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 .
Applicants’ amendment to the claims filed on 5/15/2025 is acknowledged. This listing of claims replaces all prior listings of claims in the application.
Claims 56-74 are pending.
Claims 1-55 are cancelled.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 5/15/2025 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Drawings
The Drawings filed on 9/12/2024 are acknowledged and accepted by the Examiner.
Claim Objections
Claim 69 is objected to because of the following informalities: missing the recitation ‘of.’ The claim should recite ‘The method of claim…’ Appropriate correction is suggested.
Nucleotide and/or Amino Acid Sequence Disclosures
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d) in paras 0057, para 0065, para 0139, para 0140, para 0141, para 0152 of the instant application specification.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Written Description
Claims 56-74 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.
MPEP 2163.II.A.2.(a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention”.
For claims drawn to a genus, MPEP § 2163 states the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
Claims 56-74 are drawn to a method comprising a step of: culturing a microbial cell in the presence of a medium comprising a carbon source, a fatty acid, and amino acid and in the presence of an enzyme that covalently attaches a fatty acid to an amino acid under conditions and for a time sufficient for an acyl amino acid composition to be made, wherein the microbial cell comprises a modification that modulates hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid. The specification discloses in paragraph 0005 “such an engineered cell is an acyl-amino acid-producing cell, which comprises a modification (e.g. a genetic modification) that modulates hydroxylation and/or methylation of a fatty acid portion of an acyl amino acid.” The structure of said modification is a large number of modifications.
In this regard, the reference of Singh et al. (Current Protein and Peptide Science, 2017; cited on IDS dates 5/15/2025) reviews various protein engineering methods and discloses that despite the availability of an every-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by incomplete understanding of protein functions, folding, flexibility, and conformational changes [see p. 7, column 1, top]. The reference of Zhang et al. (Structure, 2018; cited on IDS dates 5/15/2025) discloses that a mutation of a residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide [see p. 1475, column 1].
An adequate written description of a chemical invention also requires a precise definition, such as by structure, formula, chemical name, or physical properties, and not merely a wish or plan for obtaining the chemical invention claimed. See, e.g., Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004). Here, the disclosure fails to teach which combination of modifications out of the numerous possibilities would modulate hydroxylation and/or methylation of a fatty acid portion of an acyl amino acid when engineered in any microbial cell.
Accordingly, one of skill in the art would not accept the disclosure of a Bacillus subtilis cell expressing a peptide synthetase enzyme in combination with expression or deletion of a fatty acid hydroxylase and/or fatty acid methylase as being representative of the entire genus of engineered microbial cells that modulate hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid as encompassed by the claims. As such, the specification, taken with the pre-existing knowledge in the art of fatty acid hydroxylase and fatty acid methylase, fails to satisfy the written description requirement of 35 U.S.C. 112, first paragraph.
Scope of Enablement
Claims 56-74 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of Bacillus subtilis cell expressing a peptide synthetase enzyme in combination with expression or deletion of a fatty acid hydroxylase and/or fatty acid methylase, does not provide enablement for all methods of modified microbial cells comprising a modification that modulates hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid as encompassed by the claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is mostly nearly connected, to make and/or use the invention commensurate in scope with these claims.
“The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue.” In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976). Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)) as follows: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. See MPEP § 2164.01(a). The Factors considered to be most relevant to the instant rejection are addressed in detail below.
(A)The breadth of the claims:
Claims 56-74 are drawn to a method comprising a step of: culturing a microbial cell in the presence of a medium comprising a carbon source, a fatty acid, and amino acid and in the presence of an enzyme that covalently attaches a fatty acid to an amino acid under conditions and for a time sufficient for an acyl amino acid composition to be made, wherein the microbial cell comprises a modification that modulates hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid. The specification discloses in paragraph 0005 “such an engineered cell is an acyl-amino acid-producing cell, which comprises a modification (e.g. a genetic modification) that modulates hydroxylation and/or methylation of a fatty acid portion of an acyl amino acid.” The structure of said modification is a large number of modifications.
