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 .
Election/Restrictions
Applicant's election with traverse of claims 1-5 and 7-8, as well as species “single point mutation” in claim 1, “H43Y” in claim 2, and “FAK” in claim 7, in the reply filed on 8/3/2026 is acknowledged. The traversal is on the ground(s) that Trollope does not disclose the shared special technical feature of the claimed inventions because the mutations identified and experimentally validated by Applicant, including elected species H43Y, do not coincide with the mutations disclosed in Trollope. This is not found persuasive because the shared technical feature of the claimed groups of inventions is a modified FTase polypeptide from Aspergillus sp. having any mutations. The claims of groups II-VI are dependent on claim 1. Claim 1 does not require any of the specific mutations discussed by Applicant. Group VII requires an FTase protein with mutations. As such, Trollope et al. teaches the shared technical feature of the groups of inventions, and it is not considered a special technical feature. For this reason, the inventions lack unity.
The requirement is still deemed proper and is therefore made FINAL.
Claims 6 and 9-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 8/3/2026.
In view of the prior art search, the species election is expanded to include deletion mutations and the point mutation H240F.
Priority
This application is a 371 of PCT/IN2022/051021 (11/22/2022) which claims priority to IN202141053708 (11/22/2021).
Information Disclosure Statement
The information disclosure statement (IDS) filed on 5/21/2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawings
The drawings are objected to for the following reasons:
37 CFR 1.84 states “Character of lines, numbers and letters. All drawings must be made by a process that will give them satisfactory reproduction characteristics. Every line, number, and letter must be durable, clean, black (except for color drawings), sufficiently dense and dark, and uniformly thick and well-defined.”
In the current case, the words in Figures 1, 2, and 8 are illegible.
The drawings are objected to for the following reasons:
37 CFR 1.84(u)(1) states “View numbers must be preceded by the abbreviation “FIG.”.
In the current case, the view numbers for Figures 1-12 are preceded by the word “Figure” instead of the abbreviation “FIG.”. View numbers should be updated to recite the abbreviation “FIG.”. Any changes to the drawings should also be reflected in the specification.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Objections
Claims 1, 3, and 7 are objected to because of the following informalities:
Claim 1 recites the acronym FTase. Claim 3 recites the acronym “aa”. Claim 7 recites acronyms FAK, FAKS, etc. When an acronym is used in a claim set, it should be defined the first time it appears in the claims. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Claims 1-5 and 7-8 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.
Regarding written description, 35 U.S.C. 112(a) and the first paragraph of pre-AlA 35 U.S.C. 112 require that the "specification shall contain a written description of the invention ...." This requirement is separate and distinct from the enablement requirement. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010). To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention (MPEP § 2163(I)).
MPEP 2163(II)(A)(3)(a)(i and ii) states that 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.
A "representative number of species" means that the species which are adequately described are representative of the entire genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., .759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
Claim 1 recites “the polypeptide is a FTase of Aspergillus sp. comprising mutations selected from but not limited to single point mutations or multiple point mutations or deletion mutations or a combination thereof”. The phrase “but not limited to” encompasses any possible mutation that can be made to the FTase. However, the only types of mutations disclosed are point mutations and deletion mutations (see instant specification p. 15). Mutation is not defined in the specification to provide identifying structural properties for any types of mutations other than point mutations and deletion mutations.
Additionally, the disclosure does not provide support for modifications to any FTase of Aspergillus sp. The specification discusses FTases from Aspergillus niger, Aspergillus japonicus, Aspergillus fijiensis and Aspergillus aculeatus (instant specification p. 2 and SEQ ID NOs: 1-4). The only examples of modified FTases in the specification are point mutations to Aspergillus niger β-fructofuranosidase (see e.g. instant specification pp. 25-26 Ex. 1). As there are many Aspergillus sp. with different FTase polypeptide sequences, these examples from Aspergillus niger are not representative of the whole genus of modified Aspergillus sp. FTase polypeptides. Therefore, it is not clear that applicant was in possession of the entire genus of FTase polypeptides from any Aspergillus sp. which comprise any possible type of mutation.
Claims 2-5 are included in this rejection because they depend on a rejected claim and do not clarify the issue.
