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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 May 19, 2026 has been entered.
DETAILED ACTION
Claims 2 and 13-15 are canceled. Claims 1 and 3-12 are pending and under consideration in this action.
The instant claims are entitled to an effective filing date of 07/16/2020.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 5-6 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 5 recites the term “optionally” multiple times in lines 4 ,16, 24, and 30, which renders the claim indefinite because it is unclear which limitations are required, and which are optional. In lines 4-5, claim 5 recites “wherein the compound of formula (I) and/or the compound of formula (II) is optionally present together with a salt of formula (II)”. In one interpretation every limitation recited after the term “optionally” is optional, and under an alternative interpretation the presence of the formula (III) salt is optional. Claim 5 further recites “C7-C9 alkylaryl and cycloalkyl functional groups, where the cycloalkyl ring is optionally a C4-C8 cycloalkyl ring and optionally includes one or more heteroatoms selected from O, N, and S” in lines 15-17. In one interpretation the O, N, and S heteroatoms are only optionally present in C4-C8 cycloalkyl rings, and under an alternative interpretation the O, N, and S heteroatoms are optionally present on any C7-C9 cycloalkyl functional group. Furthermore, claim 5 recites “Y consists of one or more amino acid functional groups and optionally consists of an N-capping functional group” in lines 23-24, which is indefinite because the phrase “consists of” excludes additional elements. Therefore, in one interpretation Y is required to consist of one or more amino acid functional groups or consist of an N-capping functional group, and under an alternative interpretation Y is required to comprise one or more amino acid functional groups with an additional optionally N-capping functional group. Moreover, clam 5 recites “R’’ represents independently of one another, H or a linear or branched, substituted or unsubstituted alkyl group, aryl group or alkenyl group and optionally include one or more heteroatom(s)” in lines 29-31, which is indefinite because in one interpretation the one or more heteroatom(s) is/are optional addition(s) to the required H or a linear or branched, substituted or unsubstituted alkyl group, aryl group or alkenyl group, and under an alternative interpretation the R’’ as a whole can optionally represent one or more heteroatom(s). As such, one of ordinary skill in the art cannot ascertain the metes and bounds of the required versus optional limitations. Claim 6 depends from claim 5 and is rejected for the same reason.
A broad limitation together with a narrow limitation that falls within the broad limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 6 recites the broad recitation “where B2 and B3 are, in each case independently of one another, an amino acid functional group” in lines 15-16, and the claim also recites “where B2 is selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie” in lines 18-19 which is the narrower statement of the limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims. It is unclear whether B2 is required to be selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is required to be selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie, because the scope of B2 and B3 may reasonably be interpreted as encompassing any amino acid functional group.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 6 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 6 recites a broader scope of the B1 than that required in claim 5, from which claim 6 depends. Claim 5 recites “B1 is a single D or L amino acid functional group” in line 22. Claim 6 recites “B1 is an amino acid functional group having an optionally substituted aliphatic pendent group” in lines 13-14. As such, the B1 recited in claim 6 encompasses any amino acid functional group and is not limited to the D or L amino acid functional group required in claim 5. Therefore, claim 6 is of improper dependent form for failing to further limit the subject matter of the claim upon which it depends.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 4 and 10-12 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural product, which is a judicial exception, without significantly more. Each step described below is in reference to the subject matter eligibility test for products and processes (MPEP 2106).
Claim 1 recites an “agent” in line 1. Therefore, the claims are directed to a composition of matter, which is one of the statutory categories (Step 1: Yes).
The recitation “a washing or cleaning” agent in the preamble of claim 1 describes the intended use for the composition without structurally limiting the composition in anyway. See MPEP211.02(II). Claim 1 requires a protease having an amino acid sequence with at least 85% sequence identity with the amino acid sequence specified in SEQ ID NO: 1 over the entire length thereof with at least one amino acid substitution at 12, 43, 122, 127, 154, 156, 160, 211, 212, or 222, wherein the at least one amino acid substitution comprises Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212L, P212H, and A222S. The S8 family peptidase from Alkalicoccobacillus gibsonii, accession no. WP_343130824.1, is 92% identical to instant SEQ ID NO: 1 and includes a M211L mutation relative to instant SEQ ID NO: 1. See Siezen (NCBI accession no. WP_343130824.1, 1997) and the office action appendix for the alignment. Compared to the closest naturally occurring counterpart, there is no structural difference between the natural WP_343130824.1 peptidase and the instantly claimed protease.
Besides the instantly claimed protease, claim 1 requires “(ii) at least one stabilizer compound selected from the group consisting of phenylboronic acid, boric acid, a peptide inhibitor and combinations thereof” and “(iii) a surfactant”. With respect to the (ii) at least one stabilizer, boric acid naturally occurs in the environment and can be found in soil, water and plants, as evidenced by NPIC. See the last passage on page 3 of NPIC mailed 12/04/2024. Moreover, the instant peptide inhibitor encompasses naturally occurring peptide inhibitors such as antipain, which is obtained from Actinomycetes, as evidenced by Suda (1972 Apr;25(4):263-6, as relied upon in the action mailed 12/04/2024). See the second paragraph of the left column on page 269 of Suda. With respect to the (iii) surfactant, the structure of the claimed surfactant is not limited and, consequently, encompasses natural surfactants such as saponins from the sapindus trees/shrubs, as evidenced by Ariza (2025, as relied upon in the action mailed 02/23/2026). See page 9 paragraph 2. Because there is no indication in the record that the instantly disclosed (i) at least one protease with (ii) boric acid and/or a protease inhibitor, and (iii) a surfactant have markedly different characteristics in structure, function, or other properties as compared to their natural counterparts (i.e. WP_343130824.1 peptidase, surfactant, and boric acid and/or antipain) the claims are directed to a natural-product, which is a judicial exception. (Step 2A Prong 1: Yes).
