive the naturally occurring lipase in the rice bran to the desired levels. Furthermore, the selection of a known material based on its suitability for its intended use supports a prima facie obviousness determination in view of Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945) (MPEP § 2144.07). Hammond teaches that it was known in the food and beverage art to utilize one or more enzymes including a protease enzyme to inactive naturally occurring lipase in the rice bran. Furthermore, products of identical chemical composition (plant seed feedstocks comprising at least one enzyme comprising protease) can not have mutually exclusive properties in view of In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (MPEP § 2112.01.II.). Therefore, the amylase of the food and beverage composition of modified Vessio et al. would be expected to behave in the same manner as claimed, i.e. break down proteins with the protease. Additionally, What is Protease? provides evidence that it was known in the art that proteases, also known as eptidases or proteinases, are enzymes that help break down proteins in foods into amino acids (Enzymedica, Page 1) and plays a role in blood clotting, cell division, recycling of proteins, and immune support (Enzymedica, Page 2). Response to Arguments Examiner notes that the previous Claim Objection has been withdrawn in view of the amendments. Applicant’s arguments with respect to the obviousness rejections of Claim 17 under 35 USC 103(a) have been considered but are moot because the new ground of rejection does not rely on the combination of references applied in the prior rejection of record for any teaching or matter specifically challenged in the argument. Conclusion The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. Enzymedica “What is Protease?” <https://enzymedica.com/blogs/ingredient-science/what-is-protease> (published June 4, 2018) discloses proteases, also known as eptidases or proteinases, are enzymes that help break down proteins in foods into amino acids (Enzymedica, Page 1) and plays a role in blood clotting, cell division, recycling of proteins, and immune support (Enzymedica, Page 2). Triantafyllou US 2019/0110501 discloses an aqueous liquid oat product of low viscosity having a high content of maltose obtained from oats by treatment with starch degrading enzymes such as alpha and/or beta amylase (‘501, Paragraph [0051]) wherein in prior art processes for preparing oat milk the starting material such as oat flour or oat bran is heated to a temperature and for a time sufficient to substantially prevent the development of endogenous enzymatic activity such as lipase and beta glucanase activity (‘501, Paragraph [0003]). Sherlock et al. US 2020/0367528 discloses a microcrop milk (‘528, Paragraph [0002]) made by hydrolyzing a lysed biomass by adding one or more non-proteolytic enzymes such as cellulase and amylase to the lysed biomass and incubating the mixture (‘528, Paragraph [0025]). Norwood et al. US 2020/0268022 an oat based beverage composition and rapid hydrolysis method of preparing the same (‘022, Paragraph [0002]) comprising an alpha amylase having side beta glucanase activity (‘022, Paragraph [0011]). Nakazawa et al. US 2006/0068061 discloses koji including many useful enzymes including amylase, protease, lipase, and cellulase (‘061, Paragraph [0032]) wherein starch in a medium of cereal grains is converted into sugar by amylase so that the koji derived sugar sweetens the soybean dairy food (‘061, Paragraph [0039]). Molin et al. US 5,190,755 discloses a health drink prepared from oat flour hydrolyzed with an alpha amylase and a beta glucanase and optionally supplemented with soy flour and then fermented by lactobacilli. Gandhi et al. US 2002/0127325 discloses a soy drink composition (‘325, Paragraph [0002]) comprising various degradative enzymes used as needed depending upon the particular soy material chosen wherein the enzymes includes amylase and cellulase (‘325, Paragraph [0025]). Drachenberg et al. US 3,941,890 discloses a method of making soy milk from soy beans (‘890, Column 1, lines 5-10) comprising the steps of adding amylase and cellulase enzymes to a slurry of soybean material which amylase and cellulase solubilizes, or renders suspensible, carbohydrate and cellulose constituents of the soy bean material (‘890, Column 4, lines 3-38). Larrere et al. US 2022/0322689 discloses a method of making a fermented plant based composition comprising fermenting a mixture