The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 June 8, 2026 has been entered.
Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Claims 1-10, 14, 18, 22, 24, 26-27, 29-30, 32, 40 are canceled. Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50, to SEQ ID NO: 2, are under consideration.
This application is a CIP of U.S. Application 18336915, filed June 16, 2023, which is a CON of U.S. Application 18050213, filed October 27, 2022, now U.S. Patent 11718644, which is a CON of PCT/US22/380774, filed July 22, 2022, which claims benefit of provisional applications 63/225388, filed July 23, 2021, and 63/225410, filed July 23, 2021. This application is also a CIP of U.S. Application 17508064, filed October 22, 2021, now abandoned, which is a CON of PCT/US20/47076, filed August 19, 2020, which claims benefit of provisional application 62/888674, filed August 19, 2019.
Objections and Rejections
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The term “substantially” in claims 11, 31, 39, 45 is a relative term which renders the claim indefinite. The term “substantially” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
Claims 12-13, 15-17, 19-21, 23, 25, 28, 33-39, 41, 42-44, 46-50 are included in this rejection because they are dependent on the above claims and fail to cure their defects.
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 (i.e., changing from AIA to pre-AIA ) 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, 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.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-35, 37-39, 41, are rejected under 35 U.S.C. 103 as being unpatentable over Anchel (WO 2016077457; IDS 07.25.25, previously cited), and evidenced by Daly et al. (2005 J Mol Recognit 18: 119-138, published online November 26, 2004; previously cited), which disclose Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11 (p. 131) and/or Ivey et al. (WO 2020041483; IDS 07.25.25), which disclose that a recombinant egg white protein composition expressed in Pichia pastoris comprises Man7-9GlcNAc2, or 7-9 mannose units (p. 25-26 Table 1).
Anchel discloses a consumable food product comprising one (or more) recombinant egg white protein selected from ovalbumin, and one or more ingredients which are food additives (at least paragraphs 0007-0008, 0082-0083, 0131). Anchel discloses food additives add volume and/or mass to a composition and improve functional performance and/or physical characteristics; carbohydrates can be added to increase resistance to heat damage, e.g. less protein denaturation during drying and improve stability and flowability of dried compositions; where food additives include starch (at least paragraph 0146). Anchel also provides for an egg white protein composition comprising one recombinant egg white protein (at least paragraph 0013). Anchel discloses recombinant expression of an ovalbumin (an egg white protein) in a host cell (at least example 1, paragraphs 0161-0164), where the host cell is Pichia pastoris (paragraphs 0165-0169), and purifying the recombinant protein, dialyzing with an aqueous buffer of appropriate pH to obtain a recombinant ovalbumin protein composition (paragraphs 0171-0175, see also Fig. 16), and further lyophilization (e.g. spray-drying) to obtain a powdered egg white protein composition (paragraph 0174).
Anchel discloses that the consumable food product comprises one recombinant egg white protein being ovalbumin and a food additive (paragraph 0082), and an embodiment that the food additive does not comprise any egg white protein (paragraph 0083); thus, reading on the instant claim limitation that the food product does not comprise any egg white protein except the recombinant ovalbumin.
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to arrive at the claimed food product comprising a powdered composition comprising recombinant ovalbumin (rOVA) and at least one starch (instant claims 11, 31, 45, 50). The motivation to do so is given by the prior art Anchel, which discloses a consumable food product comprising recombinant ovalbumin as the one (sole) egg white protein in a powdered composition and a starch as a food additive. One of ordinary skill would have a reasonable expectation of success because Anchel discloses methods for expressing the rOVA and arriving at a powdered composition and methods and ingredients for making a consumable food product comprising an egg white protein composition.
