Prosecution Insights
Last updated: October 02, 2026
Application No. 18/259,613

LOW LIPID CONTENT OAT PROTEIN COMPOSITION WITHOUT TRACES OF ORGANIC SOLVENT OR SURFACTANT

Final Rejection §103§DP
Filed
Jun 28, 2023
Priority
Jan 04, 2021 — EU 21305001.6 +1 more
Examiner
IANNUZO, NATALIE NMN
Art Unit
1653
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Roquette Freres
OA Round
2 (Final)
12%
Grant Probability
At Risk
3-4
OA Rounds
1m
Est. Remaining
84%
With Interview

Examiner Intelligence

Grants only 12% of cases
12%
Career Allowance Rate
5 granted / 40 resolved
-47.5% vs TC avg
Strong +71% interview lift
Without
With
+71.4%
Interview Lift
resolved cases with interview
Typical timeline
3y 4m
Avg Prosecution
55 currently pending
Career history
99
Total Applications
across all art units

Statute-Specific Performance

§101
4.7%
-35.3% vs TC avg
§103
47.0%
+7.0% vs TC avg
§102
11.4%
-28.6% vs TC avg
§112
26.4%
-13.6% vs TC avg
Black line = Tech Center average estimate • Based on career data from 40 resolved cases

Office Action

§103 §DP
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 . Withdrawal of Rejections The response and amendments filed on 06/10/2026 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section. Briefly, the previous claim rejections under 35 U.S.C. 112(b) for indefiniteness have been withdrawn necessitated by Applicant’s amendments. The previous claim rejections under 35 U.S.C. 103 for obviousness have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection are set forth below. The previous double patenting rejections have been withdrawn; however, new grounds of rejection are set forth below. The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application. New Grounds of Rejection Necessitated by Amendments Claim Rejections – 35 USC § 103, Obviousness 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, 3-7, and 14-21 are rejected under 35 U.S.C. 103 as being unpatentable over Tupper (WO 01/21012; Date of Publication: March 29, 2001 – cited in the IDS filed on 06/28/2023 – previously cited) in view of Sjoo (US 2020/0368135; Date of Publication: November 26, 2020 – previously cited), Weissbrodt (US 2016/0353773; Date of Publication: December 8, 2016 – previously cited), and Bruckner-Guhmann (Foaming characteristic of oat protein and modification by partial hydrolysis; 2018 – cited in the IDS filed on 06/28/2023 – previously cited). Tupper’s general disclosure relates to “Methods of manufacturing a bran product derived from a grain, the method comprising the steps of: (a) providing a dehulled grain; (b) stabilising the dehulled grain; (c) pressing or rolling the stabilized dehulled grain to a thickness in a manner that allows minimal disruption to an outer bran layer thereof; (d) milling the pressed or rolled dehulled grain to produce a first grain flour and a coarse grain bran in a manner that allows minimal disruption to the outer bran layer; and I sieving and separating the first grain flour from the coarse grain bran; so as to provide a coarse grain bran product enriched with at least two components selected from the group consisting of beta -glucan, fats and fibre each of which being derived from the grain” (see, e.g., Tupper, abstract). Regarding claim 1 pertaining to the oat protein composition, Tupper teaches an oat composition (see, e.g., Tupper, pg. 10, lines 12-15), and does not teach that the oat composition contains organic solvents and traces of polysorbate (see, e.g., Tupper, pg. 10, lines 12-35 & pg. 11, lines 1-7). One of ordinary skill in the art would understand that less than 100 ppm of organic solvent and less than 300 ppm of polysorbate encompasses no organic solvent (i.e., 0 ppm) and no polysorbate (i.e., 0 ppm). Additionally, Tupper teaches oat compositions wherein the lipid content is below 10% (w/w), such as in groats, rolled oats, first pass oat bran, first pass oat flour, and second pass oat flour (see, e.g., Tupper, Table 2, pg. 21). Moreover, Tupper teaches that grinding and sieving the oats results in varying particle size 10 to 1000 µm (see, e.g., Tupper, pg. 8, lines 22-23 & Table 3, pg. 22). Regarding claims 3, 14, and 21 pertaining to the percentage of protein in the composition, Tupper teaches that the compositions contain proteinaceous material present in an amount greater than 15% (w/w) (see, e.g., Tupper, pg. 11, lines 16-17); therefore, one of ordinary skill in the art would readily understand that this can include proteinaceous material between 15% and 100% since the amount is greater than 15% (w/w). Regarding claims 6 and 17-18 pertaining to the percentage of total dietary fibers, Tupper teaches oat compositions comprising