The additional claimed elements separately and accumulatively fail to integrate the product of nature into practical application. Besides the natural product, claim 1 requires the washing or cleaning agent to exhibit increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one stabilizer compound. This additional limitation of claim 1 does not integrate the natural product into a practical application because the limitation is merely an attempt to generally link the natural product to its field of use. Claim 4 requires the proportion by weight of the at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, to range from 0.005 to 5.0 wt.%. This limitation only serves to generally link the natural product to a particular field of use as a washing or cleaning agent because the weight percentage range of claim 4 merely describes suitable protease amounts for use in washing or cleaning agents. As such, the additional limitation of claim 4 does not integrate the natural product into a practical application. Claim 10 limits the weight percentage of the stabilizer compound. The additional limitation of claim 10 does not integrate the natural product into a practical application because the limitation merely serves to link the natural product to its field of use as a washing or cleaning agent. Claim 11 requires the washing or cleaning agent to further comprise an enzyme selected from a group that includes naturally occurring enzymes, such as lipase. As such, the enzyme element of claim 11 is an insignificant addition because the element is a nominal or tangential addition that does not confer a markedly different characteristic to the natural product, absent evidence to the contrary. Claim 12 requires the washing or cleaning agent to further comprise a dishwashing detergent. The “dishwashing detergent” element is recited with a high level of generality, such that the term encompasses naturally occurring detergents. Accumulatively, the additional limitations of claims 4, and 10-12 do not integrate the natural product into a practical application because the limitations either serve to link the natural product to a particular field of use, or the limitations are insignificant additions. (Step 2A Prong 2: No).
The additional elements fail to amount to an inventive concept. It was well-understood that lipase is a naturally occurring enzyme that can be isolated from B. clausii, as evidenced by Lee (Journal of microbiology and biotechnology, 18(12), 1908-1914, 2008; as mailed 12/04/2024) (relevant to the additional element of instant claim 11). Moreover, it was well-understood that dishwashing detergents can be naturally derived, as evidenced by Do (Materials Today: Proceedings, 18, 5219-5230, 2019 as mailed 12/04/2024). Furthermore, O’Connell (WO 2017/207546, as provided in the IDS filed 01/21/2022) teaches protease present in amounts of 0.05-5 wt% and enzyme stabilizers in amounts of 0.05-15% by weight (relevant to instant claims 4 and 10). See paragraph [0046] of O’Connell. Thus, the additional limitations in claims 4 and 10-12 fail to amount to an inventive concept (Step 2B: No).
For all of these reasons, claims 1, 4 and 10-12 are not patent eligible.
Response to Arguments
Applicant's arguments filed 05/19/2026 have been fully considered but they are not persuasive.
§ 101 rejection of claim 1, 4 and 10-12
Applicant argues that at step 2A, prong one, claim 1 does not recite a natural product. Claim 1 requires a protease having at least 85% sequence identity with SEQ ID NO: 1 and further requires that at least one amino acid substitution is selected from Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212D, P212H and A222S based on the numbering according to SEQ ID NO: 1. The office relies on AprBG from Alkalicoccobacillus gibsonii strain DSM 8722 as naturally occurring but the office identifies only a T156S difference relative to SEQ ID NO: 1. T156S is not one of the mandatory substitutions recited in claim 1. Since the claimed composition requires a protease having at least one of the expressly recited engineered substitutions, the claimed protease is structurally different from the alleged natural product. The additional presence of a surfactant and a stabilizer do not convert the claim into a natural product. See the remarks p. 10 para. 3.
This argument is not persuasive because claim 1, as amended, encompasses protease embodiments having at least 85% sequence identity with SEQ ID NO: 1 with a M211L mutation. Alkalicoccobacillus gibsonii, accession no. WP_343130824.1, is 92% identical to instant SEQ ID NO: 1 and includes a M211L mutation relative to instant SEQ ID NO: 1. Furthermore, the instantly claimed at least one stabilizer and surfactant encompass naturally occurring compounds. There is no evidence of record indicating that the claimed protease, stabilizer, and surfactant combination is markedly different compared to the natural counterpart (i.e. the combination of WP_343130824.1 peptidase, surfactant, and boric acid and/or antipain), so the claims are directed to a natural-product judicial exception in step 2A prong one.
Applicant argues that at step 2A, prong two, the claim as a whole integrates the alleged exception into a practical application. The specification explains that proteases in washing and cleaning agents break down protein containing stains but also undergo autoproteolysis and loss of activity during storage, particularly in liquid, or water-containing formulations. Applicant cites the specification [0006]-[0008]. The claimed stabilizer addresses that technical problem in detergent formulation: the specification states that the defined B. gibsonii protease variants can be stabilized by phenylboronic acid derivatives, boric acid, peptide inhibitors, and combinations thereof, and are therefore particularly suitable for washing or cleaning agents. Applicant cites the specification [0011], [0053]. Applicant asserts that the working storage-stability example further confirms the applied detergent context, using an automatic dishwashing detergent matrix containing, among other components, non-ionic surfactant, storing the enzyme-containing matrix at 40˚C for one week, and reporting improved residual activity with 4-FPBA, peptide inhibitor and boric acid. Applicant cites the specification [0150]-[0161]. See the remarks the paragraph spanning pgs. 10-11.
This argument is not persuasive because the storage-stability example cited by Applicant is not commensurate in scope with the instant claims. The specification discloses that protease P1 can be stabilized better by all three stabilizer compounds than proteases P2, P3 or P4. See [0161]. Protease P1 is SEQ ID NO: 5 from WO 2017/215925. See [0155]. The stabilizer compounds include: 1% boric acid [0152], 4-FPBA, which is 4-formylphenylboronic acid, at 2% [0153] and the peptide inhibitor Cbz-Gly-Ala-Tyr-H at 0.5 mM [0154]. P1 is 99.2% identical to instant SEQ ID NO: 1 with the only difference being the M211L and P212D mutations. Instant claim 1 does not limit the protease to an embodiment that is 99.2% identical to instant SEQ ID NO: 1 with M211L and P212D mutations, nor does claim 1 limit the stabilizer to 1% boric acid, 2% 4-FPBA and/or 0.5 mM Cbz-Gly-Ala-Tyr-H. Therefore, Applicant has not cited evidence that the instantly claimed composition, commensurate in scope with the instant claims, has a markedly different characteristic compared to the natural counterpart.
Claim Rejections - 35 USC § 103
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, 3-4, and 10-12 are rejected under 35 U.S.C. 103 as being unpatentable over Wieland (US 2014/0017763).
