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 .
Response to Amendment
The Amendment filed on June 15th, 2026 has been entered. Claims 1-4 and claims 6-18 are pending in the application. Claim 5 has been cancelled.
The rejection of claims 1-4, 8-13, and 15-18 under 35 U.S.C. 103 as obvious over Spangenberg (WO 2018029021 A1) and Juntunen (US 20190194634 A1) is maintained.
The rejection of claims 6-7 and claim 14 under 35 U.S.C. 103 as obvious over Spangenberg (WO 2018029021 A1), Juntunen (US 20190194634 A1), and Shabelina (EP 3122786 B1) is maintained.
Claim Rejections - 35 USC § 103
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.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-4, 8-13, and 15-18 are rejected under 35 U.S.C. 103 as being unpatentable over Spangenberg (WO 2018029021 A1) and further in view of Juntunen (US 20190194634 A1).
With regard to claims 1-4, Spangenberg discloses a liquid laundry formulation (see page 1 line 1). Spangenberg further discloses the polymer may be present in an amount of 0.1 to 10wt% (see page 10 line 1-2). Spangenberg further discloses a polymer which is an ethoxylated polyethylenimine with an average molecular weight Mw in the range from 3000 to 250,000 g/mol which has 80 to 99 % by weight ethylene oxide side chains, based on total ethoxylated polyethylenimine, and/or a polymer which is an ethoxylated hexamethylene diamine, quaternized and optionally sulfated with an average molecular weight Mw in the range from 2000 to 10,000 g/mol (see page 1 line 10-16). Spangenburg further discloses the ethoxylated hexamethylene diamine as having 20-30 EO per -NH group and a molecular weight of 2,000-10,000 g/mol (see page 9 line 27-29). Spangenburg further discloses the ethoxylated polyethylenimine as having 15-25 EO per -NH group and a molecular weight of 5,000-20,000 g/mol (see page 9 line 17-25). Spangenburg further discloses further optional ingredients, including enzymes which are not protease (see page 27 line 16-21).
While Spangenburg fails to disclose 0.5-2wt% of a1 and a2, Spangenburg discloses 3wt% of b1 and b2 (see Table page 30 line 1). Further, Spangenburg discloses the preferred amount of polymer (b), which is b1 and b2, as 0.5-5wt% (see page 10 line 1-2). One having ordinary skill in the art would find it obvious to optimize within the claimed range disclosed by Spangenburg (see MPEP 2144.05(II) A).
However, Spangenburg fails to disclose at least one cellulose, wherein the at least one cellulase is an endo-β-1,4- glucanase which has no carbohydrate binding domain (CBD).
Juntunen discloses polypeptides having cellulase activity (see Abstract). Juntunen further discloses in the detergent industry, an analogous art, cellulases are used to brighten colors and to prevent graying (see [0002]). Juntunen further discloses cellulases as including endoglucanases (EG, EC 3.2.1.4) which cut internal beta-1,4-glucosidic bonds (see [0019]). EC 3.2.1.4 is disclosed in the instant specifications as endo- β-1,4-glucanase. Juntunen further teaches the polypeptide variants may be designed to comprise in addition to the catalytic core domain, which forms the active or functional site of the enzyme, one or more “cellulose binding domains” (“CBDs”) (see [0031]). “May” indicates that such domains are unnecessary and Juntunen further discloses CBDs have carbohydrate-binding activity and they mediate the binding of cellulase to crystalline and amorphous cellulose but have little or no effect on hydrolytic activity of the enzyme on soluble substrates (see [0031]). Further, Juntenen discloses variant cellulase polypeptides basing on Melanocarpus albomyces 20K-cellulase core (without CBD) (see [0006]) and variants derived from a parental molecule MA0 (SEQ ID NO: 2), which is a polynucleotide encoding for the catalytic core domain of a cellulase derived from Melanocarpus albomyces ALK04237 20K-cellulase having no cellulose binding domain (CBD) (see [0025]). Juntenen further discloses 0.00001%-0.1% of variant cellulase polypeptide by weight of the composition (see [0057]).
It would have been obvious to one of ordinary skill in the art, before the effective filing date, to utilize the endo-β-1,4-glucanase of Juntunen in the laundry detergent composition of Spangenburg for the purpose of to brighten colors and to prevent graying, as disclosed by Juntunen.
With regard to claim 8, Spangenburg discloses the composition comprises at least one builder or co-builder (see page 1 line 6).