total dietary fibers from 3.8% to 10%, such as rolled oats, first pass oat flour, and second pass oat flour (see, e.g., Tupper, Table 2, pg. 21). Regarding claims 7 and 19 pertaining to the particle size, Tupper teaches that grinding and sieving the oats results in varying particle size 10 to 1000 µm (see, e.g., Tupper, pg. 8, lines 22-23 & Table 6, pg. 27). Moreover, Tupper teaches preparation of a fine grain bran concentrate that has an average particle diameter of about 20 to 150 µm (see, e.g., Tupper, pg. 9, lines 12-13). Regarding claim 20 pertaining to the extractable lipid content, Tupper teaches oat compositions wherein the lipid content is below 10% (w/w), such as in groats, rolled oats, first pass oat bran, first pass oat flour, and second pass oat flour (see, e.g., Tupper, Table 2, pg. 21). However, Tupper does not teach: measuring the particle size using laser diffraction (claim 1); or wherein, based on the total weight of the proteins in the composition, said composition comprises: from 0.5 to 30% of proteins having a molecular weight of 300kDa and more, from 30 to 75% of proteins having a molecular weight of between 50 and 300kDa, from 10 to 50% of proteins having a molecular weight of between 10 and 50kDa, from 0.5 to 20% of proteins having a molecular weight of l0kDa and less, wherein the sum of the foregoing protein fractions is 100% (claim 1); or wherein said composition comprises, based on the total weight of proteins in the composition: from 5 to 15% of proteins having a molecular weight of 300 kDa and more, from 45 to 65% of proteins having a molecular weight of between 50 and 300 kDa, from 25 to 45% of proteins having a molecular weight of between 10 and 50 kDa, and from 1 to 10% of proteins having a molecular weight of 10 kDa and less, wherein the sum of the foregoing protein fractions is 100% (claim 4); or wherein the composition comprises from 0.1 to 10% by weight of starch on dry matter based on the total dry weight of the oat protein composition (claim 5); or wherein the composition comprises from 0.5 to 6% by weight of starch on dry matter based on the total dry weight of the oat protein composition (claim 15); or wherein the composition comprises from 1 to 4% by weight of starch on dry matter based on the total dry weight of the oat protein composition (claim 16). Sjoo’s general disclosure relates to “the use of non-dissolved starch based particles, having a particle size of 0.2-4 pm and having a composition of 0.3-5% by weight of protein, 0.1-4% by weight of lipids, 0-1.6% by weight fibre and <0.45% by weight ash and the remaining part of the composition is carbohydrate adding up to 100% by weight, in cosmetic formulations” (see, e.g., Sjoo, abstract). Moreover, Sjoo discloses “a process for the preparation of said starch particle, comprising the following steps: subjecting dehulled grains or grain press cake to wet or dry milling for providing a flour with the size of 0.2-2.0 mm; mixing said flour with water for hydration during a period of 0.5-6 hours for efficient fibre separation; separation of a light phase comprising mainly starch and protein and a heavy phase comprising fibre; pH adjustment of light phase to pH 6-12; separation of proteins and starch from light phase based on density and size; and drying (see, e.g., Sjoo, [0014]-[0020]). Furthermore, Sjoo discloses “The starch particles according to the invention is from a botanical source chosen from quinoa, amaranth, tapioca, rice, oat, wheat, barley, millet, canihua, including waxy and high amylose varieties of any of the previously mentioned botanical sources” (see, e.g., Sjoo, [0029]). Regarding claim 1 pertaining to laser diffraction, Sjoo teaches that the particle sizes of the starch granules were measured using laser diffraction (see, e.g., Sjoo, [0070]). Weissbrodt’s general disclosure relates to “large agglomerate particles obtainable by spray-drying agglomeration” (see, e.g., Weissbrodt, abstract). Moreover, Weissbrodt discloses “an object of the present invention to provide large particles, more particularly agglomerate particles which are larger than 200 μm preferably larger than 300 μm. It is intended that the agglomerate particles be toxicologically safe for the foodstuff sector. It is a further object of the present invention to provide agglomerate particles which are stable and have a good solubility and low dust values when applied. It is likewise an object of the present invention to provide agglomerate particles which have a high load of active substances, such as flavourings for example” (see, e.g., Weissbrodt, [0005]). Additionally, Weissbrodt discloses that the agglomerate particles are