Claims 7 and 8 recite signal peptides or variants thereof. “Variants” refers to peptides with amino acid substitutions, additions, deletions or alterations that do not substantially decrease the activity of the signal peptide or the enzyme (see instant specification p. 14). This functional limitation does not correspond with any particular disclosed structure. Substitutions, additions, deletions, or alterations include a vast number of potential changes to the signal peptide sequence. There is no disclosure of what specific changes can or cannot be made which “do not substantially decrease the activity of the signal peptide”, i.e. specific residues that can or cannot be altered, how many residues can be altered while maintaining the peptide activity, etc. There are no disclosed examples of signal peptide variant sequences. There is not a disclosure of a structure/function relationship to identify which of the many possible variants of the claimed signal peptides would have the required function. Therefore, it is not clear that applicant was in possession of the entire genus of signal peptide variants as claimed.
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 1-2, 4-5, and 7-8 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.
Claim 1 recites “comprising mutations selected from but not limited to single point mutations or multiple point mutations or deletion mutations or a combination thereof”. A Markush grouping is a closed group of alternatives, i.e., the selection is made from a group "consisting of" (rather than "comprising" or "including") the alternative members (see MPEP § 2173.05(h)). In this case, the claim does not recite a closed group of alternatives, given the open-ended phrase “but not limited to”. This renders the scope of the claim indefinite, as it is not clear which other types of mutations are intended to be encompassed by the claim.
Similarly, claim 2 recites “the point mutations are selected from but not limited to”, claim 3 recites “the deletion mutations are selected from but not limited to”, and claim 4 recites “wherein the polypeptide sequences are selected from but not limited to”. It is not clear which other mutations or polypeptide sequences are intended to be encompassed by the claims, rendering the scope of the claims indefinite.
Claim 7 recites “a signal peptide selected from a group comprising”. The term “comprising” is open-ended, and it is unclear what other alternative signal sequences are intended to be encompassed by the claim (see MPEP § 2173.05(h)).
Claim 2 recites the modified polypeptide as claimed in claim 1, with specific point mutations. However, claims 1 and 2 do not recite a sequence. Claim 1 recites that the polypeptide is an FTase of Aspergillus sp. There are numerous FTase polypeptides from various Aspergillus sp., and not all of these polypeptides have the same amino acids at the positions recited in claim 2. This can be seen in Figure 1 of the instant application, showing an alignment of multiple FTase polypeptide sequences from different Aspergillus sp. The FTase polypeptide sequences do not all have the same amino acids at the same residues, for example the first residue of the sequence of Aspergillus niger does not align with the first residue of Aspergillus fijiensis. Therefore, not all Aspergillus FTase polypeptides have the amino acid residues as recited in claim 2. As there is no reference sequence identified in claims 1 or 2, it is unclear what sequence the point mutations refer to. For the purposes of examination, it is considered that the mutations are made relative to the Aspergillus niger FTase sequence of SEQ ID NO: 1, as the position numbers in the claims and the examples in the specification align with this sequence (see e.g. instant specification pp. 4-12, SEQ ID NOs: 9-218).
Claim 3 recites “wherein the deletion mutations are selected from but not limited to 32-654 aa, 32-194 aa, 1-194 aa”. It is not clear whether these deletion mutations refer to the positions of the amino acids that are included in the sequence, the positions of the amino acids that are deleted from the sequence, or the number of positions that can be deleted (i.e., between 32 and 194 amino acids can be deleted). Additionally, as discussed above, there is no reference sequence identified in claims 1 or 3, so it is unclear what sequence the deletion mutations are in relation to. For the purposes of examination, it is considered that a deletion of any amino acids reads on the claim.
Claims 4 and 5 recite that the modified polypeptide of claim 1 has a polypeptide sequence selected from SEQ ID NOs: 9-218, or SEQ ID NOs: 9-66. However, some of these sequences are nucleotide sequences (see table on pp. 4-12 of instant specification). A nucleotide sequence is not a polypeptide sequence. Therefore, the scope of claims 4 and 5 is unclear.
