DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
Applicant’s claim to priority from US provisional Applications 61/973,181 filed 03/31/2014 and 62/058,230 filed 10/01/2014, as well as from PCT/US2015/023679 filed 03/31/2015, is hereby acknowledged.
Application Status
Claim 1 is cancelled. Claims 2-21 are pending. Claims 10-19 are withdrawn. Therefore, claims 2-9 and 20-21 are under examination in this office action.
Applicant’s arguments have been thoroughly reviewed, but are not persuasive to place the claims in condition for allowance for the reasons that follow.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 03/20/2026 was filed after the mailing date of the office action on 12/23/2025. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
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The following rejections are maintained from the Office Action dated 12/23/2025:
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or non-obviousness.
This application currently names joint inventors. In considering patentability of the
claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim 2 is rejected under 35 U.S.C. § 103 as being unpatentable over Elrod (Elrod, S.L. et al. US 6,261,827 B1; published Jul. 17, 2001; previously cited) and Kwon (Kwon, S.J. et al. “High-level production of porphyrins in metabolically engineered Escherichia coli: Systematic extension of a pathway assembled from overexpressed genes involved in heme biosynthesis” Applied and Environmental Microbiology, Vol. 69, No. 8 (2003), pp: 4875-4883).
Regarding claim 2, Elrod teaches a recombinant yeast cell, expressing one or more heme biosynthetic enzymes and a hemoprotein (see abstract). Elrod teaches that the hemoprotein may be a globin (see column 3, lines 63-64).
Elrod teaches that the recombinant yeast may overexpress an endogenous (i.e. yeast) first nucleic acid encoding a 5-aminolevulinic acid synthase, a porphobilinogen synthase, a porphobilinogen deaminase, an uroporphyrinogen synthase, an uroporphyrinogen decarboxylase, a coporphyrinogen oxidase, a protoporphyrinogen oxidase and a ferrochelatase (see column 5, lines 26-36).
Elrod also teaches that the recombinant yeast may overexpress one or more second nucleic acids encoding a 5-aminolevulinic acid synthase, a porphobilinogen synthase, a porphobilinogen deaminase, an uroporphyrinogen synthase, an uroporphyrinogen decarboxylase, a coporphyrinogen oxidase, a protoporphyrinogen oxidase and a ferrochelatase (see column 7,lines 41-52).
Elrod also teaches that the nucleic acids encoding the recombinant heme biosynthesis enzymes are stably integrated into the recombinant yeast (see column 4, lines 39-45). Elrod teaches “at least one” or “one or more” heme biosynthesis enzymes to be overexpressed in the recombinant yeast.
Elrod also teaches that “when a nucleic acid sequence encoding one of the enzymes in the heme biosynthetic pathway is introduced into a filamentous fungal cell, one or more pathway intermediates in one or more preceding steps may become rate-limiting (see column 11, lines 10-14).
Elrod does not teach eight genes encoding eight recombinant heme biosynthesis enzymes integrated into a recombinant yeast cell.
However, Kwon teaches expression of eight genes involved in heme biosynthetic pathways in different combinations and up to seven simultaneously, in a recombinant Escherichia coli (E.coli) cell (see title and Tables 1 and 2).
Kwon teaches at first expression of five genes (hemA (ALAS), hemB (porphobilinogen synthase; ALA dehydratase), hemC (hydroxymethylbilane synthase; porphobilinogen deaminase), hemD (uroporphyrinogen III synthase) and hemE (uroporphyrinogen decarboxylase) (see page 4879, left column, first paragraph). Kwon teaches that the assembled heme pathway expressed in a recombinant E.coli, accumulated large amounts of porphyrins in the culture medium, with partial precipitation of porphyrins (same paragraph).
Kwon teaches systematic extension of the engineered heme biosynthetic pathway, adding hemF (oxygen-dependent coproporphyrinogen III oxidase), hemY (protoporphyrinogen oxidase or coproporphyrinogen oxidase) and hemH (ferrochelatase heme synthase) (see page 4880, left column).
