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 .
The Applicants’ Amendment to the Claims filed on 03/10/2026 is entered.
Election/Restrictions
Applicant's election without traverse of invention Group II (e.g., claims 15-25) in the reply filed on 03/15/2024 is as previously acknowledged.
Applicant’s election without traverse of the species of a single species of non-bacterial host cell being a Pichia pastoris cell from among Trichoderma reesei cell, a Pichia pastoris cell, and an Aspergillus niger cell in the reply filed on 03/10/2026 is acknowledged.
Claims 35 and 38 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 03/10/2026.
Claim status
Claims 14, 19-21, 24, and 31 are cancelled.
Claims 1-13, 15-18, 22-23, 25-30, and 32-53 are pending.
Claims 1-13 are withdrawn to non-elected invention group.
Claims 35 and 38 are withdrawn to non-elected species.
Claims 15-18, 22-23, 25-30, 32-34, 36-37, and 39-53 are under examination in this office action.
Response to Amendment
The rejection of claims 15, 16-18, 21, 22-23, 24-26, and 32-34 under 35 U.S.C. 103 as being unpatentable over Berry (WO 2013/148330) is withdrawn in view of the Applicants’ Amendment to the Claims filed on 11/07/2025.
The rejection of claims 27-30 under 35 U.S.C. 103 as being unpatentable over Berry (WO 2013/148330) in view of Rodriguez (US2015/0313269) is withdrawn in view of the Applicants’ Amendment to the Claims filed on 11/07/2025.
The NSDP rejections over US Patent 11,518,797 (
The provisional NSDP rejections over US Applications 18/296,654, 17/508,064, 18/336,915, and 18/045,422, each in view of Berry et al, are withdrawn in view of the Applicants’ Amendment to the Claims filed on 11/07/2025.
Priority
This US18/455,552 is a CON of 18/047,953 filed on 10/19/2022 which is a CON of 15/522,986 filed on 04/28/2017 (now US Patent 11,518,797) which is a 371 of PCT/US15/60147 filed on 11/11/2015 which claims US priority benefit of 62/078,385 filed on 11/11/2014. The Filing receipt filed on 11/21/2023 is controlling.
Information Disclosure Statement
The IDS filed on 11/07/2025 has been considered by the examiner.
Claim Objections
Claim 18 is objected to because of the following informalities: Claim 18 appears to intend: …of claim 15, wherein the recombinantly-produced…. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 28 and 30 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. This is a new ground of rejection necessitated by amendment.
Specifically, claim 28 does not further limit the subject matter of claim 27. Claim 27 requires that the recombinantly-produced avian ovalbumin has at least 95% sequence identity to SEQ ID NO: 1 whereas claim 28 requires that the recombinantly-produced avian ovalbumin has a sequence with at least 97% sequence identity to SEQ ID NO: 1. Note that an ovalbumin having 95% sequence identity to SEQ ID NO: 1 would necessarily have a sequence with at least 97% sequence identity to SEQ ID NO: 1. A sequence is construed to encompass an amino acid sequence of only two amino acids.
Further, claim 30 does not further limit or fails to include all the limitations of claim 27. Claim 30 recites the recombinantly-produced avian ovalbumin has a glycosylation or acetylation pattern different from the corresponding naturally-occurring avian egg protein. However, base claim 27 requires a glycosylation pattern difference. Claim 30 recites the glycosylation pattern difference in the alternative with an acetylation pattern difference.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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.
New claims 49-50 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. This is a new ground of rejection necessitated by amendment.
Claims 49-50 are indefinite because they each recite the term “purified to a level such that the recombinantly-produced avian ovalbumin is able to replace the functional performance and the physical characteristics of a number of proteins of naturally-occurring egg white in the consumable food product”. The term “purified to a level” is a relative term which renders the claim indefinite. The term “purified to a level” is not defined by the claim other than by functional language, 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.