Claims 4 and 5 recite the limitation “the polypeptide sequences”. There is insufficient antecedent basis for this limitation in the claim. Claim 1, upon which claims 4 and 5 depend, does not recite a polypeptide sequence. Further, claim 1 recites only “a modified polypeptide”. Although a polypeptide would inherently have a polypeptide sequence, claims 4 and 5 recite multiple polypeptide sequences, and it is not clear what the limitation directed to multiple polypeptide sequences refers to.
Claim 7 recites the limitation “the amino acid sequence or nucleotide sequence”. There is insufficient antecedent basis for this limitation in the claim. Claim 1, upon which claim 7 depends, is directed to a polypeptide and does not recite a nucleotide sequence. Therefore, it is unclear what “the nucleotide sequence” in claim 7 is referring to.
Claim 8 is included in this rejection because it depends on a rejected claim and does not clarify the issue.
Claim Rejections - 35 USC § 102
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-5 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Nakamura et al., US 2008/0187970 A1.
Regarding claim 1, Nakamura teaches β-fructofuranosidase variants whose reaction specificities are improved to be suitable for the production of single components of fructooligosaccharides (p. 1 para. 5). Nakamura teaches a β-fructofuranosidase variant consisting of a mutated amino acid sequence of SEQ ID NO: 2, which is a β-fructofuranosidase from Aspergillus niger, wherein the mutations are single point mutations (p. 1 para. 7; para. 10; p. 8 SEQ ID NO: 2). Thus, Nakamura teaches a modified polypeptide which is an FTase from Aspergillus sp. comprising single point mutations. SEQ ID NO: 2 of Nakamura also comprises a deletion relative to the wildtype Aspergillus niger β-fructofuranosidase (instant SEQ ID NO: 1), as it does not contain positions 1-19 (see sequence alignment in OA appendix).
Regarding claim 2, Nakamura teaches that the polypeptide according to SEQ ID NO: 2 may comprise a point mutation at position 221 (p. 1 para. 7). Nakamura SEQ ID NO: 2 is 100% identical to positions 20-654 of instant SEQ ID NO: 1, which is β-fructofuranosidase from Aspergillus niger (see sequence alignment in OA appendix). Position 221 in SEQ ID NO: 2 of Nakamura corresponds to position 240 of instant SEQ ID NO: 1 (see sequence alignment in OA appendix). Nakamura teaches that the substitution at position 221 of SEQ ID NO: 2 is selected from tryptophan (W), phenylalanine (F), and tyrosine (Y) (p. 2 para. 26). Therefore, Nakamura teaches a substitution H221F, or H240F, in instant SEQ ID NO: 1.
Regarding claim 3, SEQ ID NO: 2 of Nakamura comprises a deletion mutation relative to the wildtype Aspergillus niger β-fructofuranosidase (instant SEQ ID NO: 1), as it does not comprise positions 1-19 (see sequence alignment in OA appendix).
Regarding claims 4 and 5, SEQ ID NO: 2 of Nakamura is 100% identical to instant SEQ ID NO: 58 (see sequence alignment in OA appendix).
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.
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 nonobviousness.
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.
Claims 7 and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Nakamura et al., US 2008/0187970 A1 in view of Brandt et al., US 6,183,989 B1.
Nakamura teaches a β-fructofuranosidase variant according to claim 1 as discussed above. Nakamura teaches that the β-fructofuranosidase variant is produced via expression in host cells, such as yeast cells, and that when the host cell is a yeast a secretion vector is advantageously used to extracellularly secrete the recombinant β-fructofuranosidase (Nakamura pp. 3-4 para. 52 and 57).
Nakamura does not teach that the FTase polypeptide is fused to a signal peptide FAK (claim 7) with a sequence of SEQ ID NO: 219 (claim 8).
Regarding claim 7, Brandt teaches that for expression of heterologous proteins in yeast cells such as Saccharomyces cerevisiae, signal peptides, including Saccharomyces cerevisiae MFα or α-factor, are used (Brandt col. 1 lines 20-52). The claimed signal peptide FAK is S. cerevisiae α-factor (see instant specification Table 4). Brandt teaches that the α factor signal peptide has been widely employed to obtain synthesis and secretion of heterologous proteins in S. cerevisiae, and teaches producing heterologous polypeptides of interest in yeast using the signal peptide fused to the desired polypeptide (Brandt col. 2 lines 34-50).
