DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 13-19 are pending in the application.
Applicant’s amendment to the claims, filed February 4, 2026, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s amendment to the drawing figures, filed February 4, 2026, is acknowledged.
Applicant’s remarks filed February 4, 2026 in response to the non-final rejection filed October 6, 2025 are acknowledged and have been fully considered.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Restriction/Election
In response to a requirement for restriction/election filed August 21, 2025, applicant elected with traverse the invention of Group II, corresponding to pending claims 13-19, and species (D), a protein consisting of an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO: 8, and having α-amylase activity, in the reply filed September 23, 2025. The requirement was deemed proper and made FINAL in the non-final rejection filed October 6, 2025.
Claims 13-19 are being examined on the merits with claims 13 and 18 being examined only to the extent the claims read on the elected subject matter.
Drawings
The objection to the drawing figures is withdrawn in view of applicant’s submission of amended drawing figures with view numbers preceded by the abbreviation "FIG."
Claim Rejections - 35 USC § 102
The rejection of claims 13-15 under 35 U.S.C. 102(a)(2) as being anticipated by Hioki et al. (WO 2022/071451 A1, with priority to October 2, 2020; cited on the attached Form PTO-892; hereafter “Hioki”) is withdrawn in view of applicant’s statement of common ownership or obligation of assignment to establish a prior art exception under 35 U.S.C. 102(b)(2)(C).
Claim Rejections - 35 USC § 103
Claims 13-19 are rejected under 35 U.S.C. 103 as being unpatentable over Pramod et al. (WO 1997/004067; cited on Form PTO-892 filed October 6, 2025; hereafter “Pramod”) in view of UniProt Database Accession Number K4LYT6 (February 2018, 2 pages; cited on Form PTO-892 filed October 6, 2025; hereafter “UniProt”) and Kachan et al. (Central European Journal of Biology 8:346-356, 2013; cited on the IDS filed on January 12, 2023; hereafter “Kachan”). The instant rejection has been modified from its previous version to address applicant’s amendment to the claims.
As amended, the claims are drawn to (in relevant part) a method of cleaning an article, comprising contacting the article with a composition comprising a protein consisting of an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO: 8, and having α-amylase activity,
wherein the contacting is performed at a temperature of 40°C or less, and
wherein the protein is a protein having a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12.
Regarding the claim 13 limitation “method of cleaning an article, comprising contacting the article with a composition comprising…a protein consisting of an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO: 8, and having α-amylase activity,” Pramod teaches amylase enzymes provide superior dingy clean up, whiteness maintenance, and overall cleaning performance (p. 2, top). Pramod teaches a laundry detergent composition comprising a detergent surfactant and one or more amylase enzymes in an amount effective to increase the whiteness of dingy fabrics, and methods for laundering fabrics (p. 2, middle to bottom). Pramod teaches suitable amylases for use in the compositions include α-amylases (p. 4, middle).
Regarding the claim 13 limitation “wherein the contacting is performed at a temperature of 40°C or less” and the limitations of claims 14, 16, and 17, Pramod teaches laundry wash solutions are preferably at temperatures between about 5°C and about 95°C, preferably between about 10°C and about 60°C, for this cleaning benefit (p. 3, middle).
Regarding the claim 15 limitation “wherein the article is clothing,” Pramod teaches the superior cleaning performance by amylase enzymes is illustrated by excellent soil removal on pillow cases, T-shirts and sock bottoms (p. 2, top).
The difference between Pramod and the claimed invention is that Pramod does not teach or suggest a protein consisting of an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO: 8 and having a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12.
UniProt teaches an α-amylase from Bacillus sp. 406. The amino acid sequence of UniProt has 99% sequence identity to the amino acid sequence of SEQ ID NO: 8 of this application (see Appendix B beginning at p. 13 of the Office action filed October 6, 2025).