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Regarding claim 1, Wieland teaches a protease encompassing an amino acid sequence, which is at least 70% identical to the amino acid sequence specified in SEQ ID NO. 1 over the entire length thereof and which, in the listing according to SEQ ID NO. 1, has at least one amino acid substitution selected from a group that includes Q12L, M122L, and A222S. See claim 1 of Wieland. SEQ ID NO: 1 of Wieland is 100% identical to instant SEQ ID NO: 1. See the alignment below.
Wieland teaches a washing system which contains washing liquor together with protease. See [0028]. A preferred liquid washing agent for such a washing system includes non-ionic surfactants, and boric acid. See [0029]. Moreover, Wieland suggests that increasing stability in storage leads to a longer retention of enzymatic activity and hence the cleaning. See [0050].
Wieland does not teach wherein the washing or cleaning agent exhibits increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one compound.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention that Wieland’s washing system containing the protease, the boric acid stabilizer and the surfactant necessarily exhibits increased protease activity after storage compared to a control preparation which differs only due to the absence of the at least one stabilizer compound. MPEP 2112.01(II) states that "products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990).
Regarding claim 3, Wieland teaches at least one amino acid substitution selected from a group that includes Q12L, M122L, and A222S. See claim 1 of Wieland. Wieland teaches protease variant 3, which is SEQ ID NO: 1 with the “G12L” [sic. Q12L], I21V, M122L and A222S substitutions. Wieland’s protease variant 3 is SEQ ID NO: 6, which is 99% identical to instant SEQ ID NO: 1. See [0098]. Thus, protease variant 3 includes the instantly recited Q12L, M122L and A222S substitutions (relevant to (viii) of instant claim 3).
Regarding claim 4, Wieland teaches enzymes that are advantageously contained in the agent in an amount from 1×10−8 to 5 wt%, relative to an active protein. See [0090].
Wieland does not teach at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, that ranges from 0.005 to 5.0 wt.%.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to optimize the working range of the protease. A person of ordinary skill in the art has good reason to pursue the known options within their technical grasp. There would be a reasonable expectation of success because Wieland teaches enzymes in an amount ranging from 1×10−8 to 5 wt. %, which overlaps with the instantly claimed 0.005 to 5.0 wt.%. MPEP 2144.05(II) indicates that differences in concentration generally amount to “routine optimization” and will not support patentability unless there is evidence indicating the claimed feature is critical. “Where 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).
Regarding claim 10, Wieland teaches a preferred liquid washing agent that has 1% boric acid (all figures in percentage by weight). See [0029].
Wieland does not teach an amount ranging from 0.05 to 5.5 wt.% based on the total weight of said washing or cleaning agent.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to optimize the working range of the boric acid in the preferred liquid washing agent of Wieland. Doing so is merely optimizing through routine experimentation. A person of ordinary skill in the art has good reason to pursue the known options within their technical grasp. There would be a reasonable expectation of success because the 1% boric acid amount of Wieland is within the instantly claimed range of 0.05 to 5.5 wt.%. MPEP 2144.05(II) indicates that differences in concentration generally amount to “routine optimization” and will not support patentability unless there is evidence indicating the claimed feature is critical. “Where 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).
Regarding claim 11, Wieland discloses that the washing or cleaning agents can contain further hydrolytic enzymes or other enzymes. All enzymes that can develop a catalytic activity in the agent are preferably suitable for use as further enzymes, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, β-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase or a lipase, and mixtures thereof. See [0090].
Regarding claim 12, Wieland teaches all conceivable types of washing and cleaning agents including dishwashing agents for automatic dishwashers or hand dishwashing agents. See [0083].
Claims 5-9 are rejected under 35 U.S.C. 103 as being unpatentable over Wieland (US 2014/0017763), as applied to claims 1, 3-4, and 10-12 above, and further in view of O’Connell (WO 2017/207546, as provided in the IDS filed 1/21/2022), with evidence from Pubchem (NCBI (2024), Compound Summary for CID 591073; as relied upon in the action mailed 12/04/2024).
Regarding claim 5, Wieland teaches the joint preparation of proteases with protease inhibitors. Wieland suggests that it is desirable for the preparation to have little or no activity during storage and for its enzymatic function to develop only at the moment of use. See [0061].
Wieland does not teach the instantly recited peptide inhibitor.
O’Connell, in example 1, teaches storing proteases with a peptide inhibitor. See [0103]. The peptide inhibitor is methoxycarbonyl-Val-Ala-Leu-aldehyde. See [0081]. O’Connell teaches detergents or cleaning agents, preferably containing a liquid detergent (A) at least one protease; (B) at least one enzyme stabilizer, wherein the at least one enzyme stabilizer is selected from compounds: (I) of the general formula Z-A-NH-CH(R)-C(O)-X where A is an amino acid residue; X is hydrogen; Z is an N-capping residue selected from phosphoramidate [(R'O)2(O)P-], sulfonamide [(SR')2-], sulfonamide [(R'(O)2S-], sulfonic acid, phosphinamide [(R')2(O)P-], sulfamoyl derivatives [R'O(O)2 S-], thiourea [(R')2N(O)C-], thiocarbamate [R'O(S)C-], phosphonate [R'-P(O)OH], amidophosphate [R'O(OH)(O)P-], carbamate (R'O(O)C-) and urea (R'NH(O)C-), where each R' is independently selected from straight chain or branched C1-C6 unsubstituted alkyl, phenyl, C7-C9 alkylaryl and cycloalkyl radicals, where the cycloalkyl ring may be a C4-C8 cycloalkyl ring and may contain one or more heteroatoms selected from O, N, and S; and R is selected from straight-chain or branched C1-C6 unsubstituted alkyl, phenyl and C7-C9 alkylaryl radicals; and stereoisomers, tautomers and salts thereof; or (II) the general structural formula (II) Y-B1-B0-X where X is hydrogen; B1 is a single D or L amino acid residue; Bo is an amino acid residue and Y consists of one or more, preferably one or two, amino acid residues and optionally an N-capping residue, the N-capping residue being as defined under (I); (C) at least one salt of the general structure formula (III) (CE+)p(DF-)q, where C is a cation selected from the group consisting of Al 3+ , Ca 2+ , Li + , Mg 2+ , Mn 2+ , Ni 2+ , K + , NR’’4+ and Na + , each R’’ being independent of one another represents H or a linear or branched, substituted or unsubstituted alkyl, aryl or alkenyl group, all of which may optionally contain one or more heteroatoms; E is an integer from 1 to 3 and corresponds to the valence of the cation; p corresponds to the number of cations in the salt; D is an anion selected from the group consisting of CH3COO- , Br, CO3 2- , Cl- , C3H5O(COO)33-, HCOO- , HCO3-, HSO4-, C2O4 2- , SO4 2- and SO3 2- ; F is an integer of is 1 to 3 and corresponds to the valence of the anion; q corresponds to the number of anions in the salt; where the net charge of the salt is 0. See claim 1 of O’Connell.
