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 .
Applicant’s amendment to the claims, filed July 14, 2026, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s amendment to the specification, filed July 14, 2026, is acknowledged.
Applicant’s remarks filed July 14, 2026 in response to the non-final rejection filed May 1, 2026 are acknowledged and have been fully considered.
Claims 1-4, 6-9, and 11-21 are pending in the application.
Claims 5 and 10 have been canceled by applicant’s amendment filed July 14, 2026 and any objections and rejections previously applied to these claims are withdrawn.
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
Claims 12-14, 19, and 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Claims 11 and 21 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected species, there being no allowable generic or linking claim.
Claims 1-4, 6-9, and 15-18 are being examined on the merits only to the extent the claims read on the elected subject matter.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international application PCT/EP2022/054045, filed February 18, 2022, which claims foreign priority under 35 U.S.C. 119(a-d) to European applications 21158484.2 and 21213738.4, filed February 22, 2021 and December 10, 2021, respectively. A certified copy of each of the foreign priority documents has been filed in this application on July 25, 2023. The effective filing date for claims 1-4, 6-9, and 15-18 of this application is February 22, 2021.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on July 14, 2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS has been considered by the examiner.
Specification/Informalities
The use of the term “NCBI,” which is a trade name or a mark used in commerce, has been noted in this application (specification at p. 7, line 6). The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
RESPONSE TO REMARKS: Applicant argues NCBI is not a trademark, however, contrary to applicant’s position, NCBI is a trademark, which can be confirmed by a search for “NCBI” using the Office’s Trademark Search system available at https://tmsearch.uspto.gov/search/search-information. As previously stated, the term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Claim Objections
The objection to claim 1 for reciting “(ii) said variant has at least 60%” is withdrawn in view of applicant’s amendment to claim 1 to recite “(ii) said variant comprises an amino acid sequence having at least 85%.”
The objection to claim 1 for reciting “the amino acid sequence set forth in SEQ ID NO: 1, 3, 4, or in any of SEQ ID NO: 15-41” is withdrawn in view of applicant’s amendment to claim 1 to recite “the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 3.”
The objection to claim 4 for reciting “wherein the variant has at least 85%” is withdrawn in view of applicant’s amendment to claim 1 to recite “wherein the variant comprises an amino acid sequence having at least 90%.”
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.
Claims 1-4, 6-9, and 15-18 are newly rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
This rejection is necessitated by applicant’s amendment to recite “an amino acid substitution at positions 25, 176, and 186” in claim 1.
Claim 1 (claims 2-4, 6-9, and 15-18 dependent therefrom) is confusing in the recitation of “an amino acid substitution at positions 25, 176, and 186” in lines 3-4. The recitation of the singular “an amino acid substitution” implies a single amino acid substitution at position 25, 176, or 186, however, the recitation of “at positions 25, 176, and 186” implies amino acid substitutions at all of the recited positions. In the interest of advancing prosecution, it is suggested that the noted phrase be amended to recite “an amino acid substitution at position 25, 176, or 186” for a single amino acid substitution at the recited position, or “amino acid substitutions at positions 25, 176, and 186” for amino acid substitutions at all of the recited positions.
Claim Rejections - 35 USC § 101
The rejection of claims 1, 2, 4, 6, 7, and 15-18 under 35 U.S.C. 101 is withdrawn in view of applicant’s amendment to claim 1 to limit the substitution positions and to limit the sequence of the variant to comprising an amino acid sequence having at least 85% but less than 100% sequence identity to the recited sequence identifier.
Claim Rejections - 35 USC § 112(a)
The rejection of claims 1-3, 6-9, and 15-18 under 35 U.S.C. 112(a) as failing to comply with the written description requirement is withdrawn in view of applicant’s amendment to claim 1 to limit the sequence of the variant to comprising an amino acid sequence having at least 85% but less than 100% sequence identity to the recited sequence identifier.
Claims 1, 4, 6-9, and 15-18 are newly rejected under 35 U.S.C. 112(a) because the specification, while being enabling for the alpha-amylase variant of claim 1, wherein the variant has alpha-amylase activity, does not reasonably provide enablement for alpha-amylase variants as encompassed by the claims that do not have alpha-amylase activity. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
This rejection is necessitated by applicant’s amendment to claim 1 to delete the phrase “has alpha-amylase activity” in (iii) of claim 1 and to recite “a parent alpha-amylase having alpha-amylase activity” in lines 1-2 of claim 1.