Kwon teaches that the production level of porphyrins increased from 40% with overexpression of hemA alone or with hemB, to an additional 2 to 7 fold increase with overexpression of hemC and hemD. When adding hemABC with hemE, there was no observed change in production, however when adding hemF, there was an additional 70 to 80% increase in production of porphyrins. Although adding hemH to hemABCDEF did not significantly change the production/accumulation of heme, Kwon teaches expression of these seven genes simultaneously in E.coli (see pages 4880-4881, “Production levels” section). Kwon also teaches expression of hemABCDEFY simultaneously in E.coli (see Figure 2).
Kwon teaches optimization of the system, and also the development of a versatile system for tailored (over)production of major porphyrins that occur as intermediates in heme biosynthesis (see page 4881, left column, “Discussion” section).
It would have been obvious to one having ordinary skills in the art before the effective filing date of the claimed invention to have modified Elrod and introduced the eight genes HemABCDEFHY simultaneously in a cell and obtained eight stably integrated genes into the genome of a recombinant yeast to optimize production of a heme-containing protein. Since Kwon teaches that it is feasible to overexpress HemABCDEFY and HemABCDEFH simultaneously in two different recombinant E. coli, one with ordinary skills in the art could have also express HemABCDEFHY in the same cells. Since each one of the heme biosynthesis enzyme could be rate-limiting for the overexpression of a heme-containing protein, one motivated in optimizing a yeast system for overexpression of a heme-containing protein could have performed modifications to a system through routine optimization and trials as taught by Kwon, and introduced up to eight rate-limiting enzymes into a recombinant yeast.
Since the claimed invention is merely a combination of old elements, and in the combination each element merely would have performed the same function as it did separately, one of ordinary skill in the art would have recognized that the results of the combination were predictable. KSR, 127 S.Ct. at 1740, 82 USPQ2d at 1396.
Claims 5, 6 and 7 are rejected under 35 U.S.C. § 103 as being unpatentable over Elrod (Elrod, S.L. et al. US 6,261,827 B1; published Jul. 17, 2001; previously cited) and Kwon (Kwon, S.J. et al. “High-level production of porphyrins in metabolically engineered Escherichia coli: Systematic extension of a pathway assembled from overexpressed genes involved in heme biosynthesis” Applied and Environmental Microbiology, Vol. 69, No. 8 (2003), pp: 4875-4883), as applied to claims 2 above, and in further view of Brown (Brown, P. et al. WO 2013/010042 A1; published Jan. 17, 2013; previously cited).
It is noted that the combination Elrod/Kwon renders elements of claim 2 obvious. The rejection of claim 2 is described above.
Regarding claim 5, Elrod teaches that the heme-containing protein may be a myoglobin (see column 3, lines 65-66). Elrod teaches a myoglobin as the heme-containing protein (column 3, line 66), however, Elrod does not teach a mammalian myoglobin.
Elrod does not specifically teach a mammalian myoglobin. However, Elrod teaches genes from different sources: Saccharomyces cerevisiae, Escherichia coli, Bacillus subtilis, Aspergillus nidulans, Rhodobacter capsulans, Bovine or Human sources for enzymes in the heme metabolic pathways (see column 8). Elrod teaches that the hemoprotein can be native to the filamentous fungal cell (see column 74, claim 17) or can be foreign to the filamentous fungal cell (see column 75, claim 18).
Brown also teaches an animal-source of myoglobin ( see ¶ [0051]-[0052]) that can be expressed in a non-animal source such as a yeast or bacteria (¶ [00140], [00142], [00223]-[00224]). Brown teaches an equine heart muscle myoglobin (see ¶ [00258]).