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to combine O’Connell’s peptide inhibitor with Wieland’s washing and cleaning agent. One of ordinary skill in the art would have been motivated to do so because Wieland suggests combining protease preparations with peptide inhibitors during storage (see [0061]) and O’Connell suggests that the peptide inhibitor can protect proteins and/or enzymes against proteolytic cleavage during storage (see [0004]). There would have been a reasonable expectation of success because O’Connell demonstrates combining the peptide inhibitor methoxycarbonyl-Val-Ala-Leu-aldehyde (i.e. instant formula (II) Y-B1-B0-X, where Y is valine, B1 is alanine, B0 is Leucine and X is the hydrogen in the aldehyde [-CHO]) with a protease of SEQ ID NO: 1, which is 80.4% identity match with instant SEQ ID NO: 1 and includes a M122L mutation relative to instant SEQ ID NO: 1 (see the alignment provided with the action mailed 12/04/2024).
Regarding claim 6, O’Connell teaches a detergent or cleaning agent, characterized in that
A is selected from Ala, Gly, Val, lle, Leu, Phe and Lys;
R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6H5, CH2, -C6H5, and -CH2-CH2-C6H5; and/or
Z is selected from methyl, ethyl or benzyl carbamate groups [CH3O-(O)C-; CH3CH2O-(O)C-; or C6H5CH2O-(O)C-], methyl, ethyl or benzyl urea groups [CH3NH-(O)C-; CH3CH2NH-(O)C-; or C6H5CH2NH-(O)C-], methyl, ethyl or benzylsulfonamide groups [CH3SO2 -; CH3CH2SO2-; or C6H5CH2SO2-], and a methyl, ethyl or benzylamidophosphate group [CH3O(OH)(O)P-; CH3CH2O(OH)(O)P-; or C6H5CH2O(OH)(O)P-]. See claim 3 of O’Connell.
B0 is a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, lle and Nle;
B1 is an amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle.
Y B2 , B3-B 2 , Z-B2 , ZB3 -B2, where B2 and B3 are each independently an amino acid residue and Z is an N capping residue, where the N capping residue is as defined in claim 1 under (I). See claim 4 of O’Connell.
Regarding claims 7-8, O’Connell teaches reversible protease inhibitors including boric acid and 4-formylphenylboronic acid. See [0005]. The structure of 4-formylphenylboronic acid meets the instantly required structural formula (IV) where R is hydrogen, as evidenced by PubChem.
Regarding claim 9, O’Connell teaches at least one enzyme stabilizer is selected from Cbz-Arg-Ala-Tyr-H, Ac-Gly-Ala-Tyr-H, Cbz-Gly-Ala -Tyr-H, Cbz-Gly-Ala-Tyr-H, Cbz-Val-Ala-Tyr-H, Cbz-Gly-Ala-Phe-H, Cbz-Gly-Ala-Val-H, Cbz-Gly-Gly -Tyr-H, Cbz-Gly-Gly-Phe-H, Cbz-Arg-Val-Tyr-H, Cbz-Leu-Val-Tyr-H, Ac-Leu-Gly-Ala-Tyr-H, Ac-Phe -Gly-Ala-Tyr-H(i.e. instant Ac-SEQ ID NO:21-H), Ac-Tyr-Gly-Ala-Tyr- H(i.e. instant Ac-SEQ ID NO:22-H), Ac-Phe-Gly-Ala-Leu-H(i.e. instant Ac-SEQ ID NO:23-H), Ac-Phe-Gly-Ala-Phe-H (i.e. instant Ac-SEQ ID NO:24-H), Ac-Phe-Gly -Val-Tyr-H(i.e. instant Ac-SEQ ID NO:25-H), Ac-Phe-Gly-Ala-Met-H (i.e. instant Ac-SEQ ID NO:26-H), Ac-Trp-Leu-Val-Tyr-H (i.e. instant Ac-SEQ ID NO: 27-H), MeO-CO-Val-Ala-Leu-H, MeNCO-Val-Ala-Leu -H, MeO-CO-Phe-Gly-Ala-Leu-H (i.e. instant MeO-CO-SEQ ID NO: 28-H), MeO-CO-Phe-Gly-Ala-Phe-H (i.e. instant MeO-CO-SEQ ID NO: 29-H), MeSO2 -Phe-Gly-Ala-Leu-H (i.e. instant MeSO2-SEQ ID NO: 30-H), Me-SO2-Val -Ala-Leu-H, PhCH 2 O(OH)(O)P-Val-Ala-Leu-H, EtSO2 -Phe-Gly-Ala-Leu-H (i.e. instant EtSO2-SEQ ID NO: 31-H), PhCH 2SO2 -Val-Ala-Leu- H, PhCH2O(OH)(O)P-Leu-Ala-Leu-H, PhCH2O(OH)(O)P-Phe-Ala-Leu-H, MeO(OH)(O)P-Leu-Gly-Ala-Leu-H (i.e. MeO(OH)(O)P-SEQ ID NO:32-H), a-MAPI, ß-MAPI, Phe-urea-Arg-Val-Tyr-H, Phe-urea-Gly-Gly-Tyr-H, Phe-urea-Gly-Ala-Phe -H, Phe-urea-Gly-Ala-Tyr-H, Phe-urea-Gly-Ala-Leu-H, Phe-urea-Gly-Ala-Nva-H, Phe-urea-Gly-Ala-Nle-H , Tyr-urea-Arg-Val-Tyr-H, Tyr-urea-Gly-Ala-Tyr-H, Phe-Cys-Ser-Arg-Val-Phe-H (i.e. instant SEQ ID NO: 33), Phe-Cys-Ser-Arg-Val-Tyr -H (i.e. instant SEQ ID NO: 34-H), Phe-Cys-Ser-Gly-Ala-Tyr-H (i.e. instant SEQ ID NO: 35-H), antipain, GE20372A, GE20372B, chymostatin A, chymostatin B and chymostatin C. See paragraphs [0035] and claim 7 of O’Connell.
