DETAILED ACTION
Objections and rejections raised in prior Office Actions are withdrawn unless restated below.
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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 04/13/2026 has been entered.
Claim Interpretation
Claim 16 is directed towards a product wherein embodiment alpha-amylase variants are not required to be made by any process nor from any specific “parent alpha-amylase” or any “parent” alpha-amylase at all. See MPEP 2113(I). For example, an embodiment of claim 16 can be made from solid phase peptide synthesis without involvement of DNA nor a living host cell. As such, the parent alpha-amylase recited in claim 16 does not define the scope of the embodiments of the claim 16 except for providing a reference for which a required improved performance is evaluated. In this regards, the “parent” alpha-amylase can be any second alpha-amylase including an alpha amylase that is itself an embodiment alpha-amylase variant of claim 16. For example, if an embodiment of claim 16 is identical to SEQ ID NO: 1 with amino acid residues T118 and F242, the following (and many more) are all parent alpha-amylases:
-any of SEQ ID NO: 1-5.
-an alpha-amylase with 90% identity to any of SEQ ID NO: 1-5,
-an alpha-amylase with 99% identity to any of SEQ ID NO: 1-5.
-an alpha-amylase with less than 90% identity to SEQ ID NO: 1-5 wherein such amylase can be modified to have at least 90% identity to any of SEQ ID NO: 1-5.
The above discussion is to emphasize that a parent alpha-amylase is a broad genus of alpha-amylases for any one embodiment of claim 16 (and dependent claims). This interpretation of the claims is reinforced by claim 23 reciting that a parent alpha-amylase can have at least 90% identity to SEQ ID NOS: 1-5, which encompasses a very large number of individual parent species. A parent alpha-amylase is not defined as an alpha-amylase that is otherwise identical except for having specifically recited substitutions or having specific residues present in lieu of the for example T118 and F242. That is, a parent alpha amylase can have A, C, D, E, F, G, Q, Y, etc., present at position 118 and is not required to have a residue present at position 118 of any of SEQ ID NOS: 1-5.
Claim Rejections - 35 USC § 112
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 16-23 and 26-29 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 16 recites “Improvement Factor (IF) > 1.0, when compared to said parent alpha-amylase. The Claim Interpretation set forth above is interpreted above. As stated above, for any specific embodiment alpha-amylase variant of claim 16, a “parent alpha-amylase” is a broad genus of alpha-amylases for any one embodiment of claim 16 (and dependent claims). That is, if a specific embodiment of claim 16 is SEQ ID NO: 1 with modifications H1*+ G7A+R180*+S181*+ D118T+Y242F+E259G+N279S+G303R+E390A +G475K, a “parent alpha-amylase” can be any of SEQ ID NOS: 1-5 plus any number of additional polypeptides that can be a parent that can including 1000’s, 10,000’s or even more polypeptide that can be considered to be a parent alpha-amylase or “said parent polypeptide.” Since claim 16 recites IF>1.0, such claim terms is required to be definite. The specification, in Example 2, appears to define IF as:
Improvement Factor (IF)=[Specific Activity of Hybrid polypeptide]/[Specific Activity of parent polypeptide (alpha-amylase)]
The above is understood as stating that any particular embodiment has one value for IF, or at least a limited number of values of IF. However, in order for there to be one value of IF, the ratio defining IF has to be calculated with a specific activity of a specific parent polypeptide such that one value of IF is calculable. However, as discussed, a parent alpha-amylase or polypeptide is a diverse genus of polypeptides since embodiments of the claims are not required to be made by any specific process or from any parent polypeptide at all. See MPEP 2113(I). For example, if a specific embodiment of claim 16 is SEQ ID NO: 1 with modifications H1*+ G7A+R180*+S181*+ D118T+Y242F+E259G+N279S+G303R+E390A +G475K, a different value of IF will be obtained for each of parent polypeptides of SEQ ID NOS: 1-5. Claim 23 includes parent-alpha amylases with at least 90% identity to any of SEQ ID NOS: 1-5 which covers alpha-amylase with a broad diversity of activities. That is, for any specific embodiment of claim 16 for an alpha-amylase variant, an unlimited number of IF values can be calculated since the identity of a parent alpha-amylase or polypeptide is arbitrary. For this reason, an ordinarily skilled artisan is unable to determine how to avoid infringement of IF>1.0 in the absence of any specific parent alpha-amylase or polypeptide (or small set of such parent-alpha amylases) required for calculating value of IF.