It is well-known in the prior art that the amino acid sequence of a polypeptide determines the polypeptide’s functional properties. The positions within a protein's sequence where modifications can be made with a reasonable expectation of success in obtaining a polypeptide having the desired activity/utility are limited in any protein and the result of such modifications is highly unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g., multiple substitutions. The reference of Singh et al. (Current Protein and Peptide Science, 2017; cited on IDS dates 5/15/2025) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes [see p. 7, column 1, top]. The reference of Zhang et al. (Structure, 2018; cited on IDS dates 5/15/2025) discloses that a mutation of a residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide [p. 1475, column 1].
It is well-known in the art that even a single amino acid alteration can alter the folding of a polypeptide. See, e.g., MPEP 2144.08.II.A.4.(c), which states, “[i]n the area of biotechnology, an exemplified species may differ from a claimed species by a conservative substitution (“the replacement in a protein of one amino acid by another, chemically similar, amino acid... [which] is generally expected to lead to either no change or only a small change in the properties of the protein.” Dictionary of Biochemistry and Molecular Biology 97 (John Wiley & Sons, 2d ed. 1989)). The effect of a conservative substitution on protein function depends on the nature of the substitution and its location in the chain. Although at some locations a conservative substitution may be benign, in some proteins only one amino acid is allowed at a given position. For example, the gain or loss of even one methyl group can destabilize the structure if close packing is required in the interior of domains. James Darnell et al., Molecular Cell Biology 51 (2d ed. 1990).”
(F) The amount of direction provided by the inventor and (G) The existence of working examples: The specification discloses the following working examples of modifications that modulate hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid, a Bacillus subtilis cell expressing a peptide synthetase in combination with expression or deletion of a fatty acid hydroxylase and/or fatty acid methylase. Other than these working examples, the specification fails to disclose any other working examples of modifications that modulate hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid as encompassed by the claims.
In view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability, and the state of the prior art, undue experimentation would be necessary for a skilled artisan to make and use the entire scope of the claimed invention. Applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 112(b)
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 58, 69-70 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.
Claims 58, 69 recites the phrase ‘reduced or abrogated expression.’ ’ The term "reduced" is a relative term which renders the claim indefinite. The term "reduced" is a term of degree, and there is no indication what the reduction is being compared. Accordingly, the metes and bounds upon which patent protection is sought cannot be ascertained from the claims. It is suggested that Applicant clarify the meaning of the claims. See Supplementary Examination Guidelines for Determining Compliance with 35 U.S.C. §112 and for Treatment of Related Issues in Patent Applications, 76 FR 7162 (Feb. 9, 2011), page 7165.
Claim 70 recites ‘increased expression of a gene.’ The term "increased" is a relative term which renders the claim indefinite. The term "increased" is a term of degree, and there is no indication what the increase is being compared. Accordingly, the metes and bounds upon which patent protection is sought cannot be ascertained from the claims. It is suggested that Applicant clarify the meaning of the claims. See Supplementary Examination Guidelines for Determining Compliance with 35 U.S.C. §112 and for Treatment of Related Issues in Patent Applications, 76 FR 7162 (Feb. 9, 2011), page 7165.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 56-71, 73 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Jarrell et al (US 7,981,685 B2, filed on April 16, 2008, published on July 19, 2011, cited on IDS dates 5/15/2025) {herein Jarrell 685} as evidenced by Liu et al (Date of Publication: May 9, 2014, ASBMB, Examiner cited) {herein Liu}, Perino et al (Date of Publication: 2026, Microbial Cell Factories, Examiner cited) {herein Perino} and Hannemann et al. (2 August 2006, Biochimica, 10.1016/j.bbagen.2006.07.017, cited on IDS dates 5/15/2025) {herein Hannemann). See MPEP 2131.01 regarding multiple reference 102 rejections.