Further, since the rOVA composition of Anchel is expressed and produced in the same host cell (i.e. a Pichia pastoris host cell) as the claimed rOVA composition (the instant specification discloses that a “host cell” for expression of recombinant ovalbumin is Pichia Pastoris) (instant specification paragraphs 0568, 0953-0954, 0998-0999), it would follow that the rOVA composition of Anchel necessarily comprises a rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns (instant claims 11-12, 13, 17, 28, 31, 33-35, 37, 44, 45-47). This is supported or evidenced by Daly et al., which disclose Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11 (p. 131) and/or Ivey et al., which disclose that a recombinant egg white protein composition expressed in Pichia pastoris comprises Man7-9GlcNAc2, or 7-9 mannose units (p. 25-26 Table 1).
Anchel discloses the recombinant egg white protein composition may comprise at least 80%-99% protein by dry weight (at least paragraph 0098); thus, reading on the instant range of at least 80% as recited in instant claims 11, 31, 45.
Anchel discloses the recombinant egg white protein composition may comprise drying and/or concentrating to 0.001-10% solvent (water) by weight (at least paragraph 0158); thus, reading on the instant range of less than 10% moisture content as recited in instant claims 11, 31, 45.
Anchel discloses that the recombinant egg white protein is purified by any variety of conventional methods, including but not limited to chromatography (at least paragraph 0129); treated for longer storage and to preserve color including by being clarified, filtered, desugared, spray dried, and/or pasteurized (at least paragraph 0145), where it would be obvious that such purification and/or treatment steps result in the powdered recombinant egg white protein being substantially free of exopolysaccharides (EPS) and microbial off-flavor components derived from the Pichia pastoris host cell as recited in instant claims 11, 31, 45.
Regarding the instant limitation that the powdered composition replaces functional characteristics provided by multiple proteins in native egg, Anchel discloses that the recombinant egg white protein is provided as a processing agent in the consumable food product (paragraph 0030), and an embodiment of the processing agent is to act as an egg replacement (at least paragraphs 0031-0034, 0132-0136, p. 51-52 claims 24-26). Further, since Anchel discloses a rOVA composition that appears to be essentially the same as the recited rOVA composition (the rOVA composition disclosed in Anchel is produced by the same expression system recited and Fig. 1 of Anchel discloses the amino acid sequence of chicken ovalbumin SEQ ID NO: 1, which shares 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, the amino acid sequence of chicken ovalbumin secreted from Pichia), it logically follows that the rOVA composition disclosed in Anchel provides and/or replaces functional characteristics provided by multiple proteins in native egg and having performance at least equivalent to that of native egg in a corresponding food product (instant claims 11, 31, 45). See also MPEP 2112.01, which notes 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).
Regarding the instant limitation that the powdered composition provides to the food product at least one functional characteristic selected from gelling, foaming, whipping, fluffing, binding, springiness, aeration, coating, film forming, emulsification, etc., Anchel discloses that the recombinant egg white protein is provided as a processing agent in the consumable food product (paragraph 0030), and an embodiment of the processing agent is to act as an emulsifier, binding agent, leavening agent, thickening agent, moisturizing agent, adhesive, browning agent, clarification agent, gelation agent, etc. (at least paragraphs 0031-0034, 0132-0136, p. 51-52 claims 24-26). Further, since Anchel discloses a rOVA composition that appears to be essentially the same as the recited rOVA composition (the rOVA composition disclosed in Anchel is produced by the same expression system recited and Fig. 1 of Anchel discloses the amino acid sequence of chicken ovalbumin SEQ ID NO: 1, which shares 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, the amino acid sequence of chicken ovalbumin secreted from Pichia), it logically follows that the rOVA composition disclosed in Anchel provides to the food product at least one of the recited functional characteristics including gelling, foaming, whipping, fluffing, binding, etc. (instant claims 11, 31, 45). See also MPEP 2112.01, which notes 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).
Regarding instant claims 15, 38, as noted above, Anchel discloses the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3, see also Fig. 16), where there is no galactose unit in the N-linked oligosaccharide produced in Pichia pastoris (Daly et al. p. 129). Therefore, Anchel can be deemed to disclose that the N-linked glycan does not comprise a galactose unit.