In addition, claims 49 and 50 each recite the limitation "the functional performance and the physical characteristics of a number of proteins of naturally-occurring egg white in the consumable food product" in lines 4-5. There is insufficient antecedent basis for this limitation in the claim because there is no prior reference in the claims to a functional performance and physical characteristics of a number of proteins of naturally-occurring egg white in the consumable food product. Further, claims 49-50 are indefinite because the claim language “such that the recombinantly-produced avian ovalbumin is able to replace the functional performance and the physical characteristics of a number of proteins of naturally-occurring egg white in the consumable food product” appears to require “a number of proteins of naturally-occurring egg white in the consumable food product” but the claims depend from base claims 15 or 27 which only require “one or more” egg white proteins”.
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 15-18, 22-23, 25-30, 32-34, 36-37, and 39-53 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This rejection is a NEW MATTER rejection. This is a new rejection necessitated by Applicant's amendment.
The specification as originally filed does not provide support for the invention as now claimed: Regarding base claims 15 and 27, and dependent claims therefrom, while the specification supports an embodiment where the recombinant ovalbumin has a glycosylation pattern or phosphorylation that is different from a non-recombinantly-produced avian egg white protein, support cannot be found for the present claim amendment: “wherein the recombinantly-produced ovalbumin comprises a glycosylation pattern that is different from a non-recombinantly-produced avian egg white protein and comprises a difference in phosphorylation from a non- recombinantly-produced avian egg white protein.” The specification does not provide sufficient blazemarks nor direction for the instant egg white proteins encompassed by the above-mentioned limitations. The instant claims now recite limitations, which were not clearly disclosed in the specification as filed, and now change the scope of the instant disclosure as filed. Such limitations recited in the present claims, which did not appear in the specification as filed, introduce new concepts and violate the description requirement of the first paragraph of 35 U.S.C. 112. Applicants point to claims as filed to show support but neither the Specification nor claims as filed show the scope of requiring both glycosylation and phosphorylation differences as presently claimed.
Claim Rejections - 35 USC § 103 – new grounds necessitated by amendment
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.
Currently amended claims 15, 16-18, 22-23, 25-26, 27, 28, 29-30, 32-34, 36-37, 39, 42, 45-50, and 51-53 are rejected under 35 U.S.C. 103 as being unpatentable over Berry (WO 2013/148330, published 10/3/2013, of record; as evidenced by the Score result 1 & 2 to Berry et al, of record), in view of Bretthauer et al in “Glycosylation of Pichia pastoris-derived proteins” (Biotechnol Appl Biochem 1999 Vol 30, pages 193-200), in further view of Ito et al in “Structural Characteristics of Hen Egg Ovalbumin Expressed in Yeast Pichia pastor Bioscience, Biotechnology, and Biochemistry, Volume 69, Issue 4, 1 January 2005, Pages 755–761).
Further, regarding claims 15 and 27, Berry et al disclose that the consumable food composition is a food product. (See para 241-243). Berry et al disclose their nutritive food product compositions comprise ovalbumin which is an egg white protein. For example, Berry et al explicitly disclose making recombinant proteins in Pichia pastoris (for example, page 72, line 24; page 76, line 6) and recite ovalbumin, ovotransferrin, and ovomucoid as preferred types of nutritive proteins for food/consumable compositions (e.g., para 0091). Further, regarding amended base claims 15 and 27, Berry et al disclose that the nutritive recombinant proteins have a glycosylation pattern different from the corresponding naturally occurring egg white protein (Page 49: para 144, lines 1-8). For example, Berry et al recite that in “some embodiments the first polypeptide sequence does not comprise N-linked glycosylation” and that in “some embodiments the first polypeptide sequence does not comprise O-linked glycosylation (Para 0019; 00144).
Further, regarding claims 15 and 27, Berry et al discloses that recombinant nutritive proteins of the invention are glycosylated. (See para 0144).
