The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
This office action is in response to Applicants’ amendments/remarks received January 16, 2026.
Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Claims 2-3, 6-9 are canceled. Claims 10-11, 16 are withdrawn. Claims 1, 4-5, 12-15 are under consideration.
Priority: This application is a CON of PCT/US2020/066287, filed December 21, 2020, which claims benefit of foreign application EP 19219568.3, filed December 23, 2019. A copy of the foreign priority document has been received in the instant application on August 1, 2022 and is in the English language.
Objections and Rejections
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 4-5, 12-15 are rejected under 35 U.S.C. 103 as being unpatentable over Beier II (EP 3476935A1; IDS 09.08.22, previously cited) in view of Gori (WO 2018184816; IDS 09.08.22, previously cited). Beier II discloses a detergent composition comprising a DNase variant and an adjunct and one or more enzymes such as mannanase, where the DNase variant comprises a variant of SEQ ID NO: 1 (at least paragraphs 0228-0231, p. 56 lines 4-10), where SEQ ID NO: 1 of Beier II is the DNase of Bacillus cibi (at least paragraph 0012). Beier II discloses DNase and DNase variants means a polypeptide with DNase activity (at least paragraph 0022). Beier II discloses DNase variants in a detergent composition, including a DNase variant of the polypeptide of SEQ ID NO: 1 comprising the substitutions T1I, S13Y, T22P, S27L, L33K, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 73 lines 29-32). Therefore, Beier II can be deemed to disclose a cleaning composition comprising a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36. Beier II further discloses the adjunct is a surfactant (at least paragraphs 0004,0021, 0043, 0228-0230). Beier II differs from the claimed cleaning composition by not explicitly reciting the mannanase amino acid sequence.
Gori discloses a cleaning composition comprising a mixture of enzymes, including a DNase and at least one carbohydrase being mannanase, and a cleaning component (at least p. 1 lines 33-37). Gori et al. disclose the DNase means a polypeptide with DNase activity (p. 3-4). Gori et al. disclose the mannanase is a mannanase of Family 5 or 26 (p. 26 lines 13-14), the mannanase comprises the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15.
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the mannanase polypeptide of Gori et al. for the mannanase enzyme in the cleaning composition comprising the DNase variant and surfactant of Beier II noted above because the prior art disclose combining DNase enzymes and mannanase enzymes to formulate a cleaning composition (instant claims 1, 5). One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Regarding instant claim 4, Beier II discloses the DNase variant is in a concentration in the range of 0.001-100 ppm, 0.001-1000 ppm enzyme protein (at least paragraphs 0145, 0235) and that the amount of the additional enzyme(s) is compatible with the other enzymatic ingredients and present in effective amounts (at least paragraphs 0254-0255), where compatible amounts would include the amounts present for DNase enzymes, including the noted ranges of 0.001-100 ppm, 0.001-1000 ppm enzyme protein. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). MPEP 2144.05. Therefore, it would have been obvious to arrive at the recited DNase present in an amount 0.01 to 1000 ppm and the recited at least one mannanase present in an amount 0.01 to 1000 ppm by routine optimization.
Regarding instant claim 12, as noted above, Beier II discloses a DNase variant of the polypeptide of SEQ ID NO: 1 comprising the substitutions T1I, S13Y, T22P, S27L, L33K, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 73 lines 29-32).
Regarding instant claim 13, Beier II discloses the detergent adjunct comprises an anionic surfactant to nonionic surfactant in a weight ratio from 25:1 to 1:2 (at least paragraph 0230).
Regarding instant claim 14, Beier II discloses the detergent composition further comprises additional enzymes selected from pectinases, pectin lyases, xanthanases, catalases, laccases (at least paragraphs 0231, 0254).
Regarding instant claim 15, Beier II discloses the detergent composition is in the form of a liquid laundry composition (at least paragraph 0021).
Reply: In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection as being anticipated by Beier II has been withdrawn. However, Beier II is maintained as a 103 reference in view of Gori et al. for the reasons noted above.
Applicants assert that Beier II does not identify Applicants’ SEQ ID-anchored mannanases.