Regarding instant claim 16, Anchel discloses that the recombinant egg white protein has a glycosylation, acetylation, or phosphorylation pattern different from the egg white protein in egg white (paragraphs 0011, 0061, 0089, 0169).
Regarding instant claim 17, as noted above, Anchel discloses the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3, Fig. 16), where it is known that the amino-terminal methionine residue is cleaved in recombinant proteins produced and expressed in Pichia pastoris (Daly et al. p. 126). Therefore, Anchel can be deemed to disclose that the amino acid sequence of the rOVA lacks an N-terminal methionine.
Regarding instant claims 19-20, 39, Anchel discloses that the recombinant egg white protein is provided as a processing agent in the consumable food product (paragraph 0030), and an embodiment of the processing agent is to act as an emulsifier, binding agent, leavening agent, thickening agent, moisturizing agent, adhesive, browning agent, clarification agent, gelation agent, etc. (at least paragraphs 0031-0034, 0132-0136, p. 51-52 claims 24-26). Anchel discloses that any of the recombinant egg white protein composition has improved properties, including foam strength, height, gelation, etc. (at least paragraphs 0018, 0133-0136). Additionally, since Anchel discloses a rOVA composition that appears to be essentially the same as the recited rOVA composition (the rOVA composition disclosed in Anchel is produced by the same expression system recited and Fig. 1 of Anchel discloses the amino acid sequence of chicken ovalbumin SEQ ID NO: 1, which shares 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, the amino acid sequence of chicken ovalbumin secreted from Pichia), it logically follows that the rOVA composition disclosed in Anchel provides the same improved characteristics of foaming, gelling, and binding recited in the instant claims. See also MPEP 2112.01, which notes 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).
Regarding instant claim 21, Anchel discloses the amino acid sequence of chicken ovalbumin (SEQ ID NO: 1) (paragraph 0040, also Fig. 1), which has 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, where instant SEQ ID NO: 2 is the amino acid sequence of chicken ovalbumin secreted from Pichia (instant specification p. 79 Table 1). As noted above, Anchel discloses the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3). Therefore, Anchel can be deemed to disclose that the rOVA produced in the Pichia pastoris host cell comprises the amino acid sequence of instant SEQ ID NO: 2.
Regarding instant claims 23, 44, 49, Anchel discloses there is consumer demand to eschew cholesterol-rich egg yolk in favor of relatively high protein, low carbohydrate egg white preparations (at least paragraph 0002). Anchel discloses that any of the recombinant egg white protein composition may lack cholesterol; the egg white protein composition may comprise less than 5% fat by dry weight; the egg white protein composition may lack glucose (at least paragraphs 0016, 0099). Anchel discloses that the recombinant egg white protein is purified by any variety of conventional methods, including but not limited to chromatography (at least paragraph 0129); treated for longer storage and to preserve color including by being clarified, filtered, desugared, spray dried, and/or pasteurized (at least paragraph 0145). Anchel discloses that the recombinant egg white protein isolated is soluble (at least paragraph 0129). Anchel discloses that the purified recombinant ovalbumin composition is in an aqueous buffer solution or in a powdered composition (example 3, also paragraph 0174). Therefore, it would be obvious that such purification and/or treatment steps disclosed in Anchel result in the powdered recombinant egg white protein having less than 5% mineral salts (ash) from culture medium, less than 2% total fat, and less than 22% total carbohydrate, and being soluble in water.
Regarding instant claim 25, Anchel discloses that the recombinant egg white protein composition is acidic, neutral or basic, including having a pH of about 6 (paragraph 0100).
Regarding instant claim 41, Anchel discloses purifying the recombinant ovalbumin protein composition including by diafiltration and including vessels allow continuous circulation and filtration in a separate vessel to collect protein without interrupting cell growth and dialyzing the purified recombinant ovalbumin protein and lyophilizing the purified recombinant ovalbumin protein (at least example 3, Fig. 16).