Claims 56-71, 73 are drawn to a method comprising a step of :culturing a microbial cell in the presence of a medium comprising a carbon source, a fatty acid, and amino acid and in the presence of an enzyme that covalently attaches a fatty acid to an amino acid under conditions and for a time sufficient for an acyl amino acid composition to be made, wherein the microbial cell comprises a modification that modulates hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid.
With respect to claims 56-57, 59, 71 Jarrell 685 teaches a method of making an engineered (modified) polypeptide comprising a peptide synthetase domain, a fatty acid linkage domain, and a thioesterase domain which is introduced into a host cell, Bacillus subtilis (column 1, lines 47-49; column 2, lines 26-27; column 2, line 29). Said genetically modified cells are grown in M9YE+1% casamino acids (amino acids), glucose (carbon source) and myristic acid (fatty acid) (column 28, lines 38-39; table 1). The modified cell has a beta-hydroxy fatty acid linkage domain that is covalently linked to a peptide synthetase domain and a reductase domain to generate an engineered polypeptide that is useful in the synthesis of an acyl amino acid (column 3, lines 57-61). The term “beta hydroxy fatty acid linkage domain” as used herein refers to a polypeptide domain that covalently links a beta-hydroxy fatty acid to an amino acid to form an acyl amino acid thereby increasing the number of hydroxyl groups as compared to that when the modification is absent (column 3, lines 50-53). Furthermore, Jarrell teaches that engineered polypeptides comprising such engineered fatty acid linkage domains may yield an increased amount of the acyl amino acid, may be more stable in a given host cell, may be less toxic to a given host cell, etc (column 15, liners 10-14).
With respect to claims 58, 70, Jarrell 685 teaches a method wherein the SRFA gene necessary to catalyze the addition of the amino acid (leucine) is deleted in a strain (column 20, lines 51-53). SRFA is a gene that codes for a surfactant synthetase (column 19, lines 23 and column 20, lines 16-18) and modulates hydroxylation alongside P450 enzymes. Said gene is a giant multi-modular enzyme complex that functions as a non-ribosomal peptide synthetase (NRPS). Absence of the SRFA gene results in an engineered acyl amino acid lacking a second amino acid, leucine (column 22, line 39). Furthermore, deletion of the SRFA gene results in the decreased expression of various lipid and fatty acid metabolism genes, including those encoding key modifying enzymes like hormone-sensitive lipase and desaturases. Supporting the Examiner’s position is the evidentiary reference of Liu which is cited to demonstrate that the expression of Lipe (hormone sensitive lipase) is reduced in the absence of SRFA, which is a fatty acid modifying enzyme (page 13005, column 2, para 1). In addition, deletion of the SRFA gene in Bacillus species removes surfactin production, thereby triggering a metabolic feedback response that significantly upregulates genes involved in fatty acid biosynthesis to compensate for the disrupted lipid and precursor pathways. Supporting the Examiner’s position is the evidentiary reference of Perino which is cited to demonstrate that several proteins associated with secretion and cell envelope processes were more abundant in the non-surfactin-producing mutants (page 8, column 2, para 4).
With respect to claims 60, 73, Jarrell 685 teaches a method wherein engineered polypeptides containing an engineered beta-hydroxy fatty acid linkage domain are useful in the generation of acyl amino acids comprising beta-hydroxy myristic acid, such as, without limitation, cocoyl glutamate (an acyl glutamate) (column 15, lines 2-7). The beta-hydroxy fatty acid linkage domain of the SRFA protein (srfa is a surfactin synthetase polypeptide (column 20, lines 18-19) linked such that the engineered beta-hydroxy fatty acid linkage domain still retains specificity for beta hydroxy myristic acid (column 14 lines 65-67 and column 15, lines 1-2). Furthermore, the reductase domain of the linear gramicidin synthetase complex is effective in releasing cocoyl glutamate from engineered polypeptides (column 15, lines 54-59). Specifically, SFRA catalyzes the release of the product via a nucleophilic attack of the beta-hydroxy of the fatty acid, thereby reducing the number of hydroxyl groups (column 20, lines 26-27).