Response to Arguments
Applicant's arguments filed 05/19/2026 have been fully considered to the extent that they apply to the new grounds of rejection set forth above, but they are unpersuasive.
Rejection of claims 1,3-4, and 10-12 under 35 U.S.C. §103 over Wieland
Applicant argues that Wieland does not explicitly teach the claimed washing or cleaning agent comprising the specifically defined protease together with the recited stabilizer system. The rejection proposes to replace the powdered washing-agent base formulation of Wieland Example 2 with a separate preferred liquid washing agent in Wieland that contains boric acid and surfactants. That reconstruction is not supported by an articulated reason with rationale underpinning. See the remarks p. 13 para. 2.
This argument is not persuasive because MPEP 2123 states that “[a] reference may be relied upon for all that it would have reasonably suggested to one having ordinary skill the art, including nonpreferred embodiments”. In the instant case, Wieland is not relied upon as an anticipatory reference. Rather, the teachings of Wieland render the instantly claimed composition obvious. Wieland teaches a washing system that contains a washing liquor together with a protease including a protease of SEQ ID NO: 1 (see [0028]), and Wieland further discloses that a preferred liquid washing agent for such a washing system can include non-ionic surfactants and boric acid (see [0028]). Moreover, Wieland teaches proteases of SEQ ID NO: 1 with Q12L, M122L and A222S mutations (see claim 1 of Wieland), and Wieland’s SEQ ID NO: 1 is 100% identical to instant SEQ ID NO: 1. In the previous rejection, claims 1 and 3 were rejected together and the rationale discussed replacing the washing agent base formulation in example 2 of Wieland with the liquid washing agent comprising boric acid and non-ionic surfactant, because in example 2 Wieland teaches protease variant 3 with Q12L, M122L and A222 substitution(see [0098]), which meets the requirements of instant claim 3. However, claim 1 does not require a particular combination of substitutions. Therefore, the rejection of claim 1 discussed above no longer relies on that rationale.
Applicant argues that the boric-acid-containing liquid formulation relied upon by the Office is described separately in paragraph [0029] of Wieland, whereas protease variant 3 of Wieland is limited to a specific powdered washing-agent base formulation. Wieland does not disclose that the protease variant 3 is included in that liquid formulation, does not test variant 3 in that liquid formulation and does not report that variant 3 remains effective or stable in that different liquid, boric-acid containing matrix. See the remarks p. 13 para. 2.
This argument is not persuasive for two reasons. The first reason is that the rejection set forth above does not rely on Wieland’s protease variant 3 to meet the instantly required at least one protease limitation of claim 1. The second reason is that Wieland indicates that liquid and powdered washing formulations are interchangeable because Wieland teaches embodiments that encompass all solid, powdered, liquid, gel or paste presentation forms of agents (see [0089]). Although Applicant indicates that Wieland’s protease variant 3 cannot be combined with the Wieland’s liquid formulation comprising boric acid and surfactant, Applicant has not set forth evidence and arguments of counsel cannot take the place of factually supported objective evidence (MPEP 2145 or 716.01(c)).
Applicant argues that Wieland paragraph [0089] merely states in general that agents may have solid, powdered, liquid, gel or paste presentation forms. It does not teach that an enzyme system validated in the powdered example 2 matrix should be transplanted into the distinct liquid formulation of paragraph [0029], much less that doing so would yield the presently claimed surfactant-containing washing or cleaning agent with the required protease and stabilizer. See the remarks p. 14 para. 1. Applicant asserts that the specification explains that enzyme stabilization in washing and cleaning agents is a non-trivial technical problem. The specification further explains that Bacillus gibsonii protease variants can be better stabilized by stabilizer compounds selected from phenylboronic acid derivatives, boric acid, peptide inhibitors and combinations thereof. Applicant cites [0011] of the specification. Applicant argues that the specification describes synergistic enzyme stabilization through interactions among stabilizer compounds including boric acid, 4-FPBA, and peptide inhibitor and provides formulation guidance for stabilizer and protease amounts in washing or cleaning agents. Applicant cites para [0050]-[0052]. See the remarks p. 14 para. 2.
This argument is not persuasive because Wieland meets every structural limitation required in instant claim 1, and Applicant has not pointed to a structural claim element not taught by Wieland. Instant claim 1 and the specification (e.g. see [0011]) indicate that a protease with at least 85% sequence identity with SEQ ID NO: 1 that includes at least one amino acid substitution selected from Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212D, P212H and A222S exhibits stability in the presence of phenylboronic acid derivative, boric acid, a peptide inhibitor and combinations thereof. Wieland’s protease variant 3 (SEQ ID NO: 6) is 99% identical to instant SEQ ID NO: 1 and includes Q12L, M122L and A222S mutations relative to instant SEQ ID NO: 1. Claim 1 does not require the washing or cleaning agent to be a liquid or a powdered solid. Therefore, it is unclear based on Applicant’s argument, how Wieland’s protease variant 3 would not exhibit stability or synergism in the presence of the liquid washing formulation comprising a boric acid stabilizer and surfactant. MPEP 2112.01(II) states that "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).
Applicant asserts that the interchangeability between Wieland’s powdered test matrix and the separate liquid boric-acid formulation is an unsupported hindsight assumption, not a teaching or suggestion in Wieland. See the remarks p. 14 para. 2.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). In the instant case, every limitation is accounted for in the prior art, so nothing is gleaned from the instant disclosure.
Applicant asserts that Wieland does not render independent claim 1 obvious because Wieland does not teach or suggest the specific claimed protease-plus-boric acid detergent composition and because the rejection lacks an articulated reason with rationale underpinning for combining separate embodiments in Wieland in the manner proposed. See p. 14 para. 3.
This argument is not persuasive because claim 1 does not require a specific protease-plus-boric acid detergent composition, since the at least one stabilizer compound of claim 1 is not limited to boric acid.
Applicant argues that O’Connell does not teach an amino acid sequence that is at least 85% identical to SEQ ID NO: 1. See p. 17 para. 1.
This argument is not persuasive because O’Connell is not relied upon for teaching the claimed at least one protease.