preferably intermediate products and can be used in end products in the food sector, such as in oat protein drinks (see, e.g., Weissbrodt, [0061]). Regarding claim 1 pertaining to laser diffraction, Weissbrodt teaches “The particle sizes of the agglomerates produced according to the invention were determined by means of a measurement by means of laser diffraction. The principle of laser diffraction is a distinctly flexible technique, having fundamentally the means of measuring the size of any material in another. The only conditions of the technique are that each phase is optically demarcated from the other and the medium is transparent for the laser wavelengths. This means that the refractive index of material and of the surrounding medium must differ. The measurement is achieved by introducing the sample into the laser beam by means of the corresponding modules for powders or emulsions/suspensions. The light scattered by the particles is detected. The entire laser output beamed towards the path from this system is measured and also allows the sample concentration to be inferred. The instrument available here (Malvern Mastersizer 2000 with Scirocco drying unit) provides the means of measuring powders up to a maximum particle size of 2 mm. With said instrument, it is possible to apply a dispersion pressure of from 0 to 4 bar to feed in the powder. However, care should be taken not to destroy the product while this is done, since, at the pressure set, suction is carried out against an impact plate during the feeding-in process” (see, e.g., Weissbrodt, [0081]-[0084]). Bruckner-Guhmann’s general disclosure relates to “Foaming ability of oat protein isolate (OPI) was analysed at pH 4 and 7. Foaming properties were influenced by partial hydrolysis with trypsin (OPT) and alcalase (OPA)” (see, e.g., Bruckner-Guhmann, abstract). Moreover, Bruckner-Guhmann discloses “The aim of this study was to develop a systematic understanding of the foaming characteristics of OPI and to evaluate the impact of enzymatic hydrolysis on both the foaming properties and interfacial rheology” (see, e.g., Bruckner-Guhmann, Introduction, pg. 2096). Regarding claims 1 and 4 pertaining to the total weight of the proteins, Bruckner-Guhmann teaches at pH 7 that an oat protein isolate has approximately 10% of proteins with a molecular weight >300 kDa, approximately 2% of proteins with a molecular weight of 50-300 kDa, approximately, 28% of proteins with a molecular weight of 10-50 kDa, and approximately 60% of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). However, Bruckner-Guhmann teaches that the use of alcalase and trypsin at pH 7 results in an increase in the percentage of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). Furthermore, at pH 4, Bruckner-Guhmann teaches that the percentage of proteins with a molecular weight between 5-20 kDa increases to approximately 90% in the oat protein isolate, while the percentage of proteins <2 kDa decreases to approximately 10% in the oat protein isolate (see, e.g., Bruckner-Guhmann, Figure 1D). Therefore, from these results, one of ordinary skill in the art would readily understand that the use of alcalase and trypsin for enzymatic hydrolysis, as well as altering the pH of the composition, results in varying protein molecular weights within the oat protein concentrate. Regarding claims 5 and 15-16 pertaining to the percentage of starch in the oat protein composition, Bruckner-Guhmann teaches an oat protein isolate with 1.3 ± 0.04% starch (see, e.g., Bruckner-Guhmann, Table 1). It would have been first obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Tupper’s oat composition, wherein the particle size of the oat composition is measured using laser diffraction, as taught by Sjoo and Weissbrodt. One would have been motivated to do so because Sjoo teaches measuring the particle sizes of the starch granules were measured using laser diffraction (see, e.g., Sjoo, [0070]), wherein the starch granules can be derived from oat (see, e.g., Sjoo, [0029]). Moreover, Weissbrodt teaches that laser diffraction is a distinctly flexible technique, having fundamentally the means of measuring the size of any material in another, and laser diffraction provides the means of measuring powders up to a maximum particle size of 2 mm (see, e.g., Weissbrodt, [0081]-[0084]). Furthermore, Tupper teaches particles derived from an oat protein composition, wherein the particles have a diameter of 10 to 1000 µm due to grinding and sieving (see, e.g., Tupper, pg. 8, lines 22-23 & Table 3, pg. 22). Therefore, based on the teachings of Tupper, Sjoo, and Weissbrodt, it would have been obvious to use laser diffraction