Regarding claim 8, Brandt teaches that the α factor peptide has a sequence, SEQ ID NO: 1, that is 100% identical to instant SEQ ID NO: 219 (Brandt col. 3 lines 28-34, see sequence alignment in OA appendix).
It would have been obvious for a skilled artisan to fuse the β-fructofuranosidase variant taught by Nakamura to an FAK signal peptide with a sequence according to SEQ ID NO: 219. Brandt teaches that polypeptides of interest can be modified with the FAK (α factor) signal sequence for expression in yeast systems, and a skilled artisan would recognize that the β-fructofuranosidase polypeptide of Nakamura could be modified in this manner, especially given the teachings of Nakamura that the β-fructofuranosidase variant can be expressed in a host cell and extracellularly secreted.
A person of ordinary skill in the art would have been motivated to make this modification because fusing the FAK signal polypeptide allows for secretion of polypeptides extracellularly when the polypeptide is expressed in a yeast expression system (Brandt col. 3 lines 48-64). Thus, this modification would be useful to facilitate the production and secretion of the β-fructofuranosidase polypeptide of Nakamura in an industrial or biotechnological setting. Nakamura teaches that when using a yeast host cell for production of the β-fructofuranosidase variant it is advantageous to extracellularly secrete the polypeptide (Nakamura p. 4 para. 57). Therefore, a skilled artisan would have been motivated to make a modification that is known and widely employed to secrete heterologous proteins in the yeast S. cerevisiae to the polypeptide as taught by Nakamura for achieving this same purpose.
A skilled artisan would have had a reasonable expectation of success in making this modification because Brandt teaches that the use of the α factor signal peptide is a widely employed modification for expression of heterologous proteins in yeast, and it would therefore be expected that the polypeptide sequence as taught by Nakamura could be modified with this known and established signal peptide. A person having ordinary skill in the art would have a reasonable expectation of achieving predictable results, i.e. that the modification would result in a polypeptide that can be expressed and secreted in yeast expression systems.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 7, and 8 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 2 of U.S. Patent No. US12606806 B2. Although the claims at issue are not identical, they are not patentably distinct from each other because both are directed to modified Aspergillus FTase polypeptides.
Regarding instant claims 1, 7, and 8, claim 1 of ‘806 recites a modified fructosyltransferase of Aspergillus japonicus, wherein the modification is a fusion of fructosyltransferase of Aspergillus japonicus having the amino acid sequence of SEQ ID NO: 1 to a signal peptide, wherein the signal peptide is alpha-factor of Saccharomyces cerevisiae (FAK), alpha-factor full of S. cerevisiae (FAKS), alpha factor_T of S. cerevisiae (AT), alpha-amylase of Aspergillus niger (AA), glucoamylase of Aspergillus awamori (GA), inulinase of Kluyveromyces maxianus (IN), invertase of S. cerevisiae (IV), killer protein of S. cerevisiae (KP), lysozyme of Gallus gallus (LZ), or serum albumin of Homo sapiens (SA). Claim 2 of ‘806 recites the sequences of these signal peptides.
Claims 1, 7, and 8 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 2 of copending Application No. 17/779,016 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both are directed to modified Aspergillus FTase polypeptides.
Regarding instant claims 1, 7, and 8, claim 1 of ‘016 recites a modified fructofuranosidase of Aspergillus niger, comprising the amino acid sequence of SEQ ID NO: 1 fused to a signal peptide, wherein the signal peptide is alpha-factor of Saccharomyces cerevisiae (FAK), alpha-factor full of S. cerevisiae (FAKS), alpha factor_T of S. cerevisiae (AT), alpha- amylase of Aspergillus niger (AA), glucoamylase of Aspergillus awamori (GA), inulinase of Kluyveromyces maxianus (IN), invertase of S. cerevisiae (IV), killer protein of S. cerevisiae (KP),lysozyme of Gallus gallus (LZ), or serum albumin of Homo sapiens (SA). Claim 2 of ‘016 recites the sequences of these signal peptides.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Claims 1-5 and 7-8 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to EMILY F EIX whose telephone number is (571)270-0808. The examiner can normally be reached M-F 8am-5pm ET.
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/EMILY F EIX/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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