With regard to Spangenburg discloses the composition may further comprise at least one optional ingredient, including nonionic or ionic (e.g. anionic) surfactants (see page 19 line 14-18).
With regard to claim 11 and claim 12, Spangenburg discloses customary ingredients for laundry detergent compositions, including greying inhibitors (see page 25 line 23-25).
With regard to claim 13, Spangenburg discloses “laundry” as comprising all kinds of textiles and fabrics (see page 6 line 27-29).
With regard to claim 15, Spangenburg discloses a method for removing stains and soil from laundry comprising contacting the laundry with a laundry detergent composition (see Abstract) and further discloses customary ingredients for laundry detergent compositions, including greying inhibitors (see page 25 line 23-25).
With regard to claim 16, Spangenburg discloses a composition comprising protease (see page 1 line 17).
With regard to claim 17, Spangenburg discloses the protease may be serine endopeptidase (see page 10 line 24).
With regard to claim 18, Spangenburg discloses the composition may further comprise at least one optional ingredient, including nonionic or ionic (e.g. anionic) surfactants (see page 19 line 14-18).
Claims 6-7 and claim 14 are rejected under 35 U.S.C. 103 as being unpatentable over Spangenberg (WO 2018029021 A1) and Juntunen (US 20190194634 A1), as applied to claim 1 above, and in further view of Shabelina (EP 3122786 B1).
With regard to claim 6, Spangenburg and Juntunen disclose all of the limitations of claim 1.
However, Spangenburg and Juntunen fail to disclose the liquid composition of claim 1, further comprising component (c), which is a copolymer of (i) maleic acid or maleic anhydride, and (ii) at least one hydrophobic monomer selected from the group consisting of isobutene, diisobutene, butene, and/or mixtures thereof, wherein the copolymer is partially or completely neutralized.
Shabelina discloses liquid laundry cleaning compositions (see page 5 line 22-23) which may comprise builders and cobuilders (see page 8 line 24-26). Shabelina further discloses suitable cobuilders as polymers of at least maleic acid or maleic anhydride and one or more hydrophobic monomers such as isobutene, diisobutene, and butene (see page 8 line 51-54). Shabelina further teaches builders and cobuilders as acting to bind calcium and magnesium, thereby reducing water hardness (see page 8 line 24-26).
It would have been obvious to one of ordinary skill in the art, before the effective filing date, to utilize the above disclosed cobuilders of Shabelina in the laundry detergent composition of Spangenburg and Juntunen for the purpose of reducing water hardness, as disclosed by Shabelina. Further, Spangenburg discloses the composition comprises at least one builder or co-builder (see page 1 line 6).
With regard to claim 7, Spangenburg and Juntunen disclose all of the limitations of claim 6.
While Spangenburg, Juntunen, and Shabelina do not disclose a K value of 35-45, it stands to reason that the disclosed polymer would meet the requirement of having a K value of 35-45 as the disclosed polymer teaches all of the limitations of claim 6, upon which claim 7 depends. Applicant is directed to MPEP 2112.01(I), “where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977)” and 2112.01(II), "products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
With regard to claim 14, Spangenberg discloses a liquid laundry formulation (see page 1 line 1). Spangenberg further discloses a polymer which is an ethoxylated polyethylenimine with an average molecular weight Mw in the range from 3000 to 250,000 g/mol which has 80 to 99 % by weight ethylene oxide side chains, based on total ethoxylated polyethylenimine, and/or a polymer which is an ethoxylated hexamethylene diamine, quaternized and op- tionally sulfated with an average molecular weight Mw in the range from 2000 to 10,000 g/mol (see page 1 line 10-16). Spangenburg further discloses the ethoxylated hexamethylene diamine as having 20-30 EO per -NH group and a molecular weight of 2,000-10,000 g/mol (see page 9 line 27-29). Spangenburg further discloses the ethoxylated polyethylenimine as having 15-25 EO per -NH group and a molecular weight of 5,000-20,000 g/mol (see page 9 line 17-25). Spangenburg further discloses further optional ingredients, including enzymes which are not protease (see page 27 line 16-21). Spangenburg further discloses a method for removing stains and soil from laundry comprising contacting the laundry with a laundry detergent composition (see Abstract) and further discloses customary ingredients for laundry detergent compositions, including greying inhibitors (see page 25 line 23-25).
However, Spangenburg fails to disclose at least one cellulose, wherein the at least one cellulase is an endo-β-1,4- glucanase which has no carbohydrate binding domain (CBD).