[00144] In other embodiments, the nutritive protein according to the disclosure is produced with low or no glycosylation by a host organism. Most bacteria and other prokaryotes have very limited capabilities to glycosylate proteins, especially heterologous proteins. Accordingly, in some embodiments of this disclosure a nutritive protein is made recombinantly in a microorganism such that the level of glycosylation of the recombinant protein is low or no glycosylation. In some embodiments the level of glycosylation of the recombinant nutritive protein is lower than the level of glycosylation of the protein as it occurs in the organism from which it is derived.
Further, regarding claims 15, 22-23, 26, 27, 36-37, 39, 42, and 51-53, Berry et al discloses an egg white protein composition comprising: a recombinantly-produced avian ovalbumin secreted from a non-bacterial host cell; and a first consumable ingredient. Note that the phrase in the preamble for replacing naturally-occurring egg white proteins in a consumable food product is construed as an intended use for the claimed product composition.
Berry et al disclose a method of making processed, consumable food compositions comprising chicken egg white proteins including ovalbumin, ovotransferrin, and ovomucoid. Berry recite ovalbumin, ovotransferrin, and ovomucoid as preferred types of nutritive proteins for food/consumable compositions (See para 0091). Berry et al specifically disclose protein compositions. Regarding new claims 26, 36-37, and 39, Berry explicitly discloses making recombinant proteins in Pichia pastoris (See page 72, line 24; page 76, line 6) which is a non-bacterial host cell. Berry recite ovalbumin, ovotransferrin, and ovomucoid as preferred types of nutritive proteins for food/consumable compositions (See para 0091). Berry disclose that it was well-known in the art that host cells may secrete their recombinant proteins of interest (See page 78, lines 25-27; para 194). For example, and further regarding claims 22-23,and 42, in paragraph 0091 Berry et al recites the nutritive protein is “an abundant protein in food”, and further states in para 0091, line 6-8” that “the abundant protein in food is selected from chicken egg proteins such as ovalbumin, ovotransferrin, and ovomucoid” (e.g. para 0091, lines 1-8). Berry et al disclose consumable nutritive food compositions, comprising recombinantly expressed and secreted nutritive proteins from a host cell (Page 78, para 194). For example, Berry et al recite:
Skilled artisans are aware of many suitable methods available for culturing recombinant cells to produce (an optionally secrete) a recombinant nutritive protein as disclosed herein, as well as for purification and/or isolation of expressed recombinant proteins. (Page 78, para 194).
Berry et al discloses that the nutritive proteins, including chicken egg white proteins may be recombinantly expressed in a non-animal host cell. (Paragraphs 0091, lines 1-8; paragraphs 192,194, and 195). For example, Berry et al disclose that a Pichia pastoris cell is a type of heterotroph host microorganism that may be used to “produce a recombinant nutritive protein disclosed herein”. (Page 72: para 0027 (lines 1-3 & para 0028 (line 9). Berry et al disclose that the host cell may be a yeast cell. For example, Berry teach nutritional egg white compositions and suggests using recombinant proteins made in yeast including Pichia pastoris. Berry explicitly discloses making recombinant proteins in Pichia pastoris (See page 72, line 24; page 76, line 6). Berry disclose that it was well-known in the art that host cells may secrete their recombinant proteins of interest (See page 78, lines 25-27; para 194).