It would have been obvious to one with ordinary skills in the art before the effective filing date of the claimed invention to substitute a myoglobin protein from a fungal source taught by Elrod to a myoglobin protein from a mammal source as taught by Brown. Both proteins have the same function in the system. One motivated in overproducing a mammal protein for use in a mammalian animal model or cell system, could have performed this substitution with a reasonable expectation of success, and arrived at the claimed invention.
Regarding claims 6 and 7, the combination Elrod/Kwon teaches the elements of claim 2, however Elrod does not teach the recombinant expression of leghemoglobin, wherein the leghemoglobin is from Glycine max, as in claims 6 and 7.
Elrod does not teach a mammalian myoglobin nor a leghemoglobin from Glycine max.
However, Brown teaches the recombinant expression of Soybean (Glycine max) leghemoglobin in a genetically modified yeast or bacteria as a non-animal source of isolated leghemoglobin protein (see ¶ [00223]-[00224], [00261], [00378], [00381]).
In KSR Int 'l v. Teleflex, the Supreme Court, indicated that “The principles underlying [earlier] cases are instructive when the question is whether a patent claiming the combination of elements of prior art is obvious. When a work is available in one field of endeavor, design incentives and other market forces can prompt variations of it, either in the same field or a different one. If a person of ordinary skill can implement a predictable variation, § 103 likely bars its patentability.” KSR Int'l v. Teleflex lnc., 127 S. Ct. 1727, 1740 (2007).
Applying the KSR standard of obviousness to Elrod/Kwon and Brown, it is concluded that the combination of the references represents a combination of known elements which yield the predictable result. At the time of invention, a practitioner could have combined the teachings of Elrod of expressing multiple heme biosynthesis enzymes in a recombinant yeast cell, together with a heme-containing protein, with teachings of Brown, using a Glycine max leghemoglobin as the heme-containing protein or a mammalian myoglobin. As a result, the predictable result of designing a genetically modified yeast expressing at least eight heme biosynthesis enzymes gene, overexpressing a heme-containing protein, i.e. a Glycine max leghemoglobin or a mammalian myoglobin, would be achieved. Such a combination is merely a "predictable use of prior art elements according to their established functions." KSR Int’l 7, 127 S. Ct. at 1740.
Claim 20 is rejected under 35 U.S.C. § 103 as being unpatentable over Elrod (Elrod, S.L. et al. US 6,261,827 B1; published Jul. 17, 2001; previously cited) and Kwon (Kwon, S.J. et al. “High-level production of porphyrins in metabolically engineered Escherichia coli: Systematic extension of a pathway assembled from overexpressed genes involved in heme biosynthesis” Applied and Environmental Microbiology, Vol. 69, No. 8 (2003), pp: 4875-4883), as applied to claim 2 above, and in further view of Kim (Kim, S-J et al. Journal of Microbiology and Biotechnology, Vol. 19 (2009), pp: 966-971; previously cited).
The rejection of claim 2 is described above. The combination of Elrod and Kwon renders elements of claim 2 obvious. However, the combination Elrod/Kwon does not teach a recombinant yeast cell that is Pichia pastoris.
However, Kim does teach a recombinant cell that is Pichia pastoris (see page 967, left column, lines 4-5).
Kim teaches that “[I]ndustrial applications of a fungal peroxidase require an efficient and economical production system” and that “[t]he methylotrophic yeast Pichia pastoris is well known for being effective in producing recombinant genetic material when facilitated by including a gene coding for a foreign protein behind the promoter of the AOX1 gene normally needed for methanol utilization, such that high quantities of foreign protein (10-100 times more than S. cerevisiae) can be expressed” (see page 966, right column, lines 7-18).
It would have been obvious to one with ordinary skills in the art before the effective filing date to have substituted the recombinant yeast taught by Elrod modified by Kwon, with a recombinant yeast as taught by Kim. One motivated in increasing productivity and yield in the recombinant expression system could have performed this substitution with a reasonable expectation of success and arrived at the claimed invention.