Regarding instant claims 42, 43, 48, 50, Anchel discloses that the consumable food product comprises one recombinant egg white protein being ovalbumin and a food additive (paragraph 0082), and an embodiment that the food additive does not comprise any egg white protein (paragraph 0083); thus, reading on the instant claim limitation that the food product does not comprise any egg white protein except the recombinant ovalbumin. Anchel discloses the recombinant egg white protein composition may comprise at least 80%-99% protein by dry weight (at least paragraph 0098); thus, reading on the instant range of at least 80% as recited in instant claims 11, 31, and 45 and the instant range of at least 60% as recited in instant claims 42-43, 48.
Reply: In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection anticipated by Anchel has been withdrawn. However, the claims remain unpatentable under 103 as obvious over Anchel for the reasons noted above and herein.
Applicants assert that the instant claims (i.e. amended claims 11, 31, and new claim 45) recite a “food product” comprising a “powdered composition” and a “starch.” Applicants assert that the “powdered composition” comprises: (1) "an N-linked glycan that, when secreted or expressed from a host cell, comprises 5-11 mannose units," (2) where "rOVA is the sole egg-white protein," (3) where "rOVA comprises at least 80% weight/weight of total protein in the total powdered composition," (4) where "the powdered composition is substantially free of exopolysaccharide (EPS) and microbial off-flavor compounds derived from the host cell," and (5) where "the powdered composition has less than 10% moisture content."
Applicants’ remarks are not persuasive. As noted in the 103 rejection above, Anchel fairly discloses a consumable food product comprising a powdered composition comprising recombinant ovalbumin (rOVA) and at least one starch, and where the rOVA is the only egg white protein in the powdered composition.
Regarding the instant limitation (1) "an N-linked glycan that, when secreted or expressed from a host cell, comprises 5-11 mannose units," as previously noted, the rOVA composition of Anchel is expressed and produced in the same host cell (i.e. a Pichia pastoris host cell) as the claimed rOVA composition (the instant specification discloses that a “host cell” for expression of recombinant ovalbumin is Pichia Pastoris) (instant specification paragraphs 0568, 0953-0954, 0998-0999), it would follow that the rOVA composition of Anchel necessarily comprises a rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns. This is supported or evidenced by Daly et al., which disclose Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11 (p. 131) and/or Ivey et al., which disclose that a recombinant egg white protein composition expressed in Pichia pastoris comprises Man7-9GlcNAc2, or 7-9 mannose units (p. 25-26 Table 1).
Regarding the instant limitation (2) where "rOVA is the sole egg-white protein," Anchel expressly discloses that the consumable food product comprises one recombinant egg white protein being ovalbumin and a food additive (paragraph 0082), and an embodiment that the food additive does not comprise any egg white protein (paragraph 0083); thus, reading on the instant claim limitation that the food product does not comprise any egg white protein except the recombinant ovalbumin.
Regarding instant limitation (3) where "rOVA comprises at least 80% weight/weight of total protein in the total powdered composition," Anchel discloses the recombinant egg white protein composition may comprise at least 80%-99% protein by dry weight (at least paragraph 0098); thus, reading on the instant range of at least 80% as recited in instant claim(s).
Regarding instant limitation (4) where "the powdered composition is substantially free of exopolysaccharide (EPS) and microbial off-flavor compounds derived from the host cell," Anchel discloses that the recombinant egg white protein is purified by any variety of conventional methods, including but not limited to chromatography (at least paragraph 0129); treated for longer storage and to preserve color including by being clarified, filtered, desugared, spray dried, and/or pasteurized (at least paragraph 0145), where it would be obvious that such purification and/or treatment steps result in the powdered recombinant egg white protein being substantially free of EPS and microbial off-flavor components derived from the Pichia pastoris host cell as recited in instant claims.