Further, regarding claims 51-53, the term kit is construed to read on a composition or collection and the phrase for replacing all or a portion of the naturally-occurring egg white protein in the consumable food product, is construed as intended use language. Also, the limitation of instructions specifying how to adjust an amount of recombinantly-produced avian ovalbumin to match the total protein content of the naturally-occurring egg white so that it replaces all or a portion of the naturally-occurring egg white protein in the consumable food product is not generally afforded patentable weight for purpose of applying prior art. Note that the phrase “for replacing all or a portion of the naturally-occurring egg white protein in the consumable food product” is construed as an intended use phrase. Generally, intended use does not bear patentable weight when applying prior art to the claims. Also, note that a recitation of intended use, as taught in the notice of use, is accorded patentable weight only to the extent that it limits the actual components of a kit; in the instant case the intended use does not affect the components in any way which distinguishes over the subject matter taught or suggested by the reference. The printed matter in no way depends on the kit, and the kit components in no way depend on the printed matter. All the printed matter does is teach a use for an existing product. As pointed out in In re Gulack 703 F2d 1381 (Fed Cir.1983), "[w]here the printed matter is not functionally related to the substrate, the printed matter will not distinguish the invention from the prior art in terms of patentability."
Regarding claims 16-18, 27, 28 and 32-34, Berry et al disclose the sequence for ovalbumin is a 100% identical sequence match for instant SEQ ID NO: 1. (See Score result 1 & 2 for Berry et al showing Berry et al SEQ ID NO:2610; of record). This amino acid sequence for ovalbumin of Berry et al is 386 amino acids. Note that claim 32 is met by 386 amino acids because claim 32 recites 385 amino acid using the open claim language: comprising. Regarding claim 16, note that “a sequence” is construed to encompass an amino acid sequence of only two amino acids. Regarding claim 17, note that “a sequence” is construed to encompass an amino acid sequence of only two amino acids. Regarding claim 18, note that “a sequence” is construed to encompass an amino acid sequence of only two amino acids. Regarding claim 28, note that “a sequence” is construed to encompass an amino acid sequence of only two amino acids.
Berry et al discloses that the first recombinant avian egg protein comprises ovalbumin having the amino acid sequence of in SEQ ID NO:1 which is not distinguished from the structure of the present claims. It is generally considered that a product is not separable from its properties. Thus, it is considered that the Berry et al consumable food product comprising the same ovalbumin protein of the present claims would possess the same properties as a processing agent or antimicrobial.
Regarding new claims 45-50, the limitations of functional performance and physical characteristics of native egg white regarding being an egg white replacement, it is noted that it is generally considered that a product is not separable from its properties. Berry et al disclose the sequence for ovalbumin is a 100% identical sequence match for instant SEQ ID NO: 1 of the present claims. (See attached Score result 1 & 2 for Berry et al showing Berry et al SEQ ID NO:2610; of record). This amino acid sequence for ovalbumin of Berry et al is 386 amino acids which reads on the structure of the present claims. Further, regarding the second egg white protein, Berry recite ovalbumin, ovotransferrin, and ovomucoid as preferred types of nutritive proteins for food/consumable compositions (See para 0091). The limitations of “egg replacement” and providing function and physical characteristics of native egg white is construed to be met by a composition of such preferred proteins for food/consumable compositions. The concept of a nutritive food composition meets the limitation of an egg replacement and the limitation of providing function and physical characteristics of native egg white. Thus, absent evidence to the contrary, it is considered that prior art that meets the structural limitations of a product meet the functional limitations as well.
Regarding claims 49-50, Berry et al discloses the egg white protein composition is for food composition and thus is construed to meet the limitation that it is able to replace the functional performance and the physical characteristics of a number of proteins of naturally-occurring egg white in the consumable food product.
The level of skill in the art was high before the effective filing date of the presently claimed invention.
One of ordinary skill in the art would have been motivated to combine the elements of a recombinant ovalbumin together with additional recombinant egg white proteins such as ovaltransferrin, and ovomucoid egg white proteins in a nutritive food composition for the rationale of making a nutritive consumable food composition appealing for human consumption. Further, one of ordinary skill in the art would have been motivated to make such recombination proteins by secreting the proteins from host cells include Pichia pastoris host cells for the rationale of reducing antigenicity, efficiency and cost savings. It would have been obvious to one of ordinary skill in the art to do such because Berry et al suggests combinations of ovalbumin, ovaltransferrin, and ovomucoid egg white proteins in a nutritive food composition as a preferred embodiment. Berry explicitly disclose sequences for expressing such recombinant ovalbumin and additional recombinant egg white proteins in host cells including the sequence for ovalbumin which is a 100% identical sequence match for instant SEQ ID NO: 1.