“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.
The breadth of the claims: As amended, the claims are drawn to (in relevant part) an alpha-amylase variant of a parent alpha-amylase having alpha-amylase activity, wherein said variant comprises:
(i) compared to the parent alpha-amylase, an amino acid substitution at position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,
(ii) said variant comprises an amino acid sequence having at least 85% but less than 100% sequence identity with the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 3, and
(iii) said variant comprises a deletion at position 183 and one or more amino acids corresponding to positions selected from the group consisting of 181, 182, and 184, wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
Prior to the instant amendment, claim 1 recited (in relevant part) “(iii) said variant has alpha-amylase activity.” However, by applicant’s instant amendment, the phrase “has alpha-amylase activity” in (iii) of claim 1 has been deleted and the amended claim 1 now recites “a parent alpha-amylase having alpha-amylase activity.” Given a broadest reasonable interpretation, the phrase “having alpha-amylase activity” is interpreted as being in reference to “a parent alpha-amylase” and not the “alpha-amylase variant” and thus, the alpha-amylase variant is not required to have alpha-amylase activity and the claims encompass variants having enzymatic activity other than alpha-amylase activity or non-functional variants.
The state of the prior art; The level of one of ordinary skill; and The level of predictability in the art: According to MPEP 2164.03, “…what is known in the art provides evidence as to the question of predictability” and “[I]f one skilled in the art cannot readily anticipate the effect of a change within the subject matter to which that claimed invention pertains, then there is lack of predictability in the art.”
As evidence of the unpredictability of amino acid modifications, the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892) 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).
The amount of direction provided by the inventor and The existence of working examples: The specification’s disclosed working examples of the claimed alpha-amylase variant have alpha-amylase activity. The specification fails to disclose how to use alpha-amylase variants encompassed by the claims that have enzymatic activity other than alpha-amylase activity or are non-functional variants.
The quantity of experimentation needed to make or use the invention based on the content of the disclosure: While methods of isolating or generating variants of a polypeptide were known in the art at the time of the invention, it was not routine in the art for one of skill in the art to identify or determine a use for alpha-amylase variants encompassed by the claims that have enzymatic activity other than alpha-amylase activity or are non-functional variants.
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 amount of experimentation required, 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 § 102
The rejection of claims 1, 2, 6, and 7 under 35 U.S.C. 102(a)(1) as being anticipated by GenPept Database Accession Number WP_204204294 (February 17, 2021; 1 page; cited on Form PTO-892 filed May 1, 2026; hereafter “GenPept WP_204204294”) is withdrawn in view of applicant’s amendment to claim 1 to limit the sequence of the variant to comprising an amino acid sequence having at least 85% but less than 100% sequence identity” to the recited sequence identifier. GenPept WP_204204294 does not teach or suggest an amino acid sequence that has at least 85% but less than 100% sequence identity to the recited sequence identifier.
The rejection of claims 2 and 4 under 35 U.S.C. 102(a)(1) as being anticipated by Andersen et al. (WO 2014/183921 A1; cited on the IDS filed August 14, 2023; hereafter “Andersen”) is withdrawn in view of applicant’s amendment to claim 2 to limit the amino acid substitutions and applicant’s amendment to claim 4 to limit the sequence of the variant to comprising an amino acid sequence having at least 90% but less than 100% sequence identity” to the recited sequence identifier.
Claims 1, 4, 6-8, and 15-18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Andersen.
This 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) an alpha-amylase variant of a parent alpha-amylase having alpha-amylase activity, wherein said variant comprises:
(i) compared to the parent alpha-amylase, an amino acid substitution at position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,
(ii) said variant comprises an amino acid sequence having at least 85% but less than 100% sequence identity with the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 3, and
(iii) said variant comprises a deletion at position 183 and one or more amino acids corresponding to positions selected from the group consisting of 181, 182, and 184, wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
Prior to the instant amendment, claim 1 recited (in relevant part) “(i) an amino acid alteration at one or more positions corresponding to positions selected from the group consisting of 25… according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,” thus defining the amino acid at position 25 as being relative to the sequence of SEQ ID NO: 3, which has asparagine at position 25, and thereby requiring the variant of claim 1 to have an amino acid other than asparagine at the position corresponding to amino acid 25 of SEQ ID NO: 3. However, by applicant’s instant amendment to recite “(i) compared to the parent alpha-amylase, an amino acid substitution at positions 25…according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,” the amino acid corresponding to position 25 of SEQ ID NO: 3 is now relative to an undefined sequence of a parent alpha-amylase and given a broadest reasonable interpretation, the variant of amended claim 1 can have any amino acid at position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3.