Regarding claim 26, in view of the working examples of the specification, practice of claim 26 includes, but is not limited to, expression of a heterologous nucleotide with a predefined sequence encoding a variant alpha-amylase, producible by any method, and expressing such heterologous nucleotide in a host cell to produce a variant alpha-amylase. Practice of claim 26 does not require that any specific mutagenesis procedure be performed on any specific polynucleotide encoding a parent alpha-amylase. Practice of claim 26 does not requiring the direct performance of any act on a parent alpha-amylase polypeptide to directly transform the same into a variant polypeptide. The scope of “introducing a substitution . . . into the parent alpha-amylase” includes producing an encoding polynucleotide (by any method) that is different from the parent alpha-amylase including by solid state synthesis of such polynucleotide without use of any starting or pre-existing polypeptide encoding a parent alpha-amylase. However, just as in claim 16 discussed above, such parent alpha-amylase includes at least any alpha-amylase having at least 90% identity to one of SEQ ID NOS: 1-5 (and additional alpha-amylases) as to encompass many 1000’s of species. As such, since claim 26 requires “said variant has . . . improved wash performance to said parent polypeptide,” the parent polypeptide to which such improved wash performance is evaluated is a genus of alpha-amylases that encompasses many 1000’s of species such that an ordinarily skilled artisan cannot determine how to avoid infringement of claim 26.
Claim 24 is excluded from this rejection since claim 24 is considered to be met if an increased IF is met relative to any of SEQ ID NOS: 1-3. In evaluating the meaning of IF, in Example 2 of the specification, “specific activity” is understood as a general increase in activity per amount of enzyme on starch substrates rather than tied to a specific assays, which is deemed to have a reasonable certainty of meaning in the art.
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 16-21 and 23-29 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 5, 6, 8, 9 and 19 of copending Application No. 17/841,161 in view of Kaasgaard et al. (U.S. 2014/0141489 A1).
SEQ ID NOS: 1 and 2 as recited and SEQ ID NOS: 1 and 2 of the copending claims are identical.
Copending claims in part recite:
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As such, at least copending claims 9 and 19 are considered to directly anticipate or suggest a variant alpha-amylase having over 99% identity to recited SEQ ID NO: 2 with substitution D118T and Y242F and having improved IF relative to SEQ ID NO: 2 as a parent enzyme as to meet the features of claims 16-20, 23, 24 and 27.
Regarding claim 21, a combination of the modifications recited in copending claim 1 and D118T as recited in copending claims 1 and 19 yields a combination of H1*+G7A+R180*+S181*+D118T+Y242F+E259G+N279S+G303R+E290A+G475K as to directly anticipate or suggest claim 21. Copending claims 5, 6 and 8 further recite D118T.
Regarding claims 28 and 29, the copending claims do not directly recite the composition of copending claims 9 and 19 are a liquid or liquid laundry composition.
Kaasgaard, et al., abstract:
The present invention relates to variants of a parent alpha-amylase. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.
Kaasgaard, in the claims, state:
1. An isolated variant of a parent alpha-amylase, comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity.
7. The variant according to claim 1, which comprises substitutions at two, three or four positions selected from the group consisting of G304R, W140YF, E260 GHIKNRTY and G476EK.
SEQ ID NO: 1 of Kaasgaard is over 95% identical to recited SEQ ID NO: 1
Example 1B of Kaasgaard describes that it is appropriate to include any alpha-amylase disclosed in a heavy duty liquid detergent composition. “According to the invention, the above alpha-amylase variants may typically be a component in a cleaning composition, such as a detergent composition, e.g., a laundry detergent composition or a dishwashing detergent composition. Especially preferred is a liquid laundry detergent composition.” Kaasgaard, para. [0235]. As such, at the time of filing, an ordinarily skilled artisan would have understood that it is appropriate and advantageous to formulate any cleaning composition including an amylase having a significant similarity to recited SEQ ID NO: 1 (i.e. over 95% identity thereto) as a liquid laundry detergent composition, which includes formulating the cleaning composition of the copending claims (including copending claims 9 and 19) as a liquid laundry composition.
Regarding claims 25 and 26, claim 22 of Kaasgaard teaches:
22. A method for obtaining a variant of a parent alpha-amylase, comprising introducing into the parent alpha-amylase an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion and the variant has alpha-amylase activity; and recovering the variant.
