DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 02/20/2026 has been entered.
Status of Claims
Claims 37-47 are pending following the Reply filed 02/20/2026. Claims 27-36 have been cancelled by Applicant. Claims 37-47 have been added without introducing any new matter. Claims 46-47 are withdrawn. Claims 37-45 are presently considered.
Election/Restrictions
The requirement for Restriction/Election filed on 03/05/2025 is maintained.
Applicant’s election without traverse of Group I, and the species of a cellulase and a DNase having a histidine at position 147, was acknowledged in the office action filed 05/21/2025. Newly added claims 37-45 are drawn to the invention of Group I. Claims 46-47 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention (i.e., Group IV, a method of cleaning), there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 04/29/2025.
Maintained rejections and new rejections necessitated by amendment
Claim Rejections - 35 USC § 103
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 37-45 are rejected under 35 U.S.C. 103 as being unpatentable over Beier, WO 2018011276 A1 (previously cited), and further in view of Lant et al., US 2009031221 A1 (previously cited), hereafter “Lant”.
Regarding claim 37, Beier teaches detergent compositions comprising polypeptide variants, methods of cleaning and treating surfaces using such compositions, and fabric treatment compositions comprising polypeptide variants (see Abstract). Beier teaches DNase variants exhibiting alterations relative to a parent DNase in one or more properties, including wash performance, detergent stability, and/or storage stability (see pg. 1, lines 8-10). Beier teaches a detergent composition comprising a variant of a DNase parent, wherein the variant comprises one or more substitutions compared to SEQ ID NO: 1 (see claim 1), wherein the variant of the DNase parent has an improved stability, measured as half-life improvement factor (HIF), compared to the parent DNase of SEQ ID NO: 1 (see claim 2).
Regarding claim 37(a), Beier teaches the substitutions are selected from the group which includes S13Y, T22P, S27L, S39P, S42G, D56I, S59V, T65V, V76L, Q109R, S116D, T127V, S144P, S167L and G175D, which were associated with improved activity compared to Beier’s SEQ ID NO: 1 (see claim 1; pg. 89 at lines 4-7 and Table 1). As shown in the following alignment, instant SEQ ID NO: 1 (top) shares more than 99% sequence identity with Beier’s modified SEQ ID NO: 1 (bottom) comprising the substitutions above:
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Regarding the limitation of a “Histidine at position 147”, Beier teaches the substitution A147H which was associated with improved activity compared to Beier’s SEQ ID NO: 1 (see pg. 89 at lines 4-7 and Table 1).
Beier does not teach the DNase according to SEQ ID NO: 1 comprising a lysine at position 33.
However, Beier teaches that the identification of a corresponding amino acid residue in another DNase can be determined by an alignment of multiple polypeptide sequences (see pg. 13, lines 1-3), and these alignments can in turn be used to generate homology models for the polypeptide (see pg. 13, lines 24-25) to discover possible structural homologs (see pg. 13, lines 31-33). Beier teaches that preferred DNase variants of the disclosure have a DNase parent selected from the group of polypeptides represented by SEQ ID NOs 1-24 (see pg. 31 at line 20 to pg. 34 at line 16). Of these sequences, SEQ ID NOs 11-15, 17-19, 21 and 23-24 all feature a lysine at position 33. As in the case of Beier’s SEQ ID NO: 1, these sequences are disclosed to be the mature polypeptides obtained from members of Bacillus (see pg. 5, “Sequences”), and all of these sequences are the same length and share similar sequence identity, as shown in the following alignment between Beier’s SEQ ID NO: 1 (top) and Beier’s SEQ ID NO: 17 (bottom):
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Hence, it would have been obvious to have constructed a variant with a lysine at position 33, because Beier teaches preferred variants can be constructed from parent sequences that already possess this feature. A person of ordinary skill would have recognized from Beier’s disclosure that a lysine at position 33 is a common motif in structurally-similar DNase enzymes obtained from Bacillus, and the presence of this amino acid at this position would have been recognized at the time of filing as a result-effective variable. Accordingly, one would have expected the DNase having a lysine at position 33 to function in a manner that is at least equivalent to the modified DNase taught by Beier. Furthermore, it would have been within the ordinary skill in the art to have arrived at the claimed DNase through no more than routine optimization, because Beier suggests that structural homology can be used as a basis for the rational design of the variants. Moreover, the instant specification does not disclose any evidence of any unexpected results for any embodiments of the present invention, including DNase variants with a lysine at position 33.