Regarding instant limitation (5) where "the powdered composition has less than 10% moisture content,” Anchel discloses the recombinant egg white protein composition may comprise drying and/or concentrating to 0.001-10% solvent (water) by weight (at least paragraph 0158); thus, reading on the instant range of less than 10% moisture content as recited in instant claims.
Applicants assert that the claimed powdered composition with rOVA as the sole egg-white protein surprisingly is able to replace, in a food product, “the functional characteristics that would otherwise be provided by multiple proteins in native egg” and still have a “performance at least equivalent to that of native egg” in various functional characteristics. Applicants assert that Anchel fails to disclose this element of the pending claims. Applicants assert that native whole egg is a multicomponent, function system; ovalbumin is only one component of this multicomponent/multifunctional system. Applicants assert that one of ordinary skill would have expected the functional characteristics of native whole egg in food systems arise from synergistic interactions among structurally and functionally distinct proteins and lipids, rather than from a single protein component (ovalbumin). Applicants assert that a skilled artisan would have expected that removal of even a few of these components providing these synergistic interactions in native whole egg would have impaired one or more of these characteristics; removal of all these components except for ovalbumin would have been expected to highly impair the characteristics.
Applicants’ remarks are not persuasive. Anchel discloses that there is demand for egg white proteins as a healthy option alternative to cholesterol-rich egg yolk (paragraph 0002) and that there is a need for alternative egg-free, egg white production methods which would benefit manufacturers of egg-white-based food mixes (paragraph 0005).
In this instance, Anchel expressly discloses that a consumable food product comprises one recombinant egg white protein, the one egg white protein selected from ovalbumin and a food additive (at least paragraphs 0007-0008, 0082-0083). Anchel further discloses an embodiment that the food additive does not comprise any egg white protein (paragraph 0083); therefore, making it obvious that the food product does not comprise any egg white protein except the one selected recombinant egg white protein ovalbumin. Anchel discloses that the recombinant egg white protein is provided as a processing agent in the consumable food product (paragraph 0030), and an embodiment of the processing agent is to act as an egg replacement, in addition to acting as an emulsifier, binding agent, leavening agent, thickening agent, moisturizing agent, adhesive, browning agent, clarification agent, gelation agent, etc. (at least paragraphs 0031-0034, 0132-0136, p. 51-52 claims 24-26). Therefore, Anchel discloses that the one recombinant egg white protein ovalbumin has the same purpose asserted by Applicants in a food product, which is to replace egg.
Further, as previously noted in the related parent application 17508064, it appears more expected than unexpected that food items made with ovalbumin alone is comparable to those made with native egg-white, for the reason that the prior art has recognized that ovalbumin as the most abundant protein in the egg-white possesses most of the cooking properties of egg-white. For example, US 20140099412 shows that ovalbumin has the foamability ([0026]); US 20020098198 teaches that ovalbumin is an effective foam stabilizer ([0047]); US 20090155443 discloses that ovalbumin has the gelling capability ([0046]); US 20050202149 indicates that ovalbumin has the emulsifying ability ([0026]); US 20160106701 teaches that ovalbumin has a thickening effect ([0035]); US 5514408 teaches that ovalbumin could be used as a food binder (column 4, line 1-2); US 20200345020 teaches that ovalbumin is a film-forming agent in food ([0040]) (see at least p. 11-12 of the May 20, 2022 final office action in the parent application 17508064). It is noted that instant claims 11, 31, 45 also recite these characteristics of ovalbumin. Therefore, the finding that in a food product made with ovalbumin, where the ovalbumin has the functional characteristics provided by native egg and a performance at least equivalent to that of native egg is not likely to be surprising and/or unexpected.