to measure the particle size within an oat protein composition. One would have expected success because Tupper, Sjoo, and Weissbrodt all teach particle compositions derived from oats or other plant sources, wherein the particles have varying diameters. It would have been secondly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Tupper’s oat protein composition, wherein the composition contains 0.1 to 10% starch, as taught by Bruckner-Guhmann. One would have been motivated to do so because Bruckner-Guhmann teaches that the oat protein isolate containing approximately 1.5% starch was produced from an oat protein concentrate that contains approximately 33% starch, wherein the concentrate was subsequently diluted and the pH was adjusted (see, e.g., Bruckner-Guhmann, Materials, pg. 2096). Moreover, Tupper teaches “A key characteristic of oat bran is that unlike most other cereal brands, it contains large amounts of adhering endosperm with accompanying significant concentrations of β-glucan and starch” (see, e.g., Tupper, pg. 1, lines 31-34). Additionally, Tupper teaches that starch contributes to the viscosity of an oat gel powder (see, e.g., Tupper, pg. 13, lines 29-31); therefore, one of ordinary skill in the art would readily understand that increasing the starch percentage will increase the viscosity of an oat gel powder. Therefore, based on the teachings of Tupper and Bruckner-Guhmann, it would have been obvious to produce an oat protein composition, wherein the composition comprises starch from 0.1 to 10%. One would have expected success because Tupper and Bruckner-Guhmann both teach oat protein compositions comprising starch. Regarding claim 1 and 4’s percentage limitations, those working in the biological and/or pharmaceutical arts would understand that the adjustments of particular conventional working conditions (e.g., concentration, percentages, amounts, etc.) is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan (see, e.g., MPEP 2144.05). For example, Bruckner-Guhmann teaches that the protein composition within an oat protein isolate varies based on the pH of the composition, as well as whether alcalase and/or trypsin is used (see, e.g., Bruckner-Guhmann, Figures 1C-1D). Bruckner-Guhmann teaches at pH 7 that an oat protein isolate has approximately 10% of proteins with a molecular weight >300 kDa, approximately 2% of proteins with a molecular weight of 50-300 kDa, approximately, 28% of proteins with a molecular weight of 10-50 kDa, and approximately 60% of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). However, Bruckner-Guhmann teaches that the use of alcalase and trypsin at pH 7 results in an increase in the percentage of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). Furthermore, at pH 4, Bruckner-Guhmann teaches that the percentage of proteins with a molecular weight between 5-20 kDa increases to approximately 90% in the oat protein isolate, while the percentage of proteins <2 kDa decreases to approximately 10% in the oat protein isolate (see, e.g., Bruckner-Guhmann, Figure 1D). Therefore, from these results, one of ordinary skill in the art would readily understand that the use of alcalase and trypsin for enzymatic hydrolysis, as well as altering the pH of the composition from a neutral pH to an acidic pH, results in varying protein molecular weights within the oat protein concentrate. Therefore, one of ordinary skill in the art would reasonably understand that addition of alcalase and/or trypsin for enzymatic hydrolysis will increase the percentage of small molecular weight proteins, and decreasing the pH (i.e., addition of an acidic solution) will result in a decrease in high molecular weight proteins, as taught by Bruckner-Guhmann. This is motivation for someone of ordinary skill in the art before the effective filing date of the claimed invention to practice or test the parameter(s) widely to find those that are functional or optimal which then would be inclusive or cover the steps as instantly claimed. Absent any teaching of criticality by the Applicant concerning the percentage of protein with specific molecular weights, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization Examiner’s Response to Arguments Applicant's arguments filed 06/10/2026 have been fully considered but they are not persuasive. Regarding Applicant’s arguments that Bruckner-Guhmann does not teach the claimed protein percentages at 50-300 kDa and 10 kDa and less (remarks, page 7), this argument is not persuasive because, as discussed above, these protein percentages at the claimed molecular weight ranges is a matter of routine optimization. Bruckner-Guhmann teaches at pH 7 that an