Applicants’ remarks are not persuasive. The deficiency of Beier II to not explicitly teach a mannanase amino acid sequence is remedied by Gori et al., which disclose mannanases known in the art used in cleaning compositions comprising a polypeptide having DNase activity and an adjunct, such as the cleaning compositions disclosed in Beier II, include a mannanase of Family 5 or 26 (p. 26 lines 13-14), the mannanase comprises the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15. Therefore, it would be obvious to one of ordinary skill that the mannanase polypeptide of Gori et al. can be incorporated as the mannanase enzyme in the cleaning composition comprising the DNase variant and surfactant of Beier II noted above because the prior art disclose combining DNase enzymes and mannanase enzymes to formulate a cleaning composition.
Applicants assert in addition, instant claim 1 excludes SEQ ID NO: 36 (“with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36”). Applicants assert that Beier II does not disclose this negative limitation.
Applicants’ remarks are not persuasive. As noted in the 103 rejection above, Beier II discloses DNase variants in a detergent composition, including a DNase variant of the polypeptide of SEQ ID NO: 1 comprising the substitutions T1I, S13Y, T22P, S27L, L33K, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 73 lines 29-32). Therefore, Beier II can be deemed to disclose a cleaning composition comprising a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36.
Applicants assert that Beier II in view of Gori et al. do not disclose or suggest the precise pairing of structure-constrained enzymes, nor do they provide an articulated reasoning or motivation to select Lys33, as recited in claim 12, specifically together with sequence identity thresholds for the required DNase and mannanases.
Applicants’ remarks are not persuasive. The claimed composition essentially comprises the combination of a protein or polypeptide having DNase activity and a protein having mannanase activity, regardless of the recited sequence identity thresholds. In this instance, Beier II already discloses a detergent composition or cleaning compositions comprising a DNase variant, a mannanase, and a surfactant, which is the same combination and the same types of enzymes and adjunct recited in the instant composition. Beier II further discloses a DNase variant of the polypeptide of SEQ ID NO: 1 comprising the substitutions T1I, S13Y, T22P, S27L, L33K, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 73 lines 29-32), which are the amino acid residues recited in instant claim 12. Gori et al. disclose known mannanase enzymes for incorporation in cleaning compositions comprising a polypeptide having DNase activity and an adjunct, such as the cleaning compositions disclosed in Beier II, which comprise a DNase variant and an adjunct. Therefore, one of ordinary skill would have a reasonable expectation of success that the mannanase enzymes of Gori et al., including the mannanase comprising the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15, can be incorporated as the mannanase enzyme in the cleaning composition comprising the DNase variant and surfactant of Beier II noted above because the prior art disclose the same combination of polypeptides having DNase activity and mannanase enzymes together to form a cleaning composition, where the polypeptides of the prior art having DNase activity and mannanase activity further meet the recited sequence identity thresholds.
Therefore, Applicants’ remarks that a person having ordinary skill would not reasonably expect success with the recited enzyme combination are not persuasive.
Claims 1, 4-5, 13-15 are rejected under 35 U.S.C. 103 as being unpatentable over Beier I (WO 2018011277; previously cited) in view of Gori (WO 2018184816; IDS 09.08.22, previously cited). Beier I discloses Bacillus Cibi DNase variants suitable for use in cleaning compositions, e.g. detergent compositions (at least abstract, p. 2 lines 3-4, p. 17 lines 1-3, p. 53-55). Beier I discloses SEQ ID NO: 1 is Bacillus Cibi DNase (at least p. 35 lines 16-17). Beier I discloses DNase and DNase variants means a polypeptide with DNase activity (at least p. 8 lines 9-10). Beier I discloses detergent compositions comprising at least one DNase variant and a detergent adjunct ingredient, the DNase variant comprising the polypeptide of SEQ ID NO: 1, comprising one or more substitutions, the substitutions being T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 53 lines 15 to p. 56 lines 5), where the detergent adjunct is a surfactant, which improves wash performance in the detergent composition comprising DNase, and one or more enzymes, where the one or more enzymes are mannanases (at least p. 55 lines 1-9). Therefore, Beier I can be deemed to disclose a cleaning composition comprising a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36. Beier I differs from the claimed cleaning composition by not explicitly reciting the mannanase amino acid sequence.
Gori discloses a cleaning composition comprising a mixture of enzymes, including a DNase and at least one carbohydrase being mannanase, and a cleaning component (at least p. 1 lines 33-37). Gori et al. disclose the DNase means a polypeptide with DNase activity (p. 3-4). Gori et al. disclose the mannanase is a mannanase of Family 5 or 26 (p. 26 lines 13-14), the mannanase comprises the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15.