However, Berry et al differs from the present claims because it does not disclose the combination of glycosylation and phosphorylation differences as presently claimed. Further, specifically regarding claims 25 and 30, Berry et al does not disclose that the ovalbumin has an acetylation pattern different from the corresponding naturally-occurring avian egg white protein. Also, regarding claim 29, Berry et al does not disclose that the recombinantly-produced avian ovalbumin has an increase in glycosylation as compared to animal-derived ovalbumin.
Bretthauer et al disclose that the “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. Bretthauer et al reviews the current state of knowledge of glycosylation of proteins in this methylotrophic yeast. Further, Bretthauer et al disclose that recombinant proteins expressed in Pichia pastoris inherently have different glycosylation patterns compared to non-recombinant proteins and also inherently have a difference in phosphorylation from non-recombinant proteins. In addition, Ito et al discloses that hen egg ovalbumin recombinantly produced in yeast Pichia pastoris has a different glycosylation pattern, phosphorylation pattern, and acetylation pattern compared to non-recombinant ovalbumin. (See Abstract; entire article.) Specifically, Ito et al disclose an increased glycosylation pattern in the ovalbumin expressed in Pichia pastoris, specifying that the additional glycosylation to Asn-311 in the recombinant protein does not affect protein conformation or thermostability. (See Abstract; entire article).
In view of the high skill in the art before the effective filing date of the presently claimed invention it is considered that it would have been obvious to one of ordinary skill in the art to use Pichia pastoris as the type of fungal host cell to express the rOVA for a food product composition.
One would have been motivated to do such for the rational of Bretthauer et al that “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Bretthauer et al suggest another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. In view of Ito et al, it was known in the art that expression of hen ovalbumin in Pichia pastoris inherently yields recombinant OVA having different glycosylation, acetylation and phosphorylation patterns than native hen ovalbumin.
In view of the high skill in the art it is considered that one would have had a reasonable expectation of success to combine the elements of the combination of cited references with the fungal host cell Pichia pastoris to arrive at the present claims.
Response to Arguments
The Applicants’ response filed on 11/07/2025 has been fully considered and is addressed here as it may relate to this new ground of rejection.
The applicants state that the rejection of claims 15-18, 21-26, and 32-34 over Berry et al and of claims 27-30 over Berry et al in view of Rodriguez are overcome by the present amendments. The argument that the newly added limitation to the base claims that require the combination of glycosylation and phosphorylation differences as presently claimed is not suggested in Berry et al is persuasive. However, the new ground of rejection includes the references of Bretthauer et al in “Glycosylation of Pichia pastoris-derived proteins” (Biotechnol Appl Biochem 1999 Vol 30, pages 193-200), in further view of Ito et al in “Structural Characteristics of Hen Egg Ovalbumin Expressed in Yeast Pichia pastor Bioscience, Biotechnology, and Biochemistry, Volume 69, Issue 4, 1 January 2005, Pages 755–761) which address the new limitation require the combination of glycosylation and phosphorylation differences as presently claimed as recited in the body of the rejection above.
Double Patenting – new grounds necessitated by amendment
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 15, 22-23, 26, 36, and 45-46 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 11,279,748 in view of Bretthauer et al in “Glycosylation of Pichia pastoris-derived proteins” (Biotechnol Appl Biochem 1999 Vol 30, pages 193-200), in further view of Ito et al in “Structural Characteristics of Hen Egg Ovalbumin Expressed in Yeast Pichia pastor Bioscience, Biotechnology, and Biochemistry, Volume 69, Issue 4, 1 January 2005, Pages 755–761).