oat protein isolate has approximately 10% of proteins with a molecular weight >300 kDa, approximately 2% of proteins with a molecular weight of 50-300 kDa, approximately, 28% of proteins with a molecular weight of 10-50 kDa, and approximately 60% of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). However, Bruckner-Guhmann teaches that the use of alcalase and trypsin at pH 7 results in an increase in the percentage of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). Furthermore, at pH 4, Bruckner-Guhmann teaches that the percentage of proteins with a molecular weight between 5-20 kDa increases to approximately 90% in the oat protein isolate, while the percentage of proteins <2 kDa decreases to approximately 10% in the oat protein isolate (see, e.g., Bruckner-Guhmann, Figure 1D). From the teachings of Bruckner-Guhmann, one of ordinary skill in the art would understand that the percentages of proteins at 50-300 kDa and 10 kDa and less varies based on the pH of the composition. When the pH is neutral (i.e., pH=7), the oat protein isolate has approximately 2% of proteins with a molecular weight of 50-300 kDa and approximately 60% of proteins with a molecular weight <10 kDa (see, e.g., Bruckner-Guhmann, Figure 1C). However, when the pH is more acidic (i.e., pH=4), the percentage of proteins with a molecular weight between 5-20 kDa increases to approximately 90% in the oat protein isolate, while the percentage of proteins <2 kDa decreases to approximately 10% in the oat protein isolate (see, e.g., Bruckner-Guhmann, Figure 1D). This is motivation for one of ordinary skill in the art to manipulate the pH of the oat protein composition in order to obtain percentages of proteins at specific molecular weights are functional or optimal. Furthermore, manipulation of percentages within a composition, such as percentages of proteins, is considered by those working in the biological and/or pharmaceutical arts merely adjustment(s) of particular conventional working conditions and is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan (see, e.g., MPEP 2144.05). Additionally, based on the teachings of Bruckner-Guhmann, a person of ordinary skill in the art would have has a reasonable expectation of success to formulate the claimed percentages of proteins at 50-300 kDa and 10 kDa and less by manipulating the pH of the protein composition. Furthermore, Applicant has not provided data or evidence that the claimed protein percentages are critical to the invention (see, e.g., MPEP 2144.05(III)(A)). Therefore, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization. Moreover, Applicant argues about a reading of Fuentes; however, Fuentes was not cited by Applicant for support, not relied upon in the above presented rejection; therefore, Applicant’s argument regarding this is moot. New Grounds of Rejection Necessitated by Amendments Double Patenting The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer. Claims 1, 3-4, 14, and 20-21 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 14, 16-20, and 26-27 of copending Application No. 18/260,290 (reference application; herein referred to as “App’290”). Although the claims at issue are not identical, they are not patentably distinct from each other because App’290 claims: An oat protein composition wherein the oat protein composition is a protein concentrate or a protein isolate, and wherein said oat protein composition comprises, by weight, at least 50% oat protein, less than 10% extractable lipids, a ratio of oat insoluble fiber/β- glucan of at least 5 (claim 14); wherein the oat protein composition is an oat protein isolate comprising more than 70% oat protein by weight (claim 16); wherein the oat protein composition comprises at least 80% oat protein by weight (claim 17); wherein the oat protein composition comprises at least 85% oat protein by weight (claim 18); wherein the oat protein composition comprises less than 8% extractable lipids by weight (claim 19); wherein the oat protein composition comprises less than 6% extractable lipids by weight (claim 20); wherein based on the total weight of proteins in the composition, the composition comprising: from 0.5 to 30% of proteins having a molecular weight of 300 kDa, from 30 to 75% of proteins having a molecular weight of between 50 and 300 kDa, from 10 to 50% of proteins having a molecular weight of between 10 and 50 kDa, from 0.5 to 20% of proteins having a molecular weight of 10 kDa and less. the sum of making 100% (claim 26); wherein based on the total weight of proteins in the composition, the composition comprising: from 5 to 15% of proteins having a molecular weight of 300 kDa and more, from 45 