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the mannanase polypeptide of Gori et al. for the mannanase enzyme in the cleaning composition comprising the DNase variant and surfactant of Beier I noted above because the prior art disclose combining DNase enzymes and mannanase enzymes to formulate a cleaning composition (instant claims 1, 5). One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Regarding instant claim 4, Beier I discloses the amount of DNase in the cleaning composition is from at least 0.01 ppm to at least 20 ppm (at least p. 55 lines 27-30) and that the amount of the additional enzyme(s) is compatible with the other enzymatic ingredients and present in effective amounts (p. 64 lines 35 to p. 65 lines 4), where compatible amounts would include the amounts present for DNase enzymes, including at least 0.01 ppm to at least 20 ppm. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). MPEP 2144.05. Therefore, it would have been obvious to arrive at the recited DNase present in an amount 0.01 to 1000 ppm and the recited at least one mannanase present in an amount 0.01 to 1000 ppm by routine optimization.
Regarding instant claim 13, Beier I discloses the cleaning composition comprises an anionic surfactant (0 wt% to 40 wt%) and a nonionic surfactant (0 wt% to 40 wt%) (at least p. 59 lines 5-6).
Regarding instant claim 14, Beier I discloses the cleaning composition further comprises additional enzymes selected from pectinases, pectin lyases, xanthanases, catalases (at least p. 55 lines 5-10, p. 64 lines 34 to p. 65 lines 1).
Regarding instant claim 15, Beier I discloses the cleaning composition is in the form of a liquid laundry composition (at least p. 56 lines 7 to p. 58 lines 33).
Regarding instant claim 12, as noted above, Beier I discloses a DNase variant comprising the polypeptide of SEQ ID NO: 1, comprising one or more substitutions, the substitutions being T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 53 lines 15 to p. 56 lines 5), where Beier I discloses all the amino acid residues or substitutions recited in the DNA variant of instant claim 12, except at position 33. Beier I do disclose incorporating a substitution at position 32 (at least p. 53) and construction of the DNase variants by site-directed mutagenesis (at least p. 94), including random mutagenesis (at least p. 42). MPEP 2144.09 notes that a prima facie case of obviousness may be made when chemical compounds have very close structural similarities and similar utilities. In this instance, Beier I can be deemed to disclose a DNase variant that is structurally similar to the recited DNase variant and having the same utility. It would be obvious to one of ordinary skill to modify other amino acid positions in the DNase variant of Beier I, including at position 33 to arrive at a lysine residue in combination with the substitutions noted above in the DNase variant of Beier I because there was interest in forming cleaning compositions with DNase enzymes. One of ordinary skill would have a reasonable expectation of success because mutagenesis is a known method for engineering protein variants having the same or enhanced functions and there are a finite number of amino acid substitutions.
Reply: In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection as being anticipated by Beier I has been withdrawn. However, Beier I is maintained as a 103 reference in view of Gori et al. for the reasons noted above. Additionally, Beier I and Gori et al. are maintained as 103 references for the reasons similarly noted above for Beier II and Gori et al.
Regarding Applicants’ remarks that Beier I in view of Gori et al. do not disclose or suggest the precise pairing of structure-constrained enzymes, nor do they provide an articulated reasoning or motivation to select Lys33, as recited in claim 12, specifically together with sequence identity thresholds for the required DNase and mannanases, the remarks are not persuasive.