Regarding claim 37(b), Beier teaches the detergent composition further comprising an adjunct ingredient (see claim 1), which is preferably an enzyme selected from the group that includes cellulases (see pg. 47, lines 31-34).
Regarding claim 37(c), Beier teaches the detergent composition to include additional adjuncts, including surfactants and builders (see pg. 47, lines 20-25) and may be in the form of a liquid, gel, powder, or paste (see pg. 48, lines 3-6).
Beier does not teach the cellulase having at least 99% sequence identity to the cellulase shown in SEQ ID NO: 31.
Lant teaches a laundry detergent composition comprising a variant of a parent xyloglucanase (see Abstract) having improved stability in liquid detergents (see pg. 1, para. [0015]). Lant teaches the detergent composition typically comprises conventional detergent ingredients such as surfactants, builders, bleaches, and additional enzymes (see pg. 11, para. [0392]; pg. 20, para. [0471]), and can be in any form, such as a solid, liquid, or gel (see pg. 11, para. [0392]). Lant teaches the variant to have improved chemical stability compared to the parent xyloglucanase, and this stability results in improved detergent stability (see claims 13-14). Lant teaches the variant xyloglucanase may also have cellulase activity (see pg. 2, para. [0019]), which many xyloglucanases are known to have (see pg. 1, para. [0004]), and the composition may also comprise a deoxyribonuclease (DNase) (see pg. 11, para. [0388]).
Lant teaches the variant comprising the amino acid substitutions, Q68H, T92V, K118A, K129A, R156Y, G200P and N331F, relative to the parent xyloglucanase of SEQ ID NO: 3 (see pg. 4, para. [0046]; pg. 7, para. [0079]-[0080]; pg. 7, para. [0115]; and pg. 8, para. [0147]). As shown in the following alignment, instant SEQ ID NO: 31 (top) shares 100% sequence identity with Lant’s modified SEQ ID NO: 3 (bottom) comprising the substitutions above:
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It would have been obvious at the time of filing for a person of ordinary skill in the art to have arrived at the claimed invention by combining the teachings of Beier and Lant, because both references teach detergent (cleaning) compositions comprising DNase and cellulase and disclose variants of these enzymes that have improved properties. One would have recognized the advantage of combining the DNase with improved performance and stability in a detergent taught by Beier with the xyloglucanase variant taught by Lant, because Lant teaches this variant to have improved chemical stability in a detergent composition. As both references teach detergent compositions that may include additional adjuncts/ingredients, including multiple enzymes, one of ordinary skill would have recognized that the elements of both references could be combined by known methods, and that in combination, each element merely performs the same function as it does separately. As such, the results of the combination would have been predictable, and there would have been a reasonable expectation of success. Hence, the combination would have been readily apparent and deemed to be a mere (A) combining of prior art elements according to known methods to yield predictable results (see MPEP 2143(I): Rationales to support rejections under 35 U.S.C. 103).
Regarding claim 38, Beier teaches the substitution, T1I, which was associated with improved activity compared to Beier’s SEQ ID NO: 1 (see claim 1; pg. 89, lines 4-7 and Table 1). Hence, Beier teaches the DNase further comprising an Isoleucine at position 1.
Regarding claim 39, Beier teaches the substitution, S57W, which was associated with improved activity compared to Beier’s SEQ ID NO: 1 (see claim 1; pg. 89, lines 4-7 and Table 1). Hence, Beier teaches the DNase further comprising a Tryptophan at position 57.
Regarding claim 40, Beier teaches the DNase further comprising Isoleucine at position 1 and Tryptophan at position 57, as discussed regarding claims 38 and 39.