Regarding instant claims 1, 4, 6, and 8, Andersen teaches a polypeptide having alpha-amylase activity comprising an A and B domain and a C domain wherein the amino acid sequence of the A and B domain is SEQ ID NO: 2 and the amino acid sequence of the C domain is SEQ ID NO: 6 (p. 11, line 24 to p. 12, line 9). The amino acid sequence of the alpha-amylase polypeptide of Andersen has 90% sequence identity to instant SEQ ID NO: 1 and SEQ ID NO: 3 (see attached Appendices A and B for sequence alignments between the sequence of the combined SEQ ID NO: 2 and SEQ ID NO: 6 of Anderson with the sequence of instant SEQ ID NO: 1 and SEQ ID NO: 3, respectively). As previously stated, given a broadest reasonable interpretation, the variant of amended claim 1 can have any amino acid at position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3. Also, in the interest of compact prosecution, it is noted that the alpha-amylase polypeptide of Andersen has alanine in place of glycine at the position corresponding to amino acid 186 of SEQ ID NO: 3 (see attached Appendix B for sequence alignment between the sequence of the combined SEQ ID NO: 2 and SEQ ID NO: 6 of Anderson with the sequence of instant SEQ ID NO: 3). Andersen teaches the amylase can be mutated to improve its wash performance and/or stability by deletion of any two of amino acids 181, 182, 183 and 184 such as amino acids 183 and 184 (p. 21, lines 16-19).
Regarding instant claim 7, while Andersen teaches the amylase can be mutated to improve its wash performance and/or stability by deletion of any two of amino acids 181, 182, 183 and 184 such as amino acids 183 and 184 (p. 21, lines 16-19), Anderson does not teach said improved property is expressed as an Improvement Factor (IF) of >1.0. However, according to MPEP 2112.01, 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 structure of the alpha-amylase of Andersen is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of Andersen exhibits the property recited in claim 7.
Regarding instant claims 15-18, Andersen teaches a detergent composition comprising the alpha-amylase (p. 59, lines 13-15), one or more additional enzymes (p. 66, lines 5-8), and a surfactant (p. 60, line 35).
Therefore, Andersen anticipates claims 1, 4, 6-8, and 15-18 as written.
The rejection of claims 1, 4, 6-9, and 15-18 under 35 U.S.C. 102(a)(1) as being anticipated by Jenewein et al. (WO 2021/032881 A1; cited on Form PTO-892 filed May 1, 2026; hereafter “Jenewein”) is withdrawn in view of applicant’s amendments to claims 1 and 4 to delete SEQ ID NO: 4 and 15-41. In view of applicant’s amendments to delete SEQ ID NO: 4 and 15-41, claims 1, 4-9, and 15-18 have an effective filing date of February 22, 2021.
Claims 1, 4, 6-9, and 15-18 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Jenewein.
This rejection has been modified from its previous version to address applicant’s amendment to the claims.
Regarding instant claims 1, 4, 8, and 9, Jenewein teaches an isolated, synthetic, or recombinant hybrid polypeptide having alpha-amylase activity comprising an A and B domain of a first alpha amylase and a C domain of a second alpha amylase (p. 1, lines 17-18). Jenewein teaches preferably, the isolated, synthetic, or recombinant polypeptide having alpha-amylase activity comprises SEQ ID NO: 54 with deletion of one or more amino acids corresponding to positions 181, 182, 183, and 184 of SEQ ID NO: 39 including amino acids 182 and 183 with reference to SEQ ID NO: 39 (p. 52, line 28 to p. 53, line 2). Given that SEQ ID NO: 54 of Jenewein is identical to instant SEQ ID NO: 1 and SEQ ID NO: 39 of Jenewein is identical to instant SEQ ID NO: 3, SEQ ID NO: 54 of Jenewein with deletion of amino acids 182 and 183 with reference to SEQ ID NO: 39 satisfies the structural limitations of (ii) and (iii) of instant claim 1 and the structural limitations of instant claims 4 and 8.
Regarding (i) of claim 1 and the limitations of claim 9, as previously stated, given a broadest reasonable interpretation, the variant of amended claim 1 can have any amino acid at positions 25, 176, and 186 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3.