Although the claims at issue are not identical, they are not patentably distinct from each other because the combination of patented claims in view of Bretthauer et al and Ito et al render obvious the instant claims.
Regarding instant claims 15, and 22-23, patented claims 1-2 recite an animal-free egg white composition where the proteins are a recombinantly-produced ovalbumin, ovotransferrin, and lysozyme. (Patented claim 2 also has ovomucoid in the composition). Further, patented claims 10-12 recites the recombinant egg white proteins are secreted from Pichia pastoris yeast cells which meets the limitation of a non-bacterial host cell. Also, patented claim 13 recites that the composition is packaged as a ready-made egg white which is construed to meet the limitation of a consumable food product. Further, patented claim 15 recites that the glycosylation pattern of one or more recombinant proteins is different from animal-derived proteins.
Regarding instant claims 26 and 36, patented claim 12 recites Pichia pastoris host cell.
Regarding instant claims 45-46, patented claim 1 recites the composition resembles animal-derived egg white in consistency, taste, and appearance.
However, patented claims differ because they do not recite that the rOVA has a different glycosylation, and phosphorylation pattern from native OVA.
Bretthauer et al disclose that the “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. Bretthauer et al reviews the current state of knowledge of glycosylation of proteins in this methylotrophic yeast. Further, Bretthauer et al disclose that recombinant proteins expressed in Pichia pastoris inherently have different glycosylation patterns compared to non-recombinant proteins and also inherently have a difference in phosphorylation from non-recombinant proteins. In addition, Ito et al discloses that hen egg ovalbumin recombinantly produced in yeast Pichia pastoris has a different glycosylation pattern, phosphorylation pattern, and acetylation pattern compared to non-recombinant ovalbumin. (See Abstract; entire article.) Specifically, Ito et al disclose an increased glycosylation pattern in the ovalbumin expressed in Pichia pastoris, specifying that the additional glycosylation to Asn-311 in the recombinant protein does not affect protein conformation or thermostability. (See Abstract; entire article).
In view of the high skill in the art before the effective filing date of the presently claimed invention it is considered that one of ordinary skill in the art would have been motivated to use Pichia pastoris as the type of fungal host cell to express the rOVA for a food product composition. One would have been motivated to do such for the rational of Bretthauer et al that “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Bretthauer et al suggest another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. In view of Ito et al, it was known in the art that expression of hen ovalbumin in Pichia pastoris inherently yields recombinant OVA having different glycosylation, acetylation and phosphorylation patterns.
In view of the high skill in the art it is considered that one would have had a reasonable expectation of success to combine the elements of the patented claims with the fungal host cell Pichia pastoris to arrive at the present claims.
Claims 15-18, 25-30, 36-37, 39, and 45-48 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of U.S. Patent No. 12,096,784 in view of Bretthauer et al (above), in further view of Ito et al (above).
Although the claims are not identical the combination of copending claims and references of Bretthauer et al Ito et al render obvious the instant claims.
Regarding instant base claims 15, 25-26, 29-30, 36-37, 39 patented claim 9 recites a composition for a food product comprising a recombinant ovalbumin protein and an additional consumable ingredient where the rOVA has a glycosylation, acetylation, or phosphorylation pattern different from wildtype OVA. Patented claim 14 recites avian rOVA. Patented claims 15-17 recites expression from yeast, or fungal host cells which meets the limitation of a non-bacterial host cell. Patented claim 16 recites a Pichia species yeast host cell.
Regarding instant claims 16-18 and 27-28, patented claim 2 recite SEQ ID Nos which are the same sequences as the instant SEQ ID Nos for ovalbumin comprising SEQ ID NO:1.
Regarding instant claims 45-48, patented claims 23 and 25 recite characteristics equivalent or better than a similar food product from natural egg, including stability, clarity, foam capacity, and gelling.
However, patented claims differ because they do not recite that the rOVA has a different glycosylation, and phosphorylation pattern from native OVA.