Claims 3, 4, 8, 9 and 21 are rejected under 35 U.S.C. § 103 as being
unpatentable over Elrod (Elrod, S.L. et al. US 6,261,827 B1; published Jul. 17, 2001; previously cited) and Kwon (Kwon, S.J. et al. “High-level production of porphyrins in metabolically engineered Escherichia coli: Systematic extension of a pathway assembled from overexpressed genes involved in heme biosynthesis” Applied and Environmental Microbiology, Vol. 69, No. 8 (2003), pp: 4875-4883), in view of Kim (Kim, S-J et al. Journal of Microbiology and Biotechnology, Vol. 19 (2009), pp: 966-971; previously cited).
Regarding claims 3, 8 and 9, Elrod teaches a recombinant yeast cell, expressing one or more heme biosynthetic enzymes and a hemoprotein (see abstract). Elrod teaches that the hemoprotein may be a globin (see column 3, lines 63-64).
Elrod teaches that the recombinant yeast may overexpress an endogenous (i.e. yeast) first nucleic acid encoding a 5-aminolevulinic acid synthase, a porphobilinogen synthase, a porphobilinogen deaminase, an uroporphyrinogen synthase, an uroporphyrinogen decarboxylase, a coporphyrinogen oxidase, a protoporphyrinogen oxidase and a ferrochelatase (see column 5, lines 26-36).
Elrod also teaches that the recombinant yeast may overexpress one or more second nucleic acids encoding a 5-aminolevulinic acid synthase, a porphobilinogen synthase, a porphobilinogen deaminase, an uroporphyrinogen synthase, an uroporphyrinogen decarboxylase, a coporphyrinogen oxidase, a protoporphyrinogen oxidase and a ferrochelatase (see column 7,lines 41-52).
Regarding claim 9, Elrod also teaches that the nucleic acids encoding the recombinant heme biosynthesis enzymes are stably integrated into the recombinant yeast (see column 4, lines 39-45). Elrod teaches “at least one” or “one or more” heme biosynthesis enzymes to be overexpressed in the recombinant yeast.
Elrod also teaches that “when a nucleic acid sequence encoding one of the enzymes in the heme biosynthetic pathway is introduced into a filamentous fungal cell, one or more pathway intermediates in one or more preceding steps may become rate-limiting (see column 11, lines 10-14).
However, Elrod does not teach eight genes encoding eight recombinant heme biosynthesis enzymes integrated into a recombinant yeast cell.
However, Kwon teaches expression of eight genes involved in heme biosynthetic pathways in different combinations, with up to seven genes simultaneously, in a recombinant Escherichia coli (E.coli) cell (see title and Tables 1 and 2, and figure 2).
Kwon teaches at first expression of five genes (hemA (ALAS), hemB (porphobilinogen synthase; ALA dehydratase), hemC (hydroxymethylbilane synthase; porphobilinogen deaminase), hemD (uroporphyrinogen III synthase) and hemE (uroporphyrinogen decarboxylase) (see page 4879, left column, first paragraph). Kwon teaches that the assembled heme pathway expressed in a recombinant E.coli, accumulated large amounts of porphyrins in the culture medium, with partial precipitation of porphyrins (same paragraph).
Kwon teaches systematic extension of the engineered heme biosynthetic pathway, adding hemF (oxygen-dependent coproporphyrinogen III oxidase), hemY (protoporphyrinogen oxidase or coproporphyrinogen oxidase) and hemH (ferrochelatase heme synthase) (see page 4880, left column).
Kwon teaches that the production level of porphyrins increased from 40% with overexpression of hemA alone or with hemB, to an additional 2 to 7 fold increase with overexpression of hemC and hemD. When adding hemABC with hemE, there was no observed change in production, however when adding hemF, there was an additional 70 to 80% increase in production of porphyrins. Although adding hemH to hemABCDEF did not significantly change the production, Kwon teaches overexpression of these seven genes simultaneously in E.coli (see pages 4880-4881, “Production levels” section). Kwon also teaches the overexpression of hemABCDEFY in E.coli (see Figure 2).