Applicant argues that the specification defines improvement of enzyme stability by the presence of the stabilizer compound causing the washing or cleaning agent to have higher enzymatic activity after storage compared to a control preparation that differs only by absence of the stabilizer compound. Applicant cites [0026] of the specification. The specification also evaluates storage stability in automatic dishwashing detergents, stores enzyme-containing detergent matrices with inhibitors at 40˚C for one week, and reports materially different stabilization results depending on the specific protease stabilizer. Applicant cites [0150], [0156], [0160-0161]. The data confirm that the now-claimed increased protease activity after storage is not inherent or routine consequence of merely combining any substilsin-like protease with any peptide inhibitor but instead reflects the particular interaction between the claimed B. gibsonii protease variants and the recited stabilizer system. See p. 18 para. 2.
This argument is not persuasive because the results relied upon by Applicant are not commensurate in scope with the instant claims. The specification discloses that protease P1 can be stabilized better by all three stabilizer compounds than proteases P2, P3 or P4. See [0161]. The stabilizer compounds include: 1% boric acid [0152], 4-FPBA, which is 4-formylphenylboronic acid, at 2% [0153] and the peptide inhibitor Cbz-Gly-Ala-Tyr-H at 0.5 mM [0154]. Protease P1 is SEQ ID NO: 5 from WO 2017/215925. See [0155]. P1 is 99.2% identical to instant SEQ ID NO: 1 with the only difference being the M211L and P212D mutations. Instant claim 1 does not limit the protease to an embodiment that is 99.2% identical to instant SEQ ID NO: 1 with M211L and P212D mutations, nor does claim 1 limit the stabilizer to 1% boric acid, 2% 4-FPBA and/or 0.5 mM Cbz-Gly-Ala-Tyr-H. As such, the results of the disclosed example are not commensurate in scope with the instant claims.
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 1 and 3-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of U.S. Patent No. 10941371 (Herbst ‘371) in view of Mussmann (US 2015/0175939) and O’Connell (WO 2017/07546).
Claim 1 of Herbst ‘371 recites a protease having protease activity and having an amino acid sequence that has at least 82% sequence identity to the amino acid sequence specified in SEQ ID NO:1 [i.e. a 100% identity match to instant SEQ ID NO: 1] over the entire length thereof and that has an amino acid substitution in at least the positions that correspond to positions M211L and P212D with respect to the numbering according to SEQ ID NO:1.
Claim 2 of Herbst ‘371 recites the protease according to claim 1, wherein the protease has at least one amino acid substitution being selected from the group of Q12L, I43V, D127P, N154S, T156A, G160S, and A222S, in each case with respect to the numbering according to SEQ ID NO:1.
Claim 3 of Herbst ‘371 recites the protease according to claim 1, wherein the protease has at least one of the following amino acid substitutions, in each case with respect to the numbering according to SEQ ID NO:1:
(i) I43V;
(ii) M122L, N154S, and T156A;
(iii) G160S;
(iv) D127P;
(v) P212H; or
(vi) Q12L, M122L, and A222S.
Claim 4 of Herbst ‘371 recites an agent, wherein the agent comprises at least one protease according to claim 1.
Claim 5 of Herbst ‘371 recites the agent according to claim 4, wherein the agent is a dishwashing agent.
Claim 6 of Herbst ‘371 recites the protease of claim 1, wherein the protease has utility in a washing or cleaning agent to remove peptide- or protein-containing stains.
Claim 7 of Herbst ‘371 recites the agent according to claim 5, wherein the dishwashing agent is further defined as an automatic dishwashing agent.
Claim 8 of Herbst ‘371 recites the protease of claim 1, wherein the protease comprises an amino acid substitution in a position that corresponds to position I43V with respect to the numbering according to SEQ ID NO: 1.
Claim 9 of Herbst ‘371 recites the protease of claim 1, wherein the protease comprises amino acid substitutions in positions that correspond to positions M122L, N154S, and T156A with respect to the numbering according to SEQ ID NO: 1.
Claim 11 of Herbst ‘371 recites the protease of claim 1, wherein the protease comprises an amino acid substitution in a position that corresponds to position D127P with respect to the numbering according to SEQ ID NO:1.
Claim 12 of Herbst ‘371 recites the protease of claim 1, wherein the protease comprises an amino acid substitution in a position that corresponds to position P212H with respect to the numbering according to SEQ ID NO:1.
Claim 13 of Herbst ‘371 recites the protease of claim 1, wherein the protease comprises amino acid substitutions in positions that correspond to positions Q12L, M122L, and A222S with respect to the numbering according to SEQ ID NO:1.
Claim 14 of Herbst ‘371 recites the protease of claim 1, wherein the protease has an amino acid sequence that has at least 94% sequence identity to the amino acid sequence specified in SEQ ID NO:1 over the entire length thereof.