Regarding instant claim 6, Jenewein teaches deletion of amino acids corresponding to positions 182 and 183 is a stability improving mutation (p. 17, lines 9-11).
Regarding instant claim 7, while Jenewein teaches deletion of amino acids corresponding to positions 182 and 183 is a stability improving mutation (p. 17, lines 9-11), Jenewein does not teach said improved property is expressed as an Improvement Factor (IF) of >1.0. However, according to MPEP 2112.01, 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 structure of the alpha-amylase of Jenewein (i.e., SEQ ID NO: 54 of Jenewein with a deletion of amino acids 181 and 182 or amino acids 182 and 183 with reference to SEQ ID NO: 39) is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of Jenewein exhibits the property recited in claim 7.
Regarding instant claims 15-17, Jenewein teaches the alpha-amylase is used in a detergent formulation (p. 80, lines 30-31) and teaches detergent formulations may comprise one or more surfactants (p. 83, line 27).
Regarding instant claim 18, Jenewein teaches a composition comprising the alpha-amylase, which may include another enzyme (p. 64, lines 3-7).
Therefore, Jenewein anticipates claims 1, 4, 6-9, and 15-18 as written.
RESPONSE TO REMARKS: Applicant argues the amendments overcome the rejections under 35 U.S.C. 102. According to applicant, the claimed alpha-amylase variants are not taught or suggested by the cited prior art and the exemplified alpha-amylase variants demonstrate an improved, unexpected stability that is not taught or suggested by the cited prior art.
Applicant’s arguments are not found persuasive. For reasons stated above, each of Anderson and Jenewein teaches the claimed alpha-amylase variant. To the extent applicant’s argument may be taken as an allegation of unexpected results, it is noted that evidence of secondary considerations, such as unexpected results, is irrelevant to 35 U.S.C. 102 rejections. See MPEP 2131.04.
Claim Rejections - 35 USC § 103
The rejection of claims 8 and 15-18 under 35 U.S.C. 103 as being unpatentable over GenPept WP_204204294 in view of Cascao-Pereira et al. (WO 2013/063460 A2; cited on Form PTO-892 filed May 1, 2026; hereafter “Cascao-Pereira”) is withdrawn in view of applicant’s amendment to claim 1 to limit the sequence of the variant to comprising an amino acid sequence having at least 85% but less than 100% sequence identity” to the recited sequence identifier. The combination of GenPept WP_204204294 and Cascao-Pereira does not teach or suggest an amino acid sequence that has at least 85% but less than 100% sequence identity to the recited sequence identifier.
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Jenewein.
This rejection has been modified from its previous version to address applicant’s amendment to the claims.
Claim 2 is drawn to (in relevant part) the alpha-amylase variant according to claim 1, wherein said variant comprises one or more amino acid substitutions selected from the group consisting of X25H, X25A, X25C, X25D, X25F, X25G, X25K, X25L, X25M, X25Q, X25S, X25W, and X25Y.
The relevant teachings of Jenewein as applied to claims 1, 4, 6-9, and 15-18 are set forth above.
Regarding instant claim 2, Jenewein further teaches a variant of the amylase of SEQ ID NO: 54 comprising a substitution at one or more positions, preferably conservative substitution (p. 24, lines 14-18). Jenewein teaches the amino acid residue at one or more amino acid positions including position 25 according to the numbering of SEQ ID NO: 39 is exchanged (p. 21, line 29 to p. 22, line 9). Jenewein teaches the amino acid changes may be conservative amino acid substitutions (p. 24, lines 7-8), teaches a “conservative mutation” is exchange of one amino acid with a similar amino acid (p. 9, lines 26-27), and teaches similar amino acids (p. 10, top).
Jenewein does not explicitly teach a substitution recited in claim 2.
However, in view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to perform the amino acid substitution taught by Jenewein with a similar amino acid, e.g., substituting asparagine at position 25 of SEQ ID NO: 54 of Jenewein with aspartate, histidine, or serine. One would have been motivated and would have expected success to do so because Jenewein taught a variant of the amylase of SEQ ID NO: 54 comprising a substitution, taught preferred substitution positions including position 25, taught the substitution is a conservative substitution, and taught amino acids that are suitable for a conservative substitution, e.g., Jenewein taught a variant of the amylase of SEQ ID NO: 54, taught asparagine at amino acid position 25 as a preferred substitution position, and taught aspartate, histidine, or serine for a conservative substitution of asparagine.
Therefore, claim 2 would have been obvious to one of ordinary skill in the art before the effective filing date.