Juntunen discloses polypeptides having cellulase activity (see Abstract). Juntunen further discloses in the detergent industry, an analogous art, cellulases are used to brighten colors and to prevent graying (see [0002]). Juntunen further discloses cellulases as including endoglucanases (EG, EC 3.2.1.4) which cut internal beta-1,4-glucosidic bonds (see [0019]). EC 3.2.1.4 is disclosed in the instant specifications as endo- β-1,4-glucanase. Juntunen further teaches the polypeptide variants may be designed to comprise in addition to the catalytic core domain, which forms the active or functional site of the enzyme, one or more “cellulose binding domains” (“CBDs”) (see [0031]). “May” indicates that such domains are unnecessary and Juntunen further discloses CBDs have carbohydrate-binding activity and they mediate the binding of cellulase to crystalline and amorphous cellulose but have little or no effect on hydrolytic activity of the enzyme on soluble substrates (see [0031]).
It would have been obvious to one of ordinary skill in the art, before the effective filing date, to utilize the endo-β-1,4-glucanase of Juntunen in the laundry detergent composition of Spangenburg for the purpose of to brighten colors and to prevent graying, as disclosed by Juntunen.
However, Spangenburg and Juntunen fail to disclose the liquid composition of claim 1, further comprising component (c), which is a copolymer of (i) maleic acid or maleic anhydride, and (ii) at least one hydrophobic monomer selected from the group consisting of isobutene, diisobutene, butene, and/or mixtures thereof, wherein the copolymer is partially or completely neutralized.
Shabelina discloses liquid laundry cleaning compositions (see page 5 line 22-23) which may comprise builders and cobuilders (see page 8 line 24-26). Shabelina further discloses suitable cobuilders as polymers of at least maleic acid or maleic anhydride and one or more hydrophobic monomers such as isobutene, diisobutene, and butene (see page 8 line 51-54). Shabelina further teaches builders and cobuilders as acting to bind calcium and magnesium, thereby reducing water hardness (see page 8 line 24-26).
It would have been obvious to one of ordinary skill in the art, before the effective filing date, to utilize the above disclosed cobuilders of Shabelina in the laundry detergent composition of Spangenburg and Juntunen for the purpose of reducing water hardness, as disclosed by Shabelina. Further, Spangenburg discloses the composition comprises at least one builder or co-builder (see page 1 line 6).
Response to Arguments
Applicant's arguments filed June 15th, 2026 have been fully considered but they are not persuasive.
Applicant argues that Spangenberg fails to disclose a cellulase and Juntunen fails to disclose a polymer. Applicant further argues that there is no motivation to combine Spangenberg and Juntunen. In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, it would have been obvious to one of ordinary skill in the art, before the effective filing date, to utilize the endo-β-1,4-glucanase of Juntunen in the laundry detergent composition of Spangenburg for the purpose of to brighten colors and to prevent graying, as disclosed by Juntunen.
Applicant further argues that one having ordinary skill in the art would have no reasonable expectation of success for such a modification. As stated above, Spangenburg further discloses further optional ingredients, including enzymes which are not protease (see page 27 line 16-21). Further, Juntunen further discloses cellulases as including endoglucanases (EG, EC 3.2.1.4) which cut internal beta-1,4-glucosidic bonds (see [0019]). As Spangenburg discloses enzymes which are not protease and Juntunen discloses cellulases, one having ordinary skill in the art would have a reasonable expectation of success utilizing the cellulases of Juntunen in the composition of Spangenburg.
Applicant further argues that neither Spangenburg nor Juntunen disclose the amounts of the compositions claimed. As stated above, while Spangenburg fails to disclose 0.5-2wt% of a1 and a2, Spangenburg discloses 3wt% of b1 and b2 (see Table page 30 line 1). One having ordinary skill in the art would find it obvious to optimize within the claimed range disclosed by Spangenburg (see MPEP 2144.05(II) A). Further, Juntenen discloses 0.000001%-3% of variant cellulase polypeptide by weight of the composition (see [0057]).
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to BRITTANY SHARON HARRIS whose telephone number is (571)270-1390. The examiner can normally be reached 7:30-5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Angela Brown-Pettigrew can be reached at (571) 272-2817. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/B.S.H./Examiner, Art Unit 1761
/ANGELA C BROWN-PETTIGREW/Supervisory Patent Examiner, Art Unit 1761
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