Kachan teaches a temperature profile for α-amylase from Bacillus sp. 406, referred to as “AB406” (p. 349, Figure 1) showing that AB406 maintains activity at temperatures of 27.5°C to 40°C. Kachan teaches an AB406 variant with deletion of Arg178-Gly179, which increased stability (p. 349, column 2, middle).
In view of the combination of Pramod, UniProt, and Kachan, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the α-amylase of UniProt or AB406 variant of Kachan for laundering fabrics according to Pramod. One would have been motivated and would have expected success because Pramod teaches suitable amylases for the detergent composition include α-amylases, and UniProt and Kachan each teaches an α-amylase.
Pramod’s method for laundering fabrics includes a temperature range that overlaps with the recited temperature ranges in claims 13, 14, 16, and 17. According to MPEP § 2144.05.I, “[i]n the case where the claimed ranges ‘overlap or lie inside ranges disclosed by the prior art’ a prima facie case of obviousness exists.” One would have had a reasonable expectation of success to use the α-amylase of UniProt or AB406 variant of Kachan for laundering fabrics at a temperature within the recited temperature ranges because Kachan teaches a temperature profile for AB406 showing that AB406 maintains activity at temperatures of 27.5°C to 40°C. For example, the temperature profile of Kachan shows that AB406 maintains approximately 60% relative activity at 40°C.
The combination of Pramod, UniProt, and Kachan does not teach or suggest the α-amylase of UniProt or AB406 variant of Kachan has a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12. However, according to MPEP 2112.01.I, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structures (i.e., amino acid sequences) disclosed by UniProt and Kachan are substantially identical to the amino acid sequence of SEQ ID NO: 8 of this application, it is presumed that the α-amylase of UniProt and the AB406 variant of Kachan each has a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12.
Therefore, the method of claims 13-19 would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
RESPONSE TO REMARKS: Beginning at p. 7 of the remarks, applicant argues the rejection is obviated by the instant amendment to claim 13 to recite “wherein the protein is a protein having a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12” because the prior art of record does not explicitly or inherently teach or suggest this property of the α-amylase of UniProt/Kachan.
Applicant’s arguments are not found persuasive. According to MPEP 2112, the express, implicit, and inherent disclosures of a prior art reference may be relied upon in a rejection of claims under 35 U.S.C. 103 and according to MPEP 2112.II, there is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference. As such, the cited prior art need not teach or suggest the α-amylases of UniProt/Kachan exhibit the property of “having a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12,” only that the α-amylases of UniProt/Kachan inherently have the property of “having a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12.” According to MPEP 2112.IV, the examiner must provide a rationale or evidence to show inherency and as stated above, since the structures (i.e., amino acid sequences) of the α-amylases of UniProt/Kachan are substantially identical to the structure of the α-amylase recited in the claims, it is presumed that the α-amylases of UniProt/Kachan each has a relative cleaning performance of 1 or more with respect to an amylase consisting of the amino acid sequence of SEQ ID NO: 12. While applicant may argue MPEP 2112.01 is directed to composition, product, and apparatus claims and not method claims, “[t]here is no logical reason why the nesting of a product-by-process limitation within a method…claim should change how novelty of that limitation is evaluated” (Biogen MA Inc. v. EMD Serono, Inc., 976 F.3d 1326 (Fed. Cir. 2020)).
At p. 10 of the remarks, applicant argues the combination of cited prior art fails to teach or suggest deletion of amino acid residues at two or more positions selected from the group consisting of positions R178, G179, T180, and G181, as recited in newly added claims 18 and 19.
Applicant’s arguments are not found persuasive. Contrary to applicant’s arguments, Kachan teaches an AB406 variant with deletion of Arg178-Gly179.
For these reasons, it is the examiner’s position that the method of claims 13-19 would have been prima facie obvious to one of ordinary skill in the art before the effective filing date.
Conclusion
Status of the claims:
Claims 13-19 are pending.
Claims 13-19 are rejected.
No claim is in condition for allowance.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656