An ordinarily skilled artisan at time of filing would have understood that the method outlined in claim 22 of Kaasgaard is an appropriate and effective means of obtaining an producing any variant alpha-amylases including alpha-amylases as recited in copending claims 9 and 19, such that Kaasgaard suggests an appropriate and effective means of obtaining an producing any variant alpha-amylases including alpha-amylases as recited in copending claims 9 and 19 is to introduce into an alpha-amylases of recited SEQ ID NO: 2 that alterations/substitutions/modifications of H1*+G7A+R180*+S181*+D118T+Y242F+E259G+N279S+G303R+E290A+G475K to SEQ ID NO: 2 to produce a variant alpha-amylase that has improved wash performance by means of an IF>1.0 as to meet the features of claims 25 and 26.
This is a provisional nonstatutory double patenting rejection.
Response to arguments
In brief, applicant references amendments made to the claims to address rejections under 112(b) and for double patenting. However, applicant provides no explanation regarding how such amendments address the rejections above.
Examiner’s comment regarding prior art
It is noted that recites SEQ ID NOS: 2-4 all appear to have at least about 90% identity to recited SEQ ID NO: 1.
Regueira et al. (U.S. 2018/0371441 A1) in the claims teaches:
1. A polypeptide comprising a variant amino acid sequence of SEQ ID NO: 1, wherein the polypeptide has alpha-amylase activity and exhibits an enhanced wash performance compared to the polypeptide of SEQ ID NO: 1.
12. A polypeptide according to claim 1, wherein said polypeptide comprises one or more of the following substitutions relative to the amino acid sequence of SEQ ID NO:2; M10L, N25K, D30N, K37H, K37L, K37M, K37R, K37V, S40T, W48F, A51Q, A51T, N54S, Y64W, T81S, Q86H, Q86I, Q86L, K93H, K93R, Q98R, M105Y, M105F, M105I, M105L, K108R, G109A, G109M, A113E, M116I, M116L, M116A, M116V, M116F, K118Q, K118H, K118N, K118R, E121H, E130H, E130Q, Y135H, E138Q, K142R, K142Q, W167Y, W167H, N174Q, N174*, N175Q, Y178W, T182G, A186D, A186G, W187Y, W189H, F195N, Y198F, L202M, Y203H, Y203N, Y203G, Y203F, 1206L, M208F, M208L, M208V, H210N, V214R, V214T, V214I, R218N, I235V, I235L, I235M, V238T, V238A, K242P, Y243F, Y243M, T246V, T246I, T246L, T246M, R247K, I250L, I250V, S255K, I257A, K259N, N260D, M261L, M261A, A265G, F267Y, K269S, K269N, N270G, A274K, I275L, E276Q, K281H, F295Y, F295W, Y298W, Y298F, Y299W, Y299F, Q311T, Q311H, Q311R, Q319H, Q319R, K320H, K320R, S334T, S339A, E360F, S365M, S365C, V366I, K383Q, K383R, S384E, K385H, K385Q, K385R, Q394K, Y398W, N402Y, Y404W, E416L, A434D, G460E, W469F, V474C, and W482Y, wherein numbering is according to the amino acid sequence set forth in SEQ ID NO: 2.
Recited SEQ ID NO: 1 and SEQ ID NO: 1 of Regueira are about 85% identical; position Y243 of Regueira corresponds to position 242 of recited SEQ ID NO: 1. While Regueira suggest substitutions at positions 118 and 242/243, Regueira does not sufficiently suggest the specific combination of substitutions 118T and 242F nevertheless that the same be made in an alpha-amylase having at least 90% identity to one of SEQ ID NOS: 1-5.
It is further noted that amylases are described in the prior art having amino acid residues 118T and 242F according to numbering of recited SEQ ID NO: 1. Borchert et al. (U.S. 2001/0039253 A1), in Fig. 1, describe several naturally-occurring alpha-amylases, includes SEQ ID NOS: 4 and 5 thereof that have amino acids T and F at positions corresponding to positions 118 and 242, respectively, of recited SEQ ID NO: 1. However, SEQ ID NOS: 4 and 5 of Borchert have only about 75% identity with any of recited SEQ ID NOS: 1-5. There is no apparent motivation to make the specific combination of substitutions 118T and 242F in an alpha-amylase having at least 90% identity to one of recited SEQ ID NOS: 1-5.
Conclusion
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652
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