Applicants assert that yet in the claimed “powdered composition,” rOVA replaces “functional characteristics that would otherwise be provided by multiple proteins in native egg” while still providing a “performance at least equivalent to that of native egg in a corresponding food product” in “at least one functional characteristic.” Applicants assert that this is supported by examples in the instant specification. Applicants point to examples 10, 11, 12, 20, 23 of the instant specification. Applicants assert that the amended claims are now focused on the food product made with a powdered composition comprising the rOVA. Applicants assert that the features of the powdered composition and components of the food product contribute to the functionality as well as to the features of the rOVA protein.
Applicants’ remarks are not persuasive. Firstly, it is noted that the instant claims are far broader than the examples referred to by Applicants. The showing is not commensurate in scope with the instant claims.
Further, it is noted that examples 10, 11, 12, 20, 23 all appear to disclose that the various functional characteristics observed are provided by the rOVA in the different food products (i.e. Table 6, Table 9, Table 18). As already noted, since Anchel discloses a rOVA composition that appears to be essentially the same as the recited rOVA composition (the rOVA composition disclosed in Anchel is produced by the same expression system recited and Fig. 1 of Anchel discloses the amino acid sequence of chicken ovalbumin SEQ ID NO: 1, which shares 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, the amino acid sequence of chicken ovalbumin secreted from Pichia), it logically follows that the rOVA composition disclosed in Anchel provides to the food product the same functional characteristics including gelling, foaming, whipping, fluffing, binding, etc., including any performance at least equivalent to that of native egg asserted by Applicants. See also MPEP 2112.01, which notes 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).
Anchel further discloses that the inclusion of food additives add volume and/or mass to a composition and improve functional performance and/or physical characteristics; carbohydrates can be added to increase resistance to heat damage; whipping additives may be added to dried composition to improve whipping ability and aeration properties, etc. (at least paragraph 0146). Therefore, Anchel also recognizes that any functional feature of the egg white protein in a food composition can be improved upon by including a food additive.
Therefore, Applicants’ remarks that it was unexpected and surprisingly that the claimed powdered composition provides replacement of functional characteristics of egg in a food composition are not found persuasive.
Additionally, as previously noted, MPEP 716.01(c) notes that objective evidence which must be factually supported by an appropriate affidavit or declaration to be of probative value includes evidence of unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor. See, for example, In re De Blauwe, 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984) ("It is well settled that unexpected results must be established by factual evidence." "[A]ppellants have not presented any experimental data showing that prior heat-shrinkable articles split. Due to the absence of tests comparing appellant's heat shrinkable articles with those of the closest prior art, we conclude that appellant's assertions of unexpected results constitute mere argument."). See also In re Lindner, 457 F.2d 506, 508, 173 USPQ 356, 358 (CCPA 1972); Ex parte George, 21 USPQ2d 1058 (Bd. Pat. App. & Inter. 1991).
Further, the arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965). Examples of attorney statements which are not evidence and which must be supported by an appropriate affidavit or declaration include statements regarding unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor.
Further, MPEP 716.02(b) notes that Applicant has the burden to establish that the results are unexpected and significant. Evidence of unexpected properties may be in the form of a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. See also MPEP 716.02(e) noting that the claimed subject matter has to be compared with the closest prior art to be effective to rebut a prima facie case of obviousness.
In this instance, Applicants have not provided a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. The closest prior art is the rOVA composition produced by Pichia pastoris of Anchel (Anchel examples 1-3, Fig. 16).
Regarding Applicants’ remarks on the 103 rejection and unexpected results of the claimed powdered composition as provided in the examples of the instant specification, the remarks are not persuasive for the reasons already set forth above.
For at least these reasons, the 103 rejection is maintained.
Claims 11, 17, 31, 33, 36 are rejected under 35 U.S.C. 103 as being unpatentable over Anchel (WO 2016077457; IDS 07.25.25, previously cited) in view of Kitabatake et al. (1993 Food Reviews International 9(4): 445-471; previously cited), and evidenced by Daly et al. (supra) and/or Ivey et al. (supra). The teachings of Anchel over at least instant claims 11, 31, 33 are noted above.