As noted above, the claimed composition essentially comprises the combination of a protein or polypeptide having DNase activity and a protein having mannanase activity, regardless of the recited sequence identity thresholds. In this instance, Beier I already discloses a detergent composition or cleaning compositions comprising a DNase variant, a mannanase, and a surfactant, which is the same combination and the same types of enzymes and adjunct recited in the instant composition. Beier I further discloses a DNase variant of the polypeptide of SEQ ID NO: 1 comprising the substitutions T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 53 lines 15 to p. 56 lines 5), which differs from the DNase variant of instant claim 12 by one amino acid residue. Therefore, the DNase variant of Beier I is structurally similar and has the same activity and functionality as the DNase variant of instant claim 12. MPEP 2144.09 notes that a prima facie case of obviousness may be made when chemical compounds have very close structural similarities and similar utilities. Beier I further discloses incorporating a substitution at position 32 (at least p. 53) and construction of the DNase variants by site-directed mutagenesis (at least p. 94). In this instance, Beier I can be deemed to disclose a DNase variant that is structurally similar to the recited DNase variant and having the same utility. It would be obvious to one of ordinary skill to modify other amino acid positions in the DNase variant of Beier I, including at position 33 to arrive at a lysine residue in combination with the substitutions noted above in the DNase variant of Beier I because there was interest in forming cleaning compositions with DNase enzymes. Beier I is further cited with Gori et al., where Gori et al. disclose known mannanase enzymes for incorporation in cleaning compositions comprising a polypeptide having DNase activity and an adjunct, such as the cleaning compositions disclosed in Beier I, which comprise a DNase variant and an adjunct. Therefore, one of ordinary skill would have a reasonable expectation of success that the mannanase enzymes of Gori et al., including the mannanase comprising the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15, can be incorporated as the mannanase enzyme in the cleaning composition comprising the DNase variant and surfactant of Beier I noted above because the prior art disclose the same combination of polypeptides having DNase activity and mannanase enzymes together to form a cleaning composition, where the polypeptides of the prior art having DNase activity and mannanase activity further meet the recited sequence identity thresholds (instant claim 1).
Claims 1, 4-5, 12, 13-15 are rejected under 35 U.S.C. 103 as being unpatentable over Beier I (WO 2018011277; previously cited) in view of Gori (WO 2018184816; IDS 09.08.22, previously cited) and Beier III (WO 2019081721; IDS 09.08.22). The teachings of Beier I and Gori et al. over at least instant claims 1, 4-5, 13-15 are noted above.
Regarding instant claim 12, Beier I discloses the DNase variant comprises the polypeptide of SEQ ID NO: 1, comprising one or more substitutions, the substitutions being T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D (at least p. 53 lines 15 to p. 56 lines 5). Beier III discloses DNase variants including the substitutions T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D of Beier I, in combination with the substitution L33K (at least p. 18). Beier III discloses the DNase variants are incorporate into detergent compositions (p. 1), comprising one or more enzymes including mannanase (p. 94), and a surfactant (p. 88-89). Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the L33K substitution in the DNase of Beier III with the substitutions of Beier I noted above to arrive at the recited DNase variant comprising T1I, S13Y, T22P, S27L, S39P, S42G, D56I, S57W, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, A147H, S167L, G175D. One of ordinary skill would have a reasonable expectation of success because the prior art discloses amino acid substitutions to arrive at DNase variants for cleaning compositions, including L33K.
Reply: In view of Applicants’ amendments/remarks, Beier III is newly cited, which further disclose L33K is a known substitution in DNase variants for cleaning compositions.
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, 4-5, 12-15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 14, 16, 19-24, 26-28 of copending Application No. 16757580 (‘580) (reference application) in view of Gori (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘580 application claims recite a DNase variant that is structurally the same and/or similar. The ‘580 application claims recite a polypeptide having DNase activity comprising the same amino acid residues and/or substitutions as recited in at least instant claims 1, 12. The ‘580 application claims differ from the instant claims by not explicitly reciting a composition comprising the DNase, in combination with one more enzymes elected from mannanase, and a cleaning adjunct. Gori discloses a cleaning composition comprising a mixture of enzymes, including a DNase and at least one carbohydrase being mannanase, and a cleaning component (at least p. 1 lines 33-37), where the cleaning component comprises one or more surfactants (at least p. 48-49). Gori et al. disclose the mannanase is a mannanase of Family 5 or 26 (p. 26 lines 13-14), the mannanase comprises the polypeptide having the amino acid sequence of SEQ ID NO: 82 (p. 26 lines 20-36), where SEQ ID NO: 82 has 100% sequence identity with instant SEQ ID NO: 15. Therefore, in view of the noted teachings of Gori above, it would have been obvious to one of ordinary skill to incorporate the mannanase polypeptide and surfactant of Gori et al. in a composition comprising the DNase variant of the ‘580 application claims. One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients, including surfactants, to form cleaning compositions was known in the art.
Additionally, the components and/or features recited in the instant dependent claims, i.e. surfactants, anionic surfactant, nonionic surfactants, are also reasonably recited and/or suggested in the teachings of Gori et al. for incorporation into a composition comprising DNase and a mannanase (Gori et al. p. 48).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ remarks have been considered but they are not persuasive. The reasons for maintaining the provisional nonstatutory double patenting rejection are the same as noted above.