to 65% of proteins having a molecular weight of between 50 and 300 kDa, from 25 to 45% of proteins having a molecular weight of between 10 and 50 kDa, from 10% of proteins having a molecular weight of 10 kDa and less, the sum making 100% (claim 27). This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Claim 1, 3-7, 14-21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 14, 16, 18-20, and 31-34 of copending Application No. 17/597,222 (reference application; herein referred to as “App’222”). Although the claims at issue are not identical, they are not patentably distinct from each other because App’222 claims: An oat protein composition wherein said composition does not contain traces of organic solvent, has residual lipid content below 10% by weight on dry matter based on the total dry weight of the oat protein composition and has a mean particle size (d 50), determined by laser diffraction, greater than 10 microns; and wherein said oat protein composition comprises, based on the total weight of proteins in the composition: from 5 to 15% of proteins having a molecular weight of 300kDa and more, from 45 to 65% of proteins having a molecular weight of between 50 and 300kDa, from 25 to 45% of proteins having a molecular weight of between 10 and 50kDa, from 1 to 10% of proteins having a molecular weight of l0kDa and less, the sum making 100% (claim 14); wherein said oat protein composition contains more than 70% by weight of protein on dry matter based on the total dry weight of the oat protein composition (claim 16); wherein the oat protein composition comprises from 0.1 to 10% by weight of starch on dry matter based on the total dry weight of the oat protein composition (claim 18); wherein the oat protein composition comprises a total dietary fiber going from 0.1 to 10% by weight of the dietary fiber on dry matter based on the total dry weight of the oat protein composition (claim 19); wherein the oat protein composition has: a mean particle size greater than 20 microns, and - a mean particle size lower than 300 microns (claim 20); wherein said oat protein composition contains more than 80% by weight of protein on dry matter based on the total dry weight of the oat protein composition (claim 31); wherein the oat protein composition comprises from 1 to 4% by weight of starch on dry matter based on the total dry weight of the oat protein composition (claim 32); wherein the oat protein composition comprises a total dietary fiber going from 1 to 4% by weight of the dietary fiber on dry matter based on the total dry weight of the oat protein composition (claim 33); and wherein the oat protein composition has: a mean particle size greater than 40 microns, and a mean particle size lower than 150 microns (claim 34). This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Examiner’s Response to Arguments Regarding Applicant’s arguments pertaining to the previous nonstatutory double patenting rejections (remarks, page 4), as stated above, all previous nonstatutory double patenting rejections have been withdrawn necessitated by Applicant’s amendments; therefore, Applicant’s arguments are moot. Conclusion Claims 1, 3-7, and 14-21 are rejected. No claims are allowed. THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. Correspondence Information Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 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, Sharmila Landau can be reached at (571) 272-0614. 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. /NATALIE IANNUZO/Examiner, Art Unit 1653 /SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
Read full office action

Prosecution Timeline

Jun 28, 2023
Application Filed
Feb 11, 2026
Non-Final Rejection mailed — §103, §DP
Jun 10, 2026
Response Filed
Sep 04, 2026
Final Rejection mailed — §103, §DP (current)

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4y 3m to grant Granted Sep 01, 2026
Patent 12662664
A MODIFIED BACTERIAL HYALURONIDASE POLYPEPTIDE, PRODUCTION PROCESS, PHARMACEUTICAL COMPOSITIONS AND THEIR USES
3y 8m to grant Granted Jun 23, 2026
Patent 12522810
Transaminase Mutant And Use Thereof
3y 2m to grant Granted Jan 13, 2026
Patent 12410411
BIOCATALYTIC TECHNIQUES
3y 3m to grant Granted Sep 09, 2025
Study what changed to get past this examiner. Based on 4 most recent grants.

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Prosecution Projections

3-4
Expected OA Rounds
12%
Grant Probability
84%
With Interview (+71.4%)
3y 4m (~1m remaining)
Median Time to Grant
Moderate
PTA Risk
Based on 40 resolved cases by this examiner. Grant probability derived from career allowance rate.

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