Regarding instant claims 17, 36, Kitabatake et al. disclose that to improve the functional properties of food protein, physical and enzymatic treatments are effective and attractive (p. 445). Kitabatake et al. disclose dephosphorylated phosphoproteins is expected to improve the functionality of the protein (p. 469). Kitabatake et al. disclose treating ovalbumin by acid phosphatase (p. 469). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to dephosphorylate the rOVA produced by Pichia pastoris and incorporated as a powdered composition with starch in the consumable food product of Anchel noted above with a phosphatase as suggested in Kitabatake et al. The motivation to do so is given by Kitabatake et al., which disclose that the function of food proteins, such as ovalbumin, can be modified by enzymatic treatments, including dephosphorylation by phosphatase. One of ordinary skill would have a reasonable expectation of success because the prior art discloses that the function of food proteins can be modified by enzymes, including phosphatase.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining Anchel are the same as noted above. The deficiency of Kitabatake et al. to not teach the elements recited in the instant claims are remedied by Anchel for the reasons set forth above.
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 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 19 of U.S. Patent No. 11718644 (‘644) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘644 patent claim are drawn to a consumable composition comprising a rOVA protein. The ‘644 patent specification discloses the consumable composition comprises powder. The ‘644 patent claims recite the composition comprises a purified recombinant protein. The ‘644 patent specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘644 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘644 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘644 patent claims differ from the instant claims by not explicitly reciting that the consumable composition comprises starch and that the recombinant chicken OVA is in powdered form. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the consumable composition of the ‘644 patent claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘644 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘644 patent are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-13 of U.S. Patent No. 11518797 (‘797) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘797 patent claims are drawn to a consumable composition comprising a rOVA protein and a food additive (starch). The ‘797 patent specification discloses the food additive is starch. The ‘797 patent specification discloses the recombinant chicken OVA is in powdered form. The ‘797 patent claim 9 recites the composition comprises a recombinant ovalbumin protein. The ‘797 patent specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘797 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘797 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘797 patent claims differ from the instant claims by not explicitly reciting that the food additive is starch and that the recombinant chicken OVA is in powdered form. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the consumable composition of the ‘797 patent claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘797 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘797 patent are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15, 17-18 of U.S. Patent No. 11279748 (‘748) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘748 patent claims are drawn to a composition comprising a rOVA protein. The ‘748 patent claims 1-2 recite the composition comprises a recombinant ovalbumin protein. The ‘748 patent claims 11-12 recite that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘748 specification discloses the rOVA is chicken OVA. The ‘748 patent claim 18 recites the composition is in powdered form. Since the recombinant protein composition of the ‘748 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘748 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘748 patent claims differ from the instant claims by not explicitly reciting that the composition is a consumable composition and starch. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel into the composition of the ‘748 patent claims and modify the composition of the ‘748 patent to a consumable composition. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘748 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘748 patent are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 15-18, 22-23, 25-30, 32-53 of copending Application No. 18455552 (‘552) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘552 application claim are drawn to a consumable composition comprising a rOVA protein and a consumable ingredient. The ‘552 application specification discloses the ingredient is starch. The ‘552 application specification discloses the recombinant OVA is in powdered form. The ‘552 application claim 15 recite the composition comprises a recombinant ovalbumin protein and the ‘552 application claims 26, 36 recite that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘552 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘552 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘552 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘552 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch and the rOVA is in powdered form. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the consumable composition of the ‘552 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘552 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘552 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-30 of U.S. Patent No. 12096784 (‘784) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘784 patent claims are drawn to a consumable composition comprising a rOVA protein and an ingredient. The ‘784 patent specification discloses the rOVA protein is in powdered form. The ‘784 patent claim 21 recites the composition further comprises starch. The ‘784 patent claim 8 recites the composition comprises a recombinant ovalbumin protein. The ‘784 patent claim 16 recites that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘784 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘784 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘784 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘784 patent claims differ from the instant claims by not explicitly reciting that the rOVA is in powdered form. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate the recombinant chicken OVA in powdered form in the consumable composition of the ‘784 patent claims which comprises starch. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘784 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘784 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 33-72 of copending Application No. 18766643 (‘643) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘643 application claim are drawn to a composition comprising a rOVA protein comprising a N-glycan comprising 11 or fewer mannose units and having the same mannose units and glycosylation patterns. The ‘643 application specification also discloses the rOVA is chicken OVA. The ‘643 application claims 70-71 recite the composition is a food composition. The ‘643 application claim 58 recites the rOVA is in powdered form. The ‘643 application specification discloses ingredients for the food composition include starch and that the rOVA protein is in powdered form. The ‘643 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch and the rOVA is in powdered form in the food composition. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the food composition of the ‘643 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘643 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘643 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 48-49, 51, 54 of copending Application No. 18907140 (‘140) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘140 application claim are drawn to a consumable composition comprising a rOVA protein. The ‘140 application claims recite the composition comprises a recombinant protein. The ‘140 specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘140 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘140 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘140 application claim 48 recites the composition is in powdered form and claims 51, 54 recite the composition is a consumable composition. The ‘140 application specification discloses ingredients for the consumable compositions include starch. The ‘140 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch and the rOVA is in powdered form in the food composition. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the food composition of the ‘140 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘140 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘140 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 51-52 of copending Application No. 18903982 (‘982) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘982 application claim are drawn to a powdered/consumable composition comprising a rOVA protein. The ‘982 application specification discloses ingredients for the consumable composition include starch. The ‘982 application claims recite the composition comprises a recombinant protein. The ‘982 application specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘982 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘982 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘982 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel in the powdered composition of the ‘982 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘982 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘982 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-27, 30 of copending Application No. 19399116 (‘116) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘116 application claim are drawn to a consumable composition comprising a rOVA protein. The ‘116 application specification discloses ingredients for the consumable composition include starch. The ‘116 application claim 1 recites the composition comprises a recombinant ovalbumin protein and the ‘116 application claims 26-27 recite that the recombinant ovalbumin is produced and/or expressed by a Pichia host cell. The ‘116 application claims 11-12 recite the rOVA protein is in powdered form. The ‘116 application specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘116 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘116 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘116 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel in the powdered composition of the ‘116 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘116 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘116 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
Claims 11-13, 15-17, 19-21, 23, 25, 28, 31, 33-39, 41, 42-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of copending Application No. 18761860 (‘860) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘860 application claim are drawn to a consumable composition comprising a rOVA protein. The ‘860 application specification discloses ingredients for the consumable composition include starch. The ‘860 application specification discloses the rOVA protein in powdered form. The ‘860 application claim 1 recites the composition comprises a recombinant ovalbumin protein, claim 7 recites the recombinant ovalbumin is a chicken ovalbumin, and claims 15-16 recite that the recombinant ovalbumin is produced and/or expressed by a Pichia host cell. The ‘860 application specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘860 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘860 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. The ‘860 application claims differ from the instant claims by not explicitly reciting that the ingredient is starch and the rOVA is in powdered form in the consumable composition. However, in view of the noted teachings of Anchel noted above, it would have been obvious for one of ordinary skill to incorporate a starch as suggested in Anchel and recombinant chicken OVA in powdered form in the consumable composition of the ‘860 application claims. One of ordinary skill would have a reasonable expectation of success because Anchel discloses consumable food products comprising powdered rOVA and starch. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘860 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting over the ‘860 application are noted above. Additionally, the reasons for maintaining Anchel are the same as noted above.
No claim is allowed.
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/Marsha Tsay/Primary Examiner, Art Unit 1656
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