Regarding claim 41, Beier teaches the substitution, S25P, which was associated with improved activity compared to Beier’s SEQ ID NO: 1 (see claim 1; pg. 89, lines 4-7 and Table 1). Hence, Beier teaches the DNase further comprising a Proline at position 25.
Regarding claim 42, Beier teaches the DNase variant having more than 99% sequence identity to the DNase shown in SEQ ID NO: 1, as discussed regarding claim 37.
Regarding claim 43, Beier teaches the DNase variant having more than 99% sequence identity to the DNase shown in SEQ ID NO: 1, as discussed regarding claim 37.
Regarding claim 44, Beier teaches the DNase variant having more than 99% sequence identity to the DNase shown in SEQ ID NO: 1, as discussed regarding claim 37.
Regarding claim 45, Beier and Lant teach the detergent compositions may comprise surfactants, as discussed above.
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 37-45 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6 and 13-14 of U.S. Patent No. 10,781,408 B2 (previously cited), hereafter, “Oestergaard”, and further in view of Lant.
Claim 1 of Oestergaard recites a detergent composition comprising a) a variant of a
DNase parent, which compared to a DNase with SEQ ID NO: 1, comprises two or more substitutions selected from the group consisting of: TlI, TlL, TlV, S13Y, T22P, S25P, S27L, S39P, S42G, S42A, S42T, S57W, S57Y, S57F, S59V, S59I, S59L, V76L, V76I, Q109R, S116D, S116E, T127V, T127I, T127L, S144P, A147H, S167L, S167I, S167V, G175D and G175E, wherein the positions correspond to the positions of SEQ ID NO: 1 (numbering according to SEQ ID NO: 1 ), wherein the variant has a sequence identity to the polypeptide shown in SEQ ID NO: 1 or SEQ ID NO: 28 of at least 90% and wherein the variant has DNase activity; and b) from 0.01 to 99.9 wt % of an adjunct.
Claim 6 of Oestergaard teaches a detergent composition of claim 1 wherein the DNase variant is selected from variants from the group comprising one of the following sets of substitutions, using numbering compared to SEQ ID NO: 1 (see Oestergaard at claim 6, i-xxiii for the full list of substitution sets). In particular, claim 6(xii) of Oestergaard recites the substitution set TlI+S13Y+T22P+S27L+L33K+S39P+ S42G+D56I+S57W+S59V+T65V+ V76L+Q109R+S116D+T127V+S144P+A147H+S167L+ Gl75D.
Claim 13 of Oestergaard recites a detergent composition according to claim 1 wherein the adjunct comprises an additional enzyme selected from the group consisting of proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidaes, haloperoxygenases, catalases and mannanases, and mixtures thereof.
Claim 14 of Oestergaard recites a detergent composition according to claim 1 wherein
the adjunct comprises from 5 to 70 wt % surfactant.
Regarding instant claim 37(a), claim 1 of Oestergaard teaches a variant of a DNase parent comprising SEQ ID NO: 1 with the substitutions S13Y, T22P, S27L, S39P, S42G, D56I, S59V, V76L, Q109R, S116D, T127V, S144P, S167L and G175D. As shown in the following alignment, instant SEQ ID NO: 1 (top) shares more than 98% sequence identity with Oestergaard’s modified SEQ ID NO: 1 (bottom) comprising the above substitutions:
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Claim 6(xii) of Oestergaard teaches the substitution set TlI+S13Y+T22P+S27L+L33K+S39P+ S42G+D56I+S57W+S59V+T65V+V76L+Q109R+S116D+T127V+S144P+A147H+S167L+ Gl75D. Hence, Oestergaard teaches the DNase with all of the same amino acid residues at the recited positions of instant claim 37.
Regarding instant claim 37(b), claims 1 and 13 of Oestergaard teach the composition further comprising an adjunct, wherein the adjunct is a cellulase.