comprising a vegetal base and heterofermenatative bifidobacteria and/or lactic acid bacteria to obtain a fermented plant based composition (‘689, Paragraph [0007]) wherein the vegetal base is an aqueous suspension comprising water and plant matter of legumes, seeds, and/or cereals (‘689, Paragraph [0057]) wherein the plant matter is a hydrolyzed cereal suspension such as an oat milk that is treated enzymatically by amylases to hydrolyze starch followed by removal of suspended matter (‘689, Paragraph [0065]). Dionisi et al. US 2022/0039417 discloses a vegan food composition that preserves natural goodness and avoids grittiness without discarding any nutrients such as dietary fibers (‘417, Paragraph [0010]) wherein the vegan food composition comprises legume and non legume seeds or non legume nuts (‘417, Paragraph [0011]) wherein the vegan food composition is a milk analogue (‘417, Paragraph [0017]) and is made by a method comprising the steps of enzymatically treating a mixture diluted with water by adding alpha amylase for 15 minutes at 80°C followed by a deactivation step (‘417, Paragraph [0091]) and carrying out a homogenization step at a pressure of 250 bar then at 50 bar (‘417, Paragraph [0094]) wherein most prior art vegan compositions use filtering to reduce filter size which has the disadvantage of removing dietary fiber and other beneficial components from the composition (‘417, Paragraph [0009]). Kizer et al. US 2019/0000112 discloses a method of making dairy like food products and/or other analogous food products derived substantially from or wholly from non-animal sources having color, flavor, nutritional content, and/or other qualities that are similar to those of dairy products and/or other food products (‘112, Paragraph [0002]) wherein the non-animal source is a plant source of oats, rye, buckwheat, wheat, barley, bamboo, millet, and corn (‘112, Paragraphs [0226]-[0229]) or milk derived from rice milk cereals (‘112, Paragraph [0151]) and made by emulsification at high amounts of mechanical energy using microfluidic homogenization between about 500 and about 2000 bar (’112, Paragraph [0123]). Kim et al. US 2019/0289870 discloses a vegetable milk substitute comprising quinoa and/or amaranth grains comprising the steps of forming a suspension by diffusing an oil ingredient of ground grain material of quinoa and/or amaranth with purified water and a wet nano pulverizing means for grinding the particles in the suspension into nano scale particles and a high pressure homogenizing means for mixing and homogenizing the final liquid to add an edible additive depending on the ingredient design of the vegetable milk alternative (‘870, Paragraph [0068]) wherein quinoa naturally has no gluten components and contains various minerals and vitamins including protein and dietary fiber (‘870, Paragraph [0023]) and amaranth is a gluten free grain having excellent effects on hypertension, diabetes, and hyperlipidemia (‘870, Paragraph [0024]) wherein a variety of grains other than soybeans, quinoa or amaranth can be used wherein the selection of the grain material whether the skin needs to be removed are determined depending on the ingredient design of the vegetable milk substitute to be manufactured (‘870, Paragraph [0051]) wherein the diffusion of materials comprises high pressure non diffusers, a high shear mixer, a microfluidizer, and/or a high pressure homogenizer (‘870, Paragraph [0052]) wherein soybeans are utilized with the skin or selectively used with the skin off (‘870, Paragraph [0075]) wherein the skin of black beans contains a black pigment of anthocyanin having an antioxidant action and a cholesterol lowering action along with medicinal anti cancer and anti ulcer effects (‘870, Paragraph [0018]) wherein the grain that is mixed includes rice, barley, oats, corn, millet, buckwheat (‘870, Paragraph [0076]). Pouvreau et al. US 2014/0161950 discloses a method of processing quinoa for use in food products (‘950, Paragraph [0002]) for making a milk analog (‘950, Paragraph [0028]) comprising the steps of soaking quinoa seeds and foregoing mechanical abrasion of the outer layers of the quinoa seed that potentially removes desired nutrients (‘950, Paragraphs [0018]-[0019]) and subjecting a blended mixture to ultra high temperature processing (UHT) then homogenizing the mixture to produce the resulting milk (‘950, Paragraph [0029]) wherein the embryo that surrounds the perisperm of the quinoa seed is high in protein and lipid