RESPONSE TO REMARKS: Applicant argues that claim 2 is dependent from claim 1 and the rejection of claim 2 as being unpatentable over Jenewein should be withdrawn for the same reasons addressing the rejection under 35 U.S.C. 102.
Applicant’s arguments are not found persuasive. For reasons stated above, the alpha-amylase variant of claim 2 would have been obvious in view of Jenewein.
Claim Rejections - 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.
Co-Pending Application No. 19/103,190
Claims 1-4, 6-9, and 15-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5, 7-9, and 11-14 of co-pending application no. 19/103,190 (reference application).
This provisional rejection has been modified from its previous version to address applicant’s amendment to the claims.
Regarding instant claims 1 and 4, claim 1 of the reference application recites (in relevant part) an amylase variant of a parent amylase, wherein said amylase variant
(i) comprises an amino acid substitution at position 4 according to the numbering of SEQ ID NO: 3,
(ii) comprises an amino acid substitution at amino acid position corresponding to amino acid position 25 according to the numbering of SEQ ID NO: 3, and
(iii) has at least 60%, but less than 100% sequence identity with SEQ ID NO: 1; and
claim 7 of the reference application recites the amylase variant according to claim 1, further comprising a deletion at one or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of two or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of amino acids corresponding to positions 181 and 182, 182 and 183, or 183 and 184, wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
SEQ ID NO: 3 of the reference application is identical to instant SEQ ID NO: 3 and SEQ ID NO: 1 of the reference application is identical to instant SEQ ID NO: 1.
Regarding instant claims 2 and 3, claim 5 of the reference application recites (in relevant part) the amylase variant according to claim 1,
wherein said amylase variant comprises
a) a substitution at one or more positions selected from 25, 176, and 186; optionally one or more substitutions selected from X25H, X176K, and X186E.
Regarding instant claim 6, claim 9 of the reference application recites the amylase variant according to claim 1, wherein the amylase variant exhibits improved storage stability and/or improved wash performance, optionally the amylase variant exhibits improved storage stability in a detergent composition.
Regarding instant claim 7, while claim 9 of the reference application recites the amylase variant according to claim 1, wherein the amylase variant exhibits improved storage stability and/or improved wash performance, optionally the amylase variant exhibits improved storage stability in a detergent composition, the claims of the reference application do not recite said improved property is expressed as an Improvement Factor (IF) of >1.0. However, according to MPEP 2112.01, 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 structure of the alpha-amylase of the claims of the reference application is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of the claims of the reference application exhibit the property recited in claim 7.
Regarding instant claim 8, claim 7 of the reference application recites the amylase variant according to claim 1, further comprising a deletion at one or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of two or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of amino acids corresponding to positions 181 and 182, 182 and 183, or 183 and 184, wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
Regarding instant claim 9, claim 8 of the reference application recites (in relevant part) the amylase variant according to claim 1, wherein the amylase variant has at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, or at least 99.5%, but less than 100% sequence identity to SEQ ID NO: 1. Polypeptide sequences within the recited ranges of claim 8 of the reference application have the number of substitutions recited in instant claim 9.
Regarding instant claim 15, claim 11 of the reference application recites a composition comprising the amylase variant according to claim 1 and at least one additional component.
Regarding instant claim 16, claim 13 of the reference application recites the composition according to claim 11, wherein the composition is a detergent composition, optionally a laundry detergent composition or a hard surface cleaning detergent composition.
Regarding instant claim 17, claim 14 of the reference application recites the composition according to claim 11, wherein composition comprises one or more surfactants and/or one or more builders, optionally one or more strong sequestering builders.
Regarding instant claim 18, claim 12 of the reference application recites the composition according to claim 11, wherein the composition comprises one or more second enzyme different from the amylase variant, optionally one or more second enzyme selected from the group consisting of proteases, second amylases, lipases, cellulases, hemicellulases, mannanases, xylanases, DNases, dispersins, pectinases, oxidoreductases, and cutinases.
Therefore, claims 1-4, 6-9, and 15-18 of this application are unpatentable over claims 1, 5, 7-9, and 11-14 of the reference application.
U.S. Patent No. 12,595,471 B2
Claims 1, 4, 6-9, 15, and 18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 (cited on the attached Form PTO-892).
This rejection has been modified from its previous version to address applicant’s amendment to the claims.