Regarding instant claim 37(c), claim 14 of Oestergaard teaches the detergent composition further comprising a surfactant. In view of Oestergaard’s specification “The term ‘detergent composition’ includes, unless otherwise indicated, granular or powder-form all-purpose or heavy-duty washing agents” (see col. 4, lines 64-67). Hence, the detergent composition of Oestergaard meets the limitation of the cleaning composition in the form of a “granulate” or “powder”. See MPEP §804(II)(B)(1) which states:
The specification can be used as a dictionary to learn the meaning of a term in the patent claim. Toro Co. v. White Consol. Indus., Inc., 199 F.3d 1295, 1299, 53 USPQ2d 1065, 1067 (Fed. Cir. 1999)(“[W]ords in patent claims are given their ordinary meaning in the usage of the field of the invention, unless the text of the patent makes clear that a word was used with a special meaning.” ); Renishaw PLC v. Marposs Societa' per Azioni, 158 F.3d 1243, 1250, 48 USPQ2d 1117, 1122 (Fed. Cir. 1998) (“Where there are several common meanings for a claim term, the patent disclosure serves to point away from the improper meanings and toward the proper meanings.”). See also MPEP § 2111.01. Further, those portions of the specification which provide support for the patent claims may also be examined and considered when addressing the issue of whether a claim in the application defines an obvious variation of an invention claimed in the patent. In re Vogel, 422 F.2d 438, 441-42, 164 USPQ 619, 622 (CCPA 1970). The court in Vogel recognized “that it is most difficult, if not meaningless, to try to say what is or is not an obvious variation of a claim,” but that one can judge whether or not the invention claimed in an application is an obvious variation of an embodiment disclosed in the patent which provides support for the patent claim. According to the court, one must first “determine how much of the patent disclosure pertains to the invention claimed in the patent” because only “[t]his portion of the specification supports the patent claims and may be considered.' The court pointed out that ‘this use of the disclosure is not in contravention of the cases forbidding its use as prior art, nor is it applying the patent as a reference under 35 U.S.C. 103, since only the disclosure of the invention claimed in the patent may be examined.”
Oestergaard does not teach the cellulase having at least 99% sequence identity to the cellulase shown in SEQ ID NO: 31.
As previously discussed under 35 U.S.C. 103, Lant teaches a laundry detergent composition comprising a variant of a parent xyloglucanase (see Abstract) having improved stability in liquid detergents (see pg. 1, para. [0015]). Lant teaches the detergent composition typically comprises conventional detergent ingredients such as surfactants, builders, bleaches, and additional enzymes (see pg. 11, para. [0392]; pg. 20, para. [0471]), and can be in any form, such as a solid, liquid, or gel (see pg. 11, para. [0392]). Lant teaches the variant to have improved chemical stability compared to the parent xyloglucanase, and this stability results in improved detergent stability (see claims 13-14). Lant teaches the variant xyloglucanase may also have cellulase activity (see pg. 2, para. [0019]), which many xyloglucanases are known to have (see pg. 1, para. [0004]), and the composition may also comprise a deoxyribonuclease (DNase) (see pg. 11, para. [0388]).
Lant teaches the variant comprising the amino acid substitutions, Q68H, T92V, K118A, K129A, R156Y, G200P and N331F, relative to the parent xyloglucanase of SEQ ID NO: 3 (see pg. 4, para. [0046]; pg. 7, para. [0079]-[0080]; pg. 7, para. [0115]; and pg. 8, para. [0147]). As shown in the following alignment, instant SEQ ID NO: 31 (top) shares 100% sequence identity with Lant’s modified SEQ ID NO: 3 (bottom) comprising the substitutions above:
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It would have been obvious at the time of filing for a person of ordinary skill in the art to have arrived at the claimed invention by combining the teachings of Oestergaard and Lant, because both references teach detergent (cleaning) compositions comprising DNase and cellulase and disclose variants of these enzymes that have improved properties. One would have recognized the advantage of combining the DNase with improved performance and stability in a detergent taught by Oestergaard with the xyloglucanase variant taught by Lant, because Lant teaches this variant to have improved chemical stability in a detergent composition. As both references teach detergent compositions that may include additional adjuncts/ingredients, including multiple enzymes, one of ordinary skill would have recognized that the elements of both references could be combined by known methods, and that in combination, each element merely performs the same function as it does separately. As such, the results of the combination would have been predictable, and there would have been a reasonable expectation of success. Hence, the combination would have been readily apparent and deemed to be a mere (A) combining of prior art elements according to known methods to yield predictable results (see MPEP 2143(I): Rationales to support rejections under 35 U.S.C. 103).