Bretthauer et al disclose that the “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. Bretthauer et al reviews the current state of knowledge of glycosylation of proteins in this methylotrophic yeast. Further, Bretthauer et al disclose that recombinant proteins expressed in Pichia pastoris inherently have different glycosylation patterns compared to non-recombinant proteins and also inherently have a difference in phosphorylation from non-recombinant proteins. In addition, Ito et al discloses that hen egg ovalbumin recombinantly produced in yeast Pichia pastoris has a different glycosylation pattern, phosphorylation pattern, and acetylation pattern compared to non-recombinant ovalbumin. (See Abstract; entire article.) Specifically, Ito et al disclose an increased glycosylation pattern in the ovalbumin expressed in Pichia pastoris, specifying that the additional glycosylation to Asn-311 in the recombinant protein does not affect protein conformation or thermostability. (See Abstract; entire article).
In view of the high skill in the art before the effective filing date of the presently claimed invention it is considered that one of ordinary skill in the art would have been motivated to use Pichia pastoris as the type of fungal host cell to express the rOVA for a food product composition. One would have been motivated to do such for the rational of Bretthauer et al that “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Bretthauer et al suggest another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. In view of Ito et al, it was known in the art that expression of hen ovalbumin in Pichia pastoris inherently yields recombinant OVA having different glycosylation, acetylation and phosphorylation patterns.
In view of the high skill in the art it is considered that one would have had a reasonable expectation of success to combine the elements of the patented claims with the fungal host cell Pichia pastoris to arrive at the present claims.
Currently amended claims 15-18, 22-23, 25-30, 36-37, and 39 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. US 11,518,797 in view of Bretthauer et al (above), in further view of Ito et al (above).
Although the claims are not identical the combination of copending claims and references of Bretthauer et al Ito et al render obvious the instant claims.
Regarding instant base claims 15, 25-26, 27, and 29-30, 36-37, and 39, patented claims 13 and 16 recite a processed consumable product composition or method of making such, the composition comprising a recombinant ovalbumin protein and an additional consumable ingredient where the rOVA has a glycosylation or phosphorylation pattern or acetylation pattern different from wildtype OVA. Patented claim 14 recites avian rOVA. Patented claim 3 recites a yeast or fungal cell which meets the limitation of a non-bacterial host cell. Patented claim 4 recites a Pichia species yeast host cell. Patented claims 1 and 18 recite a food product.
Regarding instant claims 16-18 and 27-28, patented claims recite SEQ ID Nos which are the same sequences as the instant SEQ ID Nos. (i.e., ovalbumin comprising SEQ ID NO:1).
Regarding instant claims 22-23, patented claims, including patented claim 9, recite a second avian egg white protein, including lysozyme.
However, patented claims differ because they do not recite that the rOVA has a different glycosylation, and phosphorylation pattern from native OVA.
Bretthauer et al disclose that the “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. Bretthauer et al reviews the current state of knowledge of glycosylation of proteins in this methylotrophic yeast. Further, Bretthauer et al disclose that recombinant proteins expressed in Pichia pastoris inherently have different glycosylation patterns compared to non-recombinant proteins and also inherently have a difference in phosphorylation from non-recombinant proteins. In addition, Ito et al discloses that hen egg ovalbumin recombinantly produced in yeast Pichia pastoris has a different glycosylation pattern, phosphorylation pattern, and acetylation pattern compared to non-recombinant ovalbumin. (See Abstract; entire article.) Specifically, Ito et al disclose an increased glycosylation pattern in the ovalbumin expressed in Pichia pastoris, specifying that the additional glycosylation to Asn-311 in the recombinant protein does not affect protein conformation or thermostability. (See Abstract; entire article).