Kwon teaches optimization of the system, and also the development of a versatile system for tailored (over)production of major porphyrins that occur as intermediates in heme biosynthesis (see page 4881, left column, “Discussion” section).
It would have been obvious to one having ordinary skills in the art before the effective filing date of the claimed invention to have modified Elrod and introduced the eight genes HemABCDEFHY simultaneously in a cell and obtained eight stably integrated genes into the genome of a recombinant yeast to optimize production of a heme-containing protein. Since Kwon teaches that it is feasible to overexpress HemABCDEFY and HemABCDEFH simultaneously in two different recombinant E. coli, one with ordinary skills in the art could have also express HemABCDEFHY in the same cells. Since each one of the heme biosynthesis enzyme could be rate-limiting for the overexpression of a heme-containing protein, one motivated in optimizing a yeast system for overexpression of a heme-containing protein could have performed modifications to a system through routine optimization and trials as taught by Kwon, and introduced up to eight rate-limiting enzymes into a recombinant yeast.
Since the claimed invention is merely a combination of old elements, and in the combination each element merely would have performed the same function as it did separately, one of ordinary skill in the art would have recognized that the results of the combination were predictable. KSR, 127 S.Ct. at 1740, 82 USPQ2d at 1396.
Regarding claims 3, 4, 8, 9 and 21, the combination Elrod/Kwon does not teach a recombinant heme-containing protein expressed by a methanol inducible promoter, or wherein the promoter is pAOX1 promoter, as in claims 3 and 4. The combination Elrod/Kwon does not teach Pichia pastoris yeast cell, as in claim 8.
However, Kim teaches the use of a methanol inducible, i.e. pAOX1, referred to as pPICZαA, in the expression vector of a recombinant peroxidase (see title, abstract and figures 1A and 2).
Regarding claims 8 and 21, Kim also teaches a recombinant Pichia pastoris yeast cell (see page 967, left column, lines 4-5).
Kim teaches that “[I]ndustrial applications of a fungal peroxidase require an efficient and economical production system” and that “[t]he methylotrophic yeast Pichia pastoris is well known for being effective in producing recombinant genetic material when facilitated by including a gene coding for a foreign protein behind the promoter of the AOX1 gene normally needed for methanol utilization, such that high quantities of foreign protein (10-100 times more than S. cerevisiae) can be expressed” (see page 966, right column, lines 7-18).
It would have been obvious to one with ordinary skills in the art, before the effective filing date, to have substituted the control sequence in the vector used by Elrod to the methanol-inducible promoter taught by Kim. One motivated in using an endogenous sequence to the Pichia pastoris yeast and an endogenous methanol-inducible promoter to increase production of an exogenous protein, could have performed this substitution with a reasonable expectation of success, and arrived at the claimed invention.
Response to Arguments
Applicant's arguments filed 03/20/2026 regarding the rejections of claim 2-9 and 20-21 under 35 U.S.C. §103, have been fully considered but they are not persuasive.
Applicant argues on page 6/16 of Remarks, that “to establish a prima facie case of obviousness, the cited references must teach every limitation of the claims. In addition, there must be some suggestion or motivation, either in the references themselves or in the knowledge generally available to one of ordinary skill in the art, to modify the reference or to combine reference teachings.”
This argument has been addressed in the prior Office Action. Examiner previously stated:
“In response, Examiner respectfully disagrees. Elrod modified by Kwon teaches a recombinant cell overexpressing eight heme biosynthetic enzymes. The combination of Elrod and Kwon makes the product obvious. Since Elrod teaches one or more second nucleic acids encoding a 5-aminolevulinic acid synthase, a porphobilinogen synthase, a porphobilinogen deaminase, an uroporphyrinogen synthase, an uroporphyrinogen decarboxylase, a coporphyrinogen oxidase, a protoporphyrinogen oxidase and a ferrochelatase (see column 7,lines 41-52), and Kwon teaches at least two different combinations of the eight genes, overexpressing seven simultaneously, obtaining a cell that expresses eight genes from the heme biosynthetic pathway is rendered obvious with the combination of Elrod and Kwon. The genes are known in the art, as well as their functions. Therefore, the overexpression of a combination of eight genes from the heme biosynthetic pathway together is obvious. Transforming a cell with multiple nucleic acids encoding heme biosynthetic pathways enzymes is feasible, as shown by Kwon.”