Regarding instant claim 38, claim 1 and claim 6(xii) of Oestergaard recite the substitution, TlI, which results in an Isoleucine at position 1.
Regarding instant claim 39, claim 1 and claim 6(xii) of Oestergaard recite the substitution, S57W, which results in Tryptophan at position 57.
Regarding instant claim 40, claims 1 and claim 6(xii) of Oestergaard recite an Isoleucine at position at position 1 and a Tryptophan at position 57, as discussed above.
Regarding instant claim 41, claims 1 and claim 6(xii) of Oestergaard recite a Tryptophan at position 57, as discussed above.
Regarding instant claim 42, Oestergaard teaches the DNase variant having more than 98% sequence identity to the DNase shown in SEQ ID NO: 1, as discussed above.
Regarding instant claim 43, Oestergaard teaches the DNase variant having more than 98% sequence identity to the DNase shown in SEQ ID NO: 1, as discussed above.
Regarding claim 44, claim 6(xii) of Oestergaard teaches the substitution set that includes L33K, D56I and T65V. Hence, it would have been obvious to have included these substitutions, which renders Oestergaard’s variant DNase 100% identical to instant SEQ ID NO: 1.
Regarding claim 45, Oestergaard and Lant teach the detergent compositions may comprise surfactants, as discussed above.
Claim 37-43 and 45 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 9 and 11-12 of copending Application No. 17/923,489 (reference application) in view of Lant. This is an obvious-type rejection.
This is a provisional nonstatutory double patenting rejection.
Claim 9 of the reference application recites:
A medical cleaning composition comprising a polypeptide having DNase activity, wherein the composition has a pH in the range of 6.0-10.0 and wherein the polypeptide having DNase activity is a polypeptide having at least 90% sequence identity to the polypeptide shown in SEQ ID NO: 2.
Claim 11 of the reference application recites:
The medical cleaning composition according to claim 9, wherein the composition further comprises one or more cleaning components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.
Claim 12 of the reference application recites:
The medical cleaning composition according to claim 9, wherein the medical cleaning composition further comprises one or more enzymes selected from the group consisting of proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases, galactanase, mannanases, or any mixture thereof.
Regarding instant claim 37, reference claim 9 recites “A medical cleaning composition comprising a polypeptide having DNase activity… wherein the polypeptide having DNase activity is a polypeptide having at least 90% sequence identity to the polypeptide shown in SEQ ID NO: 2.” As shown in the following alignment, instant SEQ ID NO: 1 (top) is more than 98% identical to the reference sequence (bottom):
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Note that the reference sequence contains all of the amino acids at the positions recited in instant claim 1.
Regarding instant claim 37(b), reference claim 12 recites the cleaning composition further comprising a cellulase.
Regarding instant claim 37(c), reference claim 11 recites the cleaning composition further comprising a surfactant.
The reference claims do not recite the cellulase having at least 99% sequence identity to the cellulase shown in SEQ ID NO: 31.
As previously discussed under 35 U.S.C. 103, Lant teaches a laundry detergent composition comprising a variant of a parent xyloglucanase (see Abstract) having improved stability in liquid detergents (see pg. 1, para. [0015]). Lant teaches the detergent composition typically comprises conventional detergent ingredients such as surfactants, builders, bleaches, and additional enzymes (see pg. 11, para. [0392]; pg. 20, para. [0471]), and can be in any form, such as a solid, liquid, or gel (see pg. 11, para. [0392]). Lant teaches the variant to have improved chemical stability compared to the parent xyloglucanase, and this stability results in improved detergent stability (see claims 13-14). Lant teaches the variant xyloglucanase may also have cellulase activity (see pg. 2, para. [0019]), which many xyloglucanases are known to have (see pg. 1, para. [0004]), and the composition may also comprise a deoxyribonuclease (DNase) (see pg. 11, para. [0388]). As discussed under 35 U.S.C. 103, Lant teaches a cellulase that is identical to instant SEQ ID NO: 31.