Regarding instant claims 1, 4, 8, and 9, claim 1 of the patent recites an isolated, synthetic, or recombinant polypeptide having alpha-amylase activity comprising an A and B domain and a C domain wherein the amino acid sequence of the A and B domain is at least 90% identical to the amino acid sequence of SEQ ID NO: 42 and the amino acid sequence of the C domain is at least 90% identical to the amino acid sequence of SEQ ID NO: 44;
claim 11 of the patent recites (in relevant part) the polypeptide according to claim 1 comprising a deletion of one or more amino acids corresponding to positions 181, 182, 183 and 184 corresponding to the numbering of SEQ ID NO: 39; and
claim 13 of the patent recites the polypeptide according to claim 1 comprising: an amino acid sequence having at least 90% sequence identity to SEQ ID NO:54.
SEQ ID NO: 39 of the patent is identical to instant SEQ ID NO: 3 and SEQ ID NO: 54 of the patent is identical to instant SEQ ID NO: 1. As such, the alpha-amylase polypeptide of the claims of the patent comprising the amino acid sequence of SEQ ID NO:54 and comprising a deletion of amino acid position 183 corresponding to the numbering of SEQ ID NO: 39 satisfies the structural limitations of (ii) and (iii) of instant claim 1 and the structural limitations of instant claims 4 and 8.
Regarding (i) of claim 1 and the limitations of claim 9, as previously stated, given a broadest reasonable interpretation, the variant of amended claim 1 can have any amino acid at positions 25, 176, and 186 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3.
Regarding instant claim 6, claim 14 of the patent recites the polypeptide according to claim 1, wherein the amylase has an increase in expression, activity, thermostability, stability, performance in laundry, specific activity, substrate specificity, pH-dependent activity, pH-dependent stability, oxidative stability, Ca2+ dependency, or any combination thereof compared to the amylase having the amino acid sequence of SEQ ID NO: 39 or SEQ ID NO: 40.
Regarding instant claim 7, while claim 6 of the patent recites the amylase variant according to claim 1, wherein the amylase has an increase in expression, activity, thermostability, stability, performance in laundry, specific activity, substrate specificity, pH-dependent activity, pH-dependent stability, oxidative stability, Ca2+ dependency, or any combination thereof compared to the amylase having the amino acid sequence of SEQ ID NO: 39 or SEQ ID NO: 40, the claims of the patent do not recite said improved property is expressed as an Improvement Factor (IF) of >1.0. However, according to MPEP 2112.01, 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 structure of the alpha-amylase of the claims of the patent is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of the claims of the patent exhibit the property recited in claim 7.
Regarding instant claims 15 and 18, claim 15 of the patent recites a composition comprising the isolated, synthetic, or recombinant polypeptide having alpha-amylase activity according to claim 1; and
claim 16 of the patent recites the composition of claim 15, further comprising at least one second enzyme selected from the group consisting of: a second amylase, a lipase, a protease, a cellulase, a laccase, a mannanase, a pectinase, xylanase, and a nuclease.
Therefore, claims 1, 4, 6-9, 15, and 18 of this application are unpatentable over claims 1, 11, and 13-16 of the patent.
Claims 2, 16, and 17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 as applied to claims 1, 4, 6-9, 15, and 18 in view of Jenewein.
This rejection has been modified from its previous version to address applicant’s amendment to the claims.
The claims of the patent do not recite the limitations of instant claims 2, 16, and 17.
Regarding instant claim 2, Jenewein teaches a variant of the amylase of SEQ ID NO: 54 comprising a substitution at one or more positions, preferably conservative substitution (p. 24, lines 14-18). SEQ ID NO: 54 of the patent is identical to SEQ ID NO: 54 of Jenewein. Jenewein teaches (in relevant part) the amino acid residue at position 25 according to the numbering of SEQ ID NO: 39 is exchanged (p. 21, line 29 to p. 22, line 9). SEQ ID NO: 39 of the patent is identical to SEQ ID NO: 39 of Jenewein. Jenewein teaches the amino acid changes may be conservative amino acid substitutions (p. 24, lines 7-8), teaches a “conservative mutation” is exchange of one amino acid with a similar amino acid (p. 9, lines 26-27), and teaches similar amino acids (p. 10, top).