and contains most of the fibers and saponins (‘950, Paragraph [0017]) wherein the processed seeds are subjected to a milling process such as wet milling after enzymatic treatment with α-amylases, pullulanases, and/or proteases wherein the enzyme enriched water benefits from the addition of calcium and sodium ions to improve the enzyme efficiency during the heat treatment (‘950, Paragraph [0021]) wherein the temperature of the mixture is raised to over 190°F to deactivate the enzyme activity and the grains are rinsed with hot water to maximize the extraction efficiency (‘950, Paragraph [0022]) wherein a quinoa seed slurry containing starch polysaccharide is broken down or hydrolyzed into the constituent sugars using one or more enzymes such as amylases to break down the carbohydrates to yield maltotriose and maltose from amylose or maltose wherein breaking down the starch to glucose further enhances the sweetness of the end product (‘950, Paragraph [0030]). Lindahl et al. US 5,686,123 discloses a cereal suspension used as an alternative to milk wherein the cereal suspension comprises rolled oats (‘123, Column 2, lines 16-40) generated by treatment with both an alpha amylase and a beta amylase to generate maltose units and having no glucanase and proteinase effect and homogenizing the enzyme treated suspension (‘123, Column 2, lines 1-15). Mitchell et al. US 4,744,992 discloses an enzymatic method for producing a milk like rice liquid for use either as a beverage or in a variety of food product was well as a product of the method (‘992, Column 1, lines 5-8) wherein ground whole grain rice is mixed with water to form a rice water slurry that is heated and then liquefied by treatment with an alpha amylase enzyme to form a liquid slurry which is treated with a glucosidase enzyme in a saccharification step to yield a rice milk product exhibiting a milk like texture (‘992, Column 3, lines 37-48) wherein the glucosidase enzyme is employed either alone or in combination with varying amounts of beta amylases enzymes in order to product a nutritional rice milk product having maltose in an amount of about 0 to 70% solids (‘992, Column 4, lines 8-18) wherein the beta amylase enzyme is employed in the saccharification step to yield a high maltose rice milk product which is nutritional and non allergenic while also having a rice like and milk like texture and functionality wherein substantially greater amounts of the beta amylase enzyme is sued if desired (‘992, Column 4, lines 46-64) wherein the rice material is cooked and liquefied with alpha amylase enzyme produce form a micro organism of Bacillus or a fungal source extracted from either barley, wheat, rye, sweet potatoes, or soybeans (‘992, Column 6, lines 4-27) wherein the rice milk is homogenized to yield a rice beverage having a fatty texture of mouthfeel similar to whole milk (‘992, Column 7, lines 35-54). The prior art made of record, cited on a previous 892 Notice of References Cited form, and not relied upon is considered pertinent to applicant's disclosure. Tsubaki et al. US 2003/0165604 discloses a fat and oil composition containing beta glucans extracted from a plant of the Graminaeae family (“604, Paragraph [0001]) wherein any enzyme expected to modify soybeans and grains to improve emulsifying capabilities is used to obtain an enzyme treated substance wherein the enzymes includes amylases, cellulases, proteases, and lipases (‘604, Paragraph [0065]). Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERICSON M LACHICA whose telephone number is (571)270-0278. The examiner can normally be reached M-F, 8:30am-5pm, EST. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Erik Kashnikow can be reached at 571-270-3475. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /ERICSON M LACHICA/Examiner, Art Unit 1792
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Prosecution Timeline

Show 8 earlier events
Apr 06, 2026
Response after Non-Final Action
Apr 15, 2026
Response Filed
Apr 28, 2026
Applicant Interview (Telephonic)
Apr 28, 2026
Examiner Interview Summary
May 06, 2026
Final Rejection mailed — §103
Aug 06, 2026
Request for Continued Examination
Aug 11, 2026
Response after Non-Final Action
Oct 05, 2026
Non-Final Rejection mailed — §103 (current)

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5-6
Expected OA Rounds
30%
Grant Probability
65%
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3y 3m (~0m remaining)
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