With respect to claims 61-64, 66-68, Jarrell 685 teaches a method for producing acyl amino acids by employing engineered polypeptides comprising a peptide synthetase domain covalently linked to a fatty acid linkage domain and a thioesterase domain or reductase domain, with the reductase domain being the fatty acid modifying enzyme (column 3, lines 19-23). In the host cell, Bacillus subtilus, the reductase domain natively contains P450s which are well-known in the art to function as fatty acid hydroxylases. Supporting the Examiner’s position is the evidentiary reference of Hannerman which is cited to demonstrate that P450 genes are inherently present in Bacillus subtilus (abstract). Such genes encode hydroxylase activities including the biosynthesis of compounds such as fatty acids via hydroxylation and hydroxylates lauric acid (Hannerman: abstract; page 330, column 2, paragraph 1; page 331, column 1, paragraph 2). Furthermore, Hannerman is cited to demonstrate that the fatty acid hydroxylase within said host cell, Bacillus subtilus, inherently shows a strong selectivity for branched fatty acids and long-chain unsaturated (unbranched) chain fatty acids (page 336, column 2, paragraph 2). Therefore, the fatty acid modifying enzyme taught by Jarrell having hydroxylase activity is inherent to the host cell Bacillus subtilus, taught by Jarrell. Since the Office does not have the facilities for examining and comparing Applicants’ fatty acid modifying enzyme with that of the prior art, the burden is on the Applicant to show a novel or unobvious difference between the claimed method and the method of the prior art (i.e., that the fatty acid modifying enzyme of the prior art does not possess the same activity of the claimed fatty acid modifying enzyme). See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
With respect to claim 65, the genes cyp102A2 and cyp102A3 are inherently present in Bacillus subtilus. As such, it is the Examiner’s position that the host strain of Bacillus subtilus, taught by Jarrell, would inherently express said genes. Especially since Jarrell does not teach said genes are deleted from the host cell. Supporting the Examiner’s position is the evidentiary reference of Hannemann which is cited to demonstrate that CYP102A2 and CYP102A3 are present in Bacillus subtilis (page 336, column 2, paragraph 2) of which the instant application states are fatty acid hydroxylases that may be involved in generation of acyl amino acids (instant application paragraph 0008). Since the Office does not have the facilities for examining and comparing Applicants’ host strain with that of the prior art, the burden is on the Applicant to show a novel or unobvious difference between the claimed method and the method of the prior art (i.e., that the host strain of the prior art does not possess the same genetic composition as the claimed host strain). See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
With respect to claim 69, Jarrell 685 teaches a method wherein the SRFA gene necessary to catalyze the addition of the amino acid (leucine) was deleted in a strain (column 20, lines 51-53). SRFA is a gene that codes for a surfactin synthetase (column 19, lines 23 and column 20, lines 16-18). The absence of the SRFA gene results in an engineered acyl amino acid lacking a second amino acid, leucine (column 22, line 39).
For the reasons stated herein, the teachings of Jarrell 685 anticipates claims 56-71, 73.
Claim Rejections - 35 USC § 103
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 72, 74 are rejected under 35 U.S.C. 103 as being unpatentable over Jarrell et al (US 7,981,685 B2, filed on April 16, 2008, patent date July 19, 2011, cited on IDS dates 5/15/2025) {herein Jarrell 685} as applied to claims 56-71, 73 in view of Su et al. (US 11,045,404 B2, filed on Dec. 14, 2016, patent date Jun. 29, 2021, cited on IDS dates 5/15/2025) {herein Su} as evidenced by Liu et al (Date of Publication: May 9, 2014, ASBMB, Examiner cited), Perino et al (Date of Publication: 2026, Microbial Cell Factories, Examiner cited) {herein Perino} and Hannemann et al. (2 August 2006, Biochimica, 10.1016/j.bbagen.2006.07.017, cited on IDS dates 5/15/2025) {herein Hannemann).
Claim 72 is drawn to the method of claim 56, wherein the acyl amino acid is acyl glycinate.