The patent claims of Herbst ‘371 lack a surfactant, and at least one stabilizer compound selected from the group consisting of a phenylboronic acid derivative, boric acid, a peptide inhibitor, and combinations thereof; and wherein the washing or cleaning agent exhibits increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one stabilizer compound (relevant to instant claim 1). The patent claims of Herbst ‘371 lack a proportion by weight of the at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, ranges from 0.005 to 5.0 wt.% (relevant to instant claim 4). The patent claims of Herbst ‘371 lack a peptide inhibitor selected from the group consisting of a compound of formula (I) Z-A-NH-CH(R)-C(O)-X, compound formula (II) Y-B1-B0-X, and combinations thereof; optionally present together with a salt of formula (III) (CE+)p(DF-)q (relevant to instant claim 5); wherein A is selected from Ala, Gly, Val, Ile, Leu, Phe, and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6Hs, -CH2-C6Hs, and - CH2-CH2-C6Hs; Z is selected from methyl, ethyl, or benzyl carbamate groups, methyl, ethyl or benzylurea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl group, ethyl group or benzyl amidophosphate group;B0 is a D or L amino acid functional group selected from Tyr, m-tyrosine, 3,4- dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile, and Nle; B1 is an amino acid functional group having an optionally substituted small aliphatic pendent group; Y is B2, B3-B2, Z-B2, Z-B3-B2, where B2 and B3 are, in each case independently of one another, an amino acid functional group and Z is an N-capping functional group, wherein the N-capping functional group is as defined in formula (I), where B2 is selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie; and combinations thereof (relevant to instant claim 6). The patent claims of Herbst ‘371 lack a phenylboronic acid derivative that has the general structure of formula (IV) (relevant to instant claim 7); and wherein the derivative is 4-FPBA (relevant to instant claim 8). The patent claims of Herbst ‘371 lack at least one stabilizer compound is selected from the group consisting of 4-FPBA, boric acid, peptide inhibitor, a combination of 4-FPBA and boric acid, a combination of 4-FPBA and peptide inhibitor, a combination of boric acid and peptide inhibitor, and a combination of 4-FPBA and boric acid and peptide inhibitor; wherein the peptide inhibitor is selected from a recited group (relevant to instant claim 9). The patent claims of Herbst ‘371 lack a cleaning or washing agent wherein there occurs at least one condition from the group consisting of: when the at least one stabilizer compound is a peptide inhibitor, said peptide inhibitor is present in the washing or cleaning agent in an amount ranging from 0.01 to 15 wt.% based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is a phenylboronic acid derivative, said phenylboronic acid derivative is present in the washing or cleaning agent in an amount ranging from 0.0005 to 2.0 wt.%, based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is boric acid, said boric acid is present in the washing or cleaning agent in an amount ranging from 0.05 to 5.5 wt.%, based on the total weight of said washing or cleaning agent; and combinations thereof (relevant to instant claim 10). The patent claims of Herbst ‘371 lack a washing or cleaning agent further comprising at least one further enzyme selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, (3-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipase, and combinations thereof (relevant to instant claim 11). The patent claims of Herbst ‘371 lack a washing or cleaning agent according to further comprising a dishwashing detergent (relevant to instant claim 12).
However, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with boric acid, 4-formylphenylboronic acid (i.e. 4-FPBA a phenylboronic acid derivative), and non-ionic surfactant. See example 1 in paragraphs [0105] and [0106]. Mussman suggests that the combination of a protease with 4-formylphenylboronic acid are not only stable in storage, but are distinguished by higher enzymatic cleaning performance. See [0014] (relevant to instant claims 1, 7, 8). Mussmann teaches a cleaning agent with protease at 0.005 to 1.0 wt. %. See claims 2-3 and paragraph [0096] (relevant to instant claim 4). O’Connell teaches detergents with at least one enzyme stabilizer selected from formulas (I) Z-A-NH-CH(R)-C(O)-X, and (II) (II) Y-B1-B0-X. See claim 1 of O’Connell (relevant to instant claim 5). O’Connell teaches A is selected from Ala, Gly, Val, lle, Leu, Phe and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6H5, CH2, -C6H5, and -CH2-CH2-C6H5; and/or Z is selected from methyl, ethyl or benzyl carbamate groups, methyl, ethyl or benzyl urea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl, ethyl or benzylamidophosphate group. See claim 3 of O’Connell. Furthermore, O’Connell teaches B0 is a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, lle and Nle; B1 is an amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. Y B2 , B3-B 2 , Z-B2 , ZB3 -B2, where B2 and B3 are each independently an amino acid residue and Z is an N capping residue, where the N capping residue is as defined in claim 1 under (I). See claim 4 of O’Connell (relevant to instant claim 6). O’Connell teaches at least one enzyme stabilizer selected from a group that includes Cbz-Arg-Ala-Tyr-H, e.g. a peptide inhibitor. See paragraph [0035] and claim 7 of O’Connell (relevant to instant claim 9). Mussmann teaches formulas a cleaning agent comprising a proportion by weight of 4-FPBA that is 0.0005 to 2 wt%. See claim 4 and paragraph [0096] (relevant to instant claim 10). Mussmann teaches at least one further enzyme other than protease, wherein the enzyme is at least one from amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases or a lipase and the mixtures thereof. See claims 1 and 5 of Mussmann (relevant to instant claim 11). Mussmann suggests that the cleaning agents may assume a combination of solid and liquid presentations [0084] (relevant to instant claim 12).
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to combine the mutated protease (SEQ ID NO: 1) of Herbst ‘371 with the peptide inhibitor of O’Connell or the 4-FPBA and boric acid and non-ionic surfactant of Mussmann; and to further optimize the weight percentages of each component in order to formulate a washing or cleaning agent.
Claims 1 and 3-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of U.S. Patent No. 9260706 (hereafter Wieland ‘706) in view of Mussmann (US 2015/0175939) and O’Connell (WO 2017/07546).
Claim 1 of Wieland ‘706 recites a protein comprising a protease which is at least 90% identical to SEQ ID NO. 1 over the full-length and comprises the substitution corresponding to I21V of SEQ ID NO. 1, and further comprising at least one further amino acid substitution corresponding to Q12L, M122L, N177V, A222S, V2228I or T247N of SEQ ID NO. 1 [i.e. 100% identical to instant SEQ ID NO: 1].
Claim 10 of Wieland ‘706 recites a protein comprising a protease according to claim 2, in which a fragment dissociates from the protease, and the protease remains active, wherein protease activity is provided by one or more fragments of the protease that is at least 90% identical to SEQ NO. 1.
Claim 11 of Wieland ‘706 recites a protein comprising a protease according to claim 1, in which the protease is at least 95% identical to SEQ ID NO. 1 over the entire length thereof.
Claim 12 of Wieland ‘706 recites the protein comprising a protease according to claim 1, wherein the protease is defined by SEQ ID. NO. 4.
Claim 13 of Wieland ‘706 recites the protein comprising a protease according to claim 1, wherein the protease is defined by SEQ ID. NO. 5.
Claim 14 of Wieland ‘706 recites the protein comprising a protease according to claim 1, wherein the protease is defined by SEQ ID. NO. 6 [i.e. Q12L, I21V, M122L and A222S substitutions].