Therefore, for reasons similar to those discussed under 35 U.S.C. 103, it would have been obvious at the time of filing for a person of ordinary skill in the art to have arrived at the claimed invention by combining the teachings of the reference claims with those of Lant, because both disclosures teach cleaning compositions comprising DNase and cellulase. One would have been motivated to use the cellulase variant taught by Lant, because Lant teaches this enzyme to have improved detergent stability. As both references teach detergent compositions that may include additional adjuncts/ingredients, including multiple enzymes, one of ordinary skill would have recognized that the elements of both references could be combined by known methods, and that in combination, each element merely performs the same function as it does separately.
Regarding instant claim 38, the reference sequence (SEQ ID NO: 2) already comprises an Isoleucine at position 1.
Regarding instant claim 39, the reference sequence (SEQ ID NO: 2) already comprises a Tryptophan at position 57.
Regarding instant claim 40, the reference sequence (SEQ ID NO: 2) already comprises an Isoleucine at position 1 and a Tryptophan at position 57.
Regarding instant claim 41, the reference sequence (SEQ ID NO: 2) already comprises a Tryptophan at position 57.
Regarding instant claim 42, the reference sequence (SEQ ID NO: 2) shares more than 98% identity with instant SEQ ID NO: 1, as discussed above.
Regarding instant claim 43, the reference sequence (SEQ ID NO: 2) shares more than 98% identity with instant SEQ ID NO: 1, as discussed above.
Regarding instant claim 45, reference claim 11 recites the cleaning composition further comprising a surfactant.
Claim 44 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 9 and 11-12 of copending Application No. 17/923,489 (reference application) and Lant, as applied to claims 37-43 and 45 above, in further view of Beier. This is an obvious-type rejection.
This is a provisional nonstatutory double patenting rejection.
As previously discussed under 35 U.S.C. 103, Beier teaches detergent compositions comprising polypeptide variants, methods of cleaning and treating surfaces using such compositions, and fabric treatment compositions comprising polypeptide variants (see Abstract). Beier teaches DNase variants exhibiting alterations relative to a parent DNase in one or more properties, including wash performance, detergent stability, and/or storage stability (see pg. 1, lines 8-10). Beier teaches a detergent composition comprising a variant of a DNase parent, wherein the variant comprises one or more substitutions compared to SEQ ID NO: 1 (see claim 1), wherein the variant of the DNase parent has an improved stability, measured as half-life improvement factor (HIF), compared to the parent DNase of SEQ ID NO: 1 (see claim 2). Beier teaches the detergent composition further comprising an adjunct ingredient (see claim 1), which is preferably an enzyme selected from the group that includes cellulases (see pg. 47, lines 31-34). Beier teaches the detergent composition to include additional adjuncts, including surfactants and builders (see pg. 47, lines 20-25) and may be in the form of a liquid, gel, powder, or paste (see pg. 48, lines 3-6). As previously discussed, Beier teaches a modified DNase having more than 99% identity with instant SEQ ID NO: 1.
Regarding instant claim 44, Beier teaches a DNase comprising substitutions, which is more than 99% identical to the DNase shown in instant SEQ ID NO: 1 when comprising said substitutions, while also comprising the same amino acid residues at the same positions recited in instant claim 37, as discussed under 35 U.S.C. 103. Beier teaches a variant of SEQ ID NO: 1 with substitutions selected from a list (see claim 1), including T1I and S47W. However, Beier clearly teaches these substitutions to be optional, as they are selected amongst numerous potential substitutions. Hence, it would have been obvious for the variant to have comprised a “T” at position 1 and/or an “S” at position 47, because these residues are already present in Beier’s SEQ ID NO: 1 by default. Hence, either of these features (T1 or S47) in the sequence of the reference application (SEQ ID NO: 2) would render a sequence with at least 99% identity with instant SEQ ID NO: 1, which would still comprise substitutions (relative to the parent sequence taught by Beier) that Beier teaches to be associated with improved properties.