In view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the alpha-amylase of the claims of the patent by performing the amino acid substitution taught by Jenewein with a similar amino acid, e.g., substituting asparagine at position 25 of SEQ ID NO: 54 with aspartate, histidine, or serine. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase having at least 90% sequence identity to SEQ ID NO:54 and Jenewein taught the following: a variant of the amylase of SEQ ID NO: 54 comprising a substitution, preferred substitution positions, the substitution is a conservative substitution, and amino acids that are suitable for a conservative substitution, e.g., Jenewein taught a variant of the amylase of SEQ ID NO: 54, taught asparagine at amino acid position 25 as a preferred substitution position, and taught aspartate, histidine, or serine for a conservative substitution of asparagine.
Regarding instant claims 16 and 17, as stated above, claim 14 of the patent recites (in relevant part) the polypeptide according to claim 1, wherein the amylase has an increase in performance in laundry.
Jenewein teaches the alpha-amylase is used in a detergent formulation (p. 80, lines 30-31) and teaches detergent formulations may comprise one or more surfactants (p. 83, line 27).
In view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to include the alpha-amylase of the claims of the patent in a detergent composition of Jenewein. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase that has an increase in performance in laundry, and Jenewein taught the alpha-amylase is used in a detergent formulation with one or more surfactants.
Therefore, claims 2, 16, and 17 of this application are unpatentable over claims 1, 11, and 13-16 of the patent in view of Jenewein.
Claims 16 and 17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 as applied to claims 1, 4, 6-9, 15, and 18 in view of Cascao-Pereira.
This rejection has been modified from its previous version to address applicant’s amendment to the claims.
Regarding instant claims 16 and 17, as stated above, claim 14 of the patent recites (in relevant part) the polypeptide according to claim 1, wherein the amylase has an increase in performance in laundry.
The claims of the patent do not recite the limitations of instant claims 16 and 17.
Cascao-Pereira teaches alpha-amylases have been used for a variety of different purposes and can be used to remove starchy soils and stains during laundry washing (paragraphs [005] and [00223]). Cascao-Pereira teaches an alpha-amylase can be used as a component in a detergent composition (paragraphs [00225] and [00228]) with one or more surfactants (paragraph [00227]).
In view of the teachings of Cascao-Pereira, it would have been obvious to one of ordinary skill in the art before the effective filing date to include the alpha-amylase of the claims of the patent in a detergent composition of Cascao-Pereira. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase that has an increase in performance in laundry, and Cascao-Pereira taught alpha-amylases can be used to remove starchy soils and stains during laundry washing and taught a detergent composition including alpha-amylase and one or more surfactants for laundry washing.
Therefore, claims 16 and 17 of this application are unpatentable over claims 1, 11, and 13-16 of the patent in view of Cascao-Pereira.
RESPONSE TO REMARKS: Applicant argues the amendments overcome the rejections.
Applicant’s arguments are not found persuasive. For reasons stated above, claims of this application are unpatentable over the claims of the reference application or patent.
Conclusion
Status of the claims:
Claims 1-4, 6-9, and 11-21 are pending.
Claims 11-14 and 19-21 are withdrawn.
Claims 1-4, 6-9, and 15-18 are rejected.
No claim is in condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, MANJUNATH N RAO can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