Claim 74 is drawn to the method of claim 56, wherein the acyl amino acid is acyl sarconsinate.
The teachings of Jarrell 685 are incorporated herein from the 102a1 rejection as applied to claims 56-71, 73.
However, Jarrell 685 does not teach a method wherein the acyl amino acid is acyl glycinate (claim 72). Jarrell 685 does not teach a method wherein the acyl amino acid is acyl sarconsinate (claim 74).
With respect to claims 72, 74, Su teaches among the four major amino acid surfactants, namely acyl glycinates , acyl glutamates and acyl sarconsinates are the most sustainable and cost-effective surfactants (column 6, lines 21-23).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to try making acyl glycinates and acyl sarconsinates based on the teachings of Jarrell 385 and Su because Su teaches acyl glycinate and acyl sarconsinate are surfactants that are readily available, utilized in the industry (column 6, lines 21-23) and cost effective when utilized in mass quantities (column 6, lines 23-24). It would be obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to try making said acyl amino acids as Jarrell teaches modified polypeptide constructs that are useful in the generation of any of a variety of acyl amino acids of interest. Therefore, one of ordinary skill in the art could reasonably envision making acyl glycinates and acyl sarconsinates. Especially since Su teaches they are cost effective when utilized in mass quantities (column 6, lines 23-24) and Jarrell teaches the commercial production of acyl amino acids (column 1, line 26). 2143.I.E. states “The rationale to support a conclusion that the claim would have been obvious is that "a person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely that product [was] not of innovation but of ordinary skill and common sense. In that instance the fact that a combination was obvious to try might show that it was obvious under § 103."KSR, 550 U.S. at 421, 82 USPQ2d at 1397.”
One of ordinary skill in the art would have had a reasonable expectation of success, a reasonable level of predictability, and would be motivated try making acyl glycinates and acyl sarconsinates based on the teachings of Jarrell 385 and Su because Jarrell 385 provides a method and teachings of engineering microbial cells to produce peptides linked to a synthetase to synthesize acyl amino acids with the ability to modulate hydroxylation of a fatty acid to produce the acyl surfactant acyl glutamate and Su acknowledges the versatility of acyl surfactants such as acyl glycinate, acyl glutamate and acyl sarconsinate and their usefulness in many facets (column 6, lines 21-23). Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 56-74 are rejected on the grounds of nonstatutory double patenting as being unpatentable over claim 13 of U.S. Patent No. US 12,123,004 B2 which are commonly owned and have common inventors and filed before the instant application s/n 18/883,913. Although the claims at issue are not identical, they are not patentably distinct from each other because the claims are drawn to a method of making an acyl amino acid composition, the method comprising a step of culturing an engineered Bacillus subtilis cell that: (i) expresses at least one peptide synthetase, which peptide synthetase synthesizes an acyl amino acid, and (ii) comprises a modification that comprises deletion of a fatty acid hydroxylase gene, wherein the modification results in a reduction in the number of hydroxyl groups of a fatty acid portion of the acyl amino acid, as compared to when the modification is absent under conditions and for a time sufficient for an acyl amino acid composition to be made which is not patentably distinct from the instant application claims 56-74, which recites, in summary, a method comprising a step of culturing a microbial cell in the presence of a medium comprising a carbon source, a fatty acid, and amino acid and in the presence of an enzyme that covalently attaches a fatty acid to an amino acid under conditions and for a time sufficient for an acyl amino acid composition to be made, wherein the microbial cell comprises a modification that modulates hydroxylation and/or methylation of a fatty acid portion of the acyl amino acid.
this
Conclusion
Status of Claims
Claims 56-74 are pending.
Claims 1-55 are cancelled.
Claim 56-74 are rejected.
No claims are in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERICA NICOLE JONES-FOSTER whose telephone number is (571)270-0360. The examiner can normally be reached mf 7:30a - 4:30p.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached at 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/ERICA NICOLE JONES-FOSTER/Examiner, Art Unit 1656
/MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656
Prosecution Insights