In view of the high skill in the art before the effective filing date of the presently claimed invention it is considered that one of ordinary skill in the art would have been motivated to use Pichia pastoris as the type of fungal host cell to express the rOVA for a food product composition. One would have been motivated to do such for the rational of Bretthauer et al that “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Bretthauer et al suggest another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. In view of Ito et al, it was known in the art that expression of hen ovalbumin in Pichia pastoris inherently yields recombinant OVA having different glycosylation, acetylation and phosphorylation patterns.
In view of the high skill in the art it is considered that one would have had a reasonable expectation of success to combine the elements of the patented claims with the fungal host cell Pichia pastoris to arrive at the present claims.
Claims 15, 25-26, 36, 39, and 45-46 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 33-72 of copending Application No. 18/766,643 in view of Bretthauer et al (above), in further view of Ito et al (above).
Although the claims are not identical the combination of copending claims and references of Bretthauer et al Ito et al render obvious the instant claims.
Regarding instant claims 15, 25-26, 36, 39, and 45-46, copending claim 70 recites a food product comprising a recombinant ovalbumin composition. Copending claim 40 recites that the rOVA has a different glycosylation, acetylation, or phosphorylation pattern from native OVA. Copending claims 45 recites the composition has improved qualities such as foaming, gelling, binding functions. Copending claim 67 recite that the rOVA is expressed by a fungal host which meets the limitation of a non-bacterial host.
However, copending claims differ because they do not recite that the rOVA has a different glycosylation, and phosphorylation pattern from native OVA.
Bretthauer et al disclose that the “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. Bretthauer et al reviews the current state of knowledge of glycosylation of proteins in this methylotrophic yeast. Further, Bretthauer et al disclose that recombinant proteins expressed in Pichia pastoris inherently have different glycosylation patterns compared to non-recombinant proteins and also inherently have a difference in phosphorylation from non-recombinant proteins. In addition, Ito et al discloses that hen egg ovalbumin recombinantly produced in yeast Pichia pastoris has a different glycosylation pattern, phosphorylation pattern, and acetylation pattern compared to non-recombinant ovalbumin. (See Abstract; entire article.) Specifically, Ito et al disclose an increased glycosylation pattern in the ovalbumin expressed in Pichia pastoris, specifying that the additional glycosylation to Asn-311 in the recombinant protein does not affect protein conformation or thermostability. (See Abstract; entire article).
In view of the high skill in the art before the effective filing date of the presently claimed invention it is considered that one of ordinary skill in the art would have been motivated to use Pichia pastoris as the type of fungal host cell to express the rOVA for a food product composition. One would have been motivated to do such for the rational of Bretthauer et al that “Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermenters”. Bretthauer et al suggest another advantage of this system centers on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. In view of Ito et al, it was known in the art that expression of hen ovalbumin in Pichia pastoris inherently yields recombinant OVA having different glycosylation, acetylation and phosphorylation patterns.
In view of the high skill in the art it is considered that one would have had a reasonable expectation of success to combine the elements of the copending claims with the fungal host cell Pichia pastoris to arrive at the present claims.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments to NSDP rejection(s)
The Applicants’ response filed on 11/07/2025 has been fully considered but is unpersuasive. The applicants submit that filing a Terminal Disclaimer will be considered but provide no reasoning why the NSDP rejections over U.S. Patent Nos. 11,718,644 and 11,279,748 are improper. In view of present claim amendments, the NSDP rejection over US Patent 11,718,644 is withdrawn. The rejection over 11,279,748 is updated for amendment and maintained.
Conclusion
No claims allowed.
Related prior art which may be applied in a future office action if appropriate:
Aro et al (Food Research International 2023 Vol 163 112131).
D’ Silva (PhD Dissertation, University of Guelph, 2010; IDS reference);
Basu et al (CA 2892021 pub 5/30/2014, IDS ref, equivalent of WO2014/081884 A9 published 05/30/2014; IDS ref).
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
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/CATHERINE S HIBBERT/Primary Examiner, Art Unit 1658
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