Therefore, for reasons similar to those discussed under 35 U.S.C. 103, it would have been obvious at the time of filing for a person of ordinary skill in the art to have arrived at the claimed invention by combining the teachings of the reference claims with those of Beier and Lant, because each reference teaches cleaning compositions comprising DNase and cellulase and Beier/Lant disclose variants of these enzymes that have improved properties. As each references teaches detergent compositions that may include additional adjuncts/ingredients, including multiple enzymes, one of ordinary skill would have recognized that the elements of each references could be combined by known methods, and that in combination, each element merely performs the same function as it does separately. Hence, the combination would have been readily apparent and deemed to be a mere (A) combining of prior art elements according to known methods to yield predictable results (see MPEP 2143(I): Rationales to support rejections under 35 U.S.C. 103).
Response to Arguments
Regarding the rejections under 35 U.S.C. 103, Applicant only argues that Beier and Lant, alone or in combination, do not teach or suggest a cleaning composition comprising a DNase having at least 96% sequence identity to the DNase shown in SEQ ID NO: 1, which comprises Tyrosine at position 13, Proline at position 22, Leucine at position 27, Lysine at position 33, Proline at position 39, Glycine at position 42, lsoleucine at position 56, Valine at position 59, Valine at position 65, Leucine at position 76, Arginine at position 109, Aspartic acid at position 116, Valine at position 127, Proline at position 144, Histidine at position 147, Leucine at position 167 and Aspartic acid at position 175, and (b) a cellulase having at least 99% sequence identity to the cellulase shown in SEQ ID NO: 31.
Applicant's arguments have been fully considered but they are not persuasive. As discussed in the present rejection, Beier and Lant both teach detergent (cleaning) compositions comprising DNase and cellulase and disclose variants of these enzymes that have improved properties. Beier teaches a DNase comprising substitutions, which is more than 96% identical to the DNase shown in instant SEQ ID NO: 1 when comprising said substitutions, while also comprising the same amino acid residues at the same positions recited in instant claim 37. Further, Lant teaches a cellulase that is identical to instant SEQ ID NO: 31.
Regarding the rejections on the ground of nonstatutory double patenting, Applicant only argues that Beier and Lant, alone or in combination, do not teach or suggest a cleaning composition comprising (a) a DNase having at least 96% sequence identity to the DNase shown in SEQ ID NO: 1, which comprises Tyrosine at position 13, Proline at position 22, Leucine at position 27, Lysine at position 33, Proline at position 39, Glycine at position 42, lsoleucine at position 56, Valine at position 59, Valine at position 65, Leucine at position 76, Arginine at position 109, Aspartic acid at position 116, Valine at position 127, Proline at position 144, Histidine at position 147, Leucine at position 167 and Aspartic acid at position 175, and (b) a cellulase having at least 99% sequence identity to the cellulase shown in SEQ ID NO: 31.
Applicant's arguments have been fully considered but they are not persuasive. First, the Beier reference was not used in the previous double-patenting rejection (in view of Oestergaard and Lant). As discussed in the present rejection, both of these references teach detergent (cleaning) compositions comprising DNase and cellulase and disclose variants of these enzymes that have improved properties. Oestergaard teaches a DNase comprising substitutions, which is more than 96% identical to the DNase shown in instant SEQ ID NO: 1 when comprising said substitutions, while also comprising the same amino acid residues at the same positions recited in instant claim 37. Further, Lant teaches a cellulase that is identical to instant SEQ ID NO: 31.
Regarding the new double-patenting rejection (in view of co-pending application 17/923,489, Lant and Beier), the Beier reference is only relied upon for the rejection of instant claim 44. Nonetheless, Beier teaches a DNase comprising substitutions, which is more than 96% identical to the DNase shown in instant SEQ ID NO: 1 when comprising said substitutions, while also comprising the same amino acid residues at the same positions recited in instant claim 37. See the present rejections under 35 U.S.C. 103 and Double Patenting for further discussion.
Conclusion
No claims are allowed.
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/DENNIS IGNATIUS ARMATO JR/Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651