In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, Elrod, in one hand, teaches that “when a nucleic acid sequence encoding one of the enzymes in the heme biosynthetic pathway is introduced into a filamentous fungal cell, one or more pathway intermediates in one or more preceding steps may become rate-limiting (see column 11, lines 10-14). Elrod further proposed to add intermediate products to the culture medium, with potentially a problem of permeability at the cell membrane level (same column). Kwon, on the other hand, teaches providing enzymes encoding nucleic acid to produce intermediate products in a host cell (see title and abstract).
In KSR Int 'l v. Teleflex, the Supreme Court, indicated that “The principles underlying [earlier] cases are instructive when the question is whether a patent claiming the combination of elements of prior art is obvious. When a work is available in one field of endeavor, design incentives and other market forces can prompt variations of it, either in the same field or a different one. If a person of ordinary skill can implement a predictable variation, § 103 likely bars its patentability”. KSR Int'l v. Teleflex lnc., 127 S. Ct. 1727, 1740 (2007).
Regarding Applicant’s arguments about Elrod and Kwon individually, and about the number of genes expressed as well as the stable expression of the genes, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
One have to consider the state of the art at the time of the invention.
Before the effective filing date, in 1998, Sears (Sears, I.B. et al. “A versatile set
of vectors for constitutive and regulated gene expression in Pichia pastoris”. YEAST, Vol. 14 (1998), pp: 783-790) teaches a set of vectors for constitutive and regulated gene expression in Pichia pastoris (see title). Sears teaches that using a vector comprising a AOX1 promoter have been widely used for the regulated over-production of cytosolic and secreted proteins (see age 783, “Introduction” section, left paragraph). Sears teaches the integration of their vectors into the HIS4 locus, therefore, stably integrating the gene of interest. Sears is cited as reference #23, in Kim (Kim, S-J et al. Journal of Microbiology and Biotechnology, Vol. 19 (2009), pp: 966-971; previously cited).
Before the effective filing date, in 2012, Mellitzer (Mellitzer, A. et al. “Expression
of lignocellulolytic enzymes in Pichia pastoris”. Microbial Cell Factories, Vol. 11 (2012), p: 61) teaches that they also used a AOX1 promoter issued from optimized library of promoter based on the wild-type version (see page 2, left column, lines 34-42). Mellitzer teaches optimizing and designing suitable expression constructs and strains for different cellulolytic enzymes (see page 2, left column, last paragraph). Mellitzer teaches the optimization of strains using multiple copy numbers of genes, designing a strain containing 25 expression cassettes (see page 4, left column, lines 16-18 and Figure 2A), and up to at least 7 copies for correlation between copy number and productivity (see page 4, left column, lines 31-34).
Therefore, the level of skills in the art before the effective filing date was high. With the advent of high-throughput screening methods for successful clones harboring multiple cassettes and gene copy numbers, it is reasonable to state that at least one clone comprising 8 genes on 8 individual expression cassettes or as a polycistronic cassette, could be obtained and isolated. The claims are drawn to a composition comprising a transgenic microorganism with 8 genes stably expressed, not to the productivity/yield of proteins expressed.
Double Patenting
The terminal disclaimer filed on 04/28/2025 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of US Patent No. 11, 439,166 B2 has been reviewed and accepted. The terminal disclaimer has been recorded.
Conclusion
No claim is allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/A.D./Examiner, Art Unit 1636
/NANCY J LEITH/Primary Examiner, Art Unit 1636
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