Claims 1, 4-5, 13-15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 37-45 of copending Application No. 17782279 (‘279) (reference application) in view of Gori (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘279 application claims are drawn to a composition comprising a DNase variant and a cleaning adjunct (surfactant) (see at least claim 37 of the ‘279 application). The ‘279 application claim 37 recites a DNase comprising substitutions that result in a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36, as recited in at least instant claim 1. The ‘279 application claims differ from the instant claims by not explicitly reciting the amino acid sequence of a mannanase enzyme. However, in view of the noted teachings of Gori above, it would have been obvious to one of ordinary skill to incorporate the mannanase polypeptide of Gori et al. in the composition comprising the DNase variant and surfactant of the ‘279 application claims. One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Additionally, the components and/or feature recited in the instant dependent claims are also reasonably recited and/or suggested in the ‘279 application claims and/or Gori et al.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ remarks have been considered but they are not persuasive. The reasons for maintaining the provisional nonstatutory double patenting rejection are the same as noted above.
Claims 1, 4-5, 12-15 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 10781408 (‘408) in view of Gori (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘408 patent claims are drawn to a composition comprising a DNase variant and a cleaning adjunct (surfactant) and a mannanase (see at least claims 1, 13-14 of the ‘408 patent). The ‘408 patent claims 2, 6 recite a DNase comprising the same amino acid residues and/or substitutions as recited in at least instant claims 1, 12. The ‘408 patent claims differ from the instant claims by not explicitly reciting the amino acid sequence of a mannanase enzyme. However, in view of the noted teachings of Gori above, it would have been obvious to one of ordinary skill to incorporate the mannanase polypeptide of Gori et al. for the mannanase enzyme in the composition comprising the DNase variant and cleaning adjunct of the ‘408 patent claims. One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Additionally, the components and/or feature recited in the instant dependent claims are also reasonably recited and/or suggested in the ‘408 patent claims and/or Gori et al.
Reply: Applicants’ remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting rejection are the same as noted above.
Claims 1, 4-5, 13-15 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 10774293 (‘293) in view of Gori (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘293 patent claims are drawn to a composition comprising a DNase variant and a cleaning component and a mannanase (see at least claims 1, 10-12 of the ‘293 patent). The ‘293 patent claims 1-2 recite a DNase comprising substitutions that result in a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36, as recited in at least instant claim 1. The ‘293 patent claims differ from the instant claims by not explicitly reciting the amino acid sequence of a mannanase enzyme. However, in view of the noted teachings of Gori above, it would have been obvious to one of ordinary skill to incorporate the mannanase polypeptide of Gori et al. for the mannanase enzyme in the composition comprising the DNase variant and cleaning component of the ‘293 patent claims. One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Additionally, the components and/or feature recited in the instant dependent claims are also reasonably recited and/or suggested in the ‘293 patent claims and/or Gori et al.
Reply: Applicants’ remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting rejection are the same as noted above.
Claims 1, 4-5, 13-15 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No. 11447723 (‘723) in view of Gori (WO 2018184816). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘723 patent claims are drawn to a composition comprising a DNase variant and a cleaning component and a mannanase (see at least claim 1 of the ‘723 patent). The ‘723 patent claim 1 recites a DNase comprising substitutions that result in a DNase having at least 90% but less than 100% amino acid sequence identity to SEQ ID NO: 1, with the proviso that the DNase is not the amino acid sequence shown in SEQ ID NO: 36, as recited in at least instant claim 1. The ‘723 patent claims differ from the instant claims by not explicitly reciting the amino acid sequence of a mannanase enzyme. However, in view of the noted teachings of Gori above, it would have been obvious to one of ordinary skill to incorporate the mannanase polypeptide of Gori et al. for the mannanase enzyme in the composition comprising the DNase variant and cleaning component of the ‘723 patent claims. One of ordinary skill would have a reasonable expectation of success because combining DNase enzymes, mannanases, and adjunct ingredients to form cleaning compositions was known in the art.
Additionally, the components and/or feature recited in the instant dependent claims are also reasonably recited and/or suggested in the ‘723 patent claims and/or Gori et al.
Reply: Applicants’ remarks have been considered but they are not persuasive. The reasons for maintaining the nonstatutory double patenting rejection are the same as noted above.
No claim is allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
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/Marsha Tsay/Primary Examiner, Art Unit 1656