Query Match 90.4%; Score 2418; DB 1; Length 483;
Best Local Similarity 89.4%;
Matches 432; Conservative 26; Mismatches 25; Indels 0; Gaps 0;
Qy 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLNSDASNLKSKGITAVWIPPAWKGASQNDVGYGA 60
||||||||||||||||||||||||||| ||||||| ||||||||||||||||||||||||
Db 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLRSDASNLKDKGITAVWIPPAWKGASQNDVGYGA 60
Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLQAAVTSLKNNGIQVYGDVVMNHKGGADATEMVRAV 120
||||||||||||||||||||||:|||||||:||:||||||||||||||||||||| ||||
Db 61 YDLYDLGEFNQKGTVRTKYGTRNQLQAAVTALKSNGIQVYGDVVMNHKGGADATEWVRAV 120
Qy 121 EVNPNNRNQEVTGEYTIEAWTRFDFPGRGNTHSSFKWRWYHFDGVDWDQSRRLNNRIYKF 180
||||:||||||:|:|||||||:|||||||||||:|||||||||||||||||:| ||||||
Db 121 EVNPSNRNQEVSGDYTIEAWTKFDFPGRGNTHSNFKWRWYHFDGVDWDQSRQLQNRIYKF 180
Qy 181 RGKAWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKHIK 240
||| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RGKGWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKHIK 240
Qy 241 YSFTRDWINHVRSATGKNMFAVAEFWKNDLGAIENYLQKTNWNHSVFDVPLHYNLYNASK 300
|||||||: |||: |||||||||||||||:||||||| |||||||||||||||||||||:
Db 241 YSFTRDWLTHVRNTTGKNMFAVAEFWKNDIGAIENYLSKTNWNHSVFDVPLHYNLYNASR 300
Qy 301 SGGNYDMRNIFNGTVVQRHPSHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTREQG 360
|||||||| |||||||||||:||||||||||||||||||||||||||||||||||||:||
Db 301 SGGNYDMRQIFNGTVVQRHPTHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRDQG 360
Qy 361 YPSVFYGDYYGIPTHGVPAMRSKIDPILEARQKYAYGTQHDYLDNQDVIGWTREGDSAHA 420
||||||||||||||||||||:|||||||||||||||||| ||||: |||||||||| ||
Db 361 YPSVFYGDYYGIPTHGVPAMKSKIDPILEARQKYAYGTQRDYLDHPDVIGWTREGDGVHA 420
Qy 421 GSGLATVMSDGPGGSKTMYVGTAHAGQVFKDITGNRTDTVTINSAGNGTFPCNGGSVSIW 480
|||||:||||||||| | || :||:|: |||||:|:||||| | | | :||||||:
Db 421 DSGLATLMSDGPGGSKWMEVGKNNAGEVWYDITGNQTNTVTINKDGWGQFHVSGGSVSIY 480
Qy 481 VKQ 483
|:|
Db 481 VQQ 483
APPENDIX B
Query Match 90.2%; Score 2413; DB 1; Length 485;
Best Local Similarity 89.0%;
Matches 430; Conservative 28; Mismatches 23; Indels 2; Gaps 1;
Qy 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLNSDASNLKSKGITAVWIPPAWKGASQNDVGYGA 60
||||||||||||||||||||||||||| ||||||| ||||||||||||||||||||||||
Db 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLRSDASNLKDKGITAVWIPPAWKGASQNDVGYGA 60
Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLQAAVTSLKNNGIQVYGDVVMNHKGGADATEMVRAV 120
||||||||||||||||||||||:|||||||:||:||||||||||||||||||||| ||||
Db 61 YDLYDLGEFNQKGTVRTKYGTRNQLQAAVTALKSNGIQVYGDVVMNHKGGADATEWVRAV 120
Qy 121 EVNPNNRNQEVTGEYTIEAWTRFDFPGRGNTHSSFKWRWYHFDGVDWDQSRRLNNRIYKF 180
||||:||||||:|:|||||||:|||||||||||:|||||||||||||||||:| ||||||
Db 121 EVNPSNRNQEVSGDYTIEAWTKFDFPGRGNTHSNFKWRWYHFDGVDWDQSRQLQNRIYKF 180
Qy 181 R--GKAWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKH 238
| || ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RGDGKGWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKH 240
Qy 239 IKYSFTRDWINHVRSATGKNMFAVAEFWKNDLGAIENYLQKTNWNHSVFDVPLHYNLYNA 298
|||||||||: |||: |||||||||||||||:||||||| ||||||||||||||||||||
Db 241 IKYSFTRDWLTHVRNTTGKNMFAVAEFWKNDIGAIENYLSKTNWNHSVFDVPLHYNLYNA 300
Qy 299 SKSGGNYDMRNIFNGTVVQRHPSHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRE 358
|:|||||||| |||||||||||:||||||||||||||||||||||||||||||||||||:
Db 301 SRSGGNYDMRQIFNGTVVQRHPTHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRD 360
Qy 359 QGYPSVFYGDYYGIPTHGVPAMRSKIDPILEARQKYAYGTQHDYLDNQDVIGWTREGDSA 418
||||||||||||||||||||||:|||||||||||||||| |:||||: ::|||||||::|
Db 361 QGYPSVFYGDYYGIPTHGVPAMKSKIDPILEARQKYAYGKQNDYLDHHNMIGWTREGNTA 420
Qy 419 HAGSGLATVMSDGPGGSKTMYVGTAHAGQVFKDITGNRTDTVTINSAGNGTFPCNGGSVS 478
| |||||:|||||||:| |||| ||||::||||||: |||||: | | | ||||||
Db 421 HPNSGLATIMSDGPGGNKWMYVGRNKAGQVWRDITGNRSGTVTINADGWGNFSVNGGSVS 480
Qy 479 IWV 481
|||
Db 481 IWV 483
Prosecution Insights