The patent claims of Wieland ‘706 lack a surfactant, and at least one stabilizer compound selected from the group consisting of a phenylboronic acid derivative, boric acid, a peptide inhibitor, and combinations thereof; and wherein the washing or cleaning agent exhibits increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one stabilizer compound (relevant to instant claim 1). The patent claims of Wieland ‘706 lack a proportion by weight of the at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, ranges from 0.005 to 5.0 wt.% (relevant to instant claim 4). The patent claims of Wieland ‘706 lack a peptide inhibitor selected from the group consisting of a compound of formula (I) Z-A-NH-CH(R)-C(O)-X, compound formula (II) Y-B1-B0-X, and combinations thereof; optionally present together with a salt of formula (III) (CE+)p(DF-)q (relevant to instant claim 5); wherein A is selected from Ala, Gly, Val, Ile, Leu, Phe, and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6Hs, -CH2-C6Hs, and - CH2-CH2-C6Hs; Z is selected from methyl, ethyl, or benzyl carbamate groups, methyl, ethyl or benzylurea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl group, ethyl group or benzyl amidophosphate group;B0 is a D or L amino acid functional group selected from Tyr, m-tyrosine, 3,4- dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile, and Nle; B1 is an amino acid functional group having an optionally substituted small aliphatic pendent group; Y is B2, B3-B2, Z-B2, Z-B3-B2, where B2 and B3 are, in each case independently of one another, an amino acid functional group and Z is an N-capping functional group, wherein the N-capping functional group is as defined in formula (I), where B2 is selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie; and combinations thereof (relevant to instant claim 6). The patent claims of Wieland ‘706 lack a phenylboronic acid derivative that has the general structure of formula (IV) (relevant to instant claim 7); and wherein the derivative is 4-FPBA (relevant to instant claim 8). The patent claims of Wieland ‘706 lack at least one stabilizer compound is selected from the group consisting of 4-FPBA, boric acid, peptide inhibitor, a combination of 4-FPBA and boric acid, a combination of 4-FPBA and peptide inhibitor, a combination of boric acid and peptide inhibitor, and a combination of 4-FPBA and boric acid and peptide inhibitor; wherein the peptide inhibitor is selected from a recited group (relevant to instant claim 9). The patent claims of Wieland ‘706 lack a cleaning or washing agent wherein there occurs at least one condition from the group consisting of: when the at least one stabilizer compound is a peptide inhibitor, said peptide inhibitor is present in the washing or cleaning agent in an amount ranging from 0.01 to 15 wt.% based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is a phenylboronic acid derivative, said phenylboronic acid derivative is present in the washing or cleaning agent in an amount ranging from 0.0005 to 2.0 wt.%, based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is boric acid, said boric acid is present in the washing or cleaning agent in an amount ranging from 0.05 to 5.5 wt.%, based on the total weight of said washing or cleaning agent; and combinations thereof (relevant to instant claim 10). The patent claims of Wieland ‘706 lack a washing or cleaning agent further comprising at least one further enzyme selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, (3-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipase, and combinations thereof (relevant to instant claim 11). The patent claims of Wieland ‘706 lack a washing or cleaning agent according to further comprising a dishwashing detergent (relevant to instant claim 12).
However, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with boric acid, and 4-formylphenylboronic acid (i.e. 4-FPBA a phenylboronic acid derivative) and non-ionic surfactant. See example 1 in paragraphs [0105] and [0106]. Mussman suggests that the combination of a protease with 4-formylphenylboronic acid are not only stable in storage, but are distinguished by higher enzymatic cleaning performance. See [0014] (relevant to instant claims 1, 7, 8). Mussmann teaches a cleaning agent with protease at 0.005 to 1.0 wt. %. See claims 2-3 and paragraph [0096] (relevant to instant claim 4). O’Connell teaches detergents with at least one enzyme stabilizer selected from formulas (I) Z-A-NH-CH(R)-C(O)-X, and (II) (II) Y-B1-B0-X. See claim 1 of O’Connell (relevant to instant claim 5). O’Connell teaches A is selected from Ala, Gly, Val, lle, Leu, Phe and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6H5, CH2, -C6H5, and -CH2-CH2-C6H5; and/or Z is selected from methyl, ethyl or benzyl carbamate groups, methyl, ethyl or benzyl urea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl, ethyl or benzylamidophosphate group. See claim 3 of O’Connell. Furthermore, O’Connell teaches B0 is a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, lle and Nle; B1 is an amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. Y B2, B3-B 2, Z-B2 , ZB3 -B2, where B2 and B3 are each independently an amino acid residue and Z is an N capping residue, where the N capping residue is as defined in claim 1 under (I). See claim 4 of O’Connell (relevant to instant claim 6). O’Connell teaches at least one enzyme stabilizer selected from a group that includes Cbz-Arg-Ala-Tyr-H, e.g. a peptide inhibitor. See paragraph [0035] and claim 7 of O’Connell (relevant to instant claim 9). Mussmann teaches formulas a cleaning agent comprising a proportion by weight of 4-FPBA that is 0.0005 to 2 wt%. See claim 4 and paragraph [0096] (relevant to instant claim 10). Mussmann teaches at least one further enzyme other than protease, wherein the enzyme is at least one from amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases or a lipase and the mixtures thereof. See claims 1 and 5 of Mussmann (relevant to instant claim 11). Mussmann suggests that the cleaning agents may assume a combination of solid and liquid presentations [0084] (relevant to instant claim 12).
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to combine the mutated protease (SEQ ID NO: 6) of Wieland ‘706 with the peptide inhibitor of O’Connell or the 4-FPBA, boric acid and surfactant of Mussmann; and to further optimize the weight percentages of each component in order to formulate a washing or cleaning agent.
Claims 1 and 3-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 7449187 (hereafter Weber ‘187) in view of Wieland (US 2014/0017763), Mussmann (US 2015/0175939), and O’Connell (WO 2017/07546).
Claim 3 of Weber ‘187 recites an isolated protein comprising a polypeptide that is at least 95% identical to SEQ ID NO: 3 [i.e. 100% identical to instant SEQ ID NO: 1], wherein the polypeptide exhibits alkaline protease activity.
The patent claims of Weber ‘187 lack a surfactant, and at least one stabilizer compound selected from the group consisting of a phenylboronic acid derivative, boric acid, a peptide inhibitor, and combinations thereof; and wherein the washing or cleaning agent exhibits increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one stabilizer compound (relevant to instant claim 1) and at least one protease that has at least one amino acid substitution selected from a group that includes Q12L, M122L and A222S (relevant to instant claim 3). The patent claims of Weber ‘187 lack a proportion by weight of the at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, ranges from 0.005 to 5.0 wt.% (relevant to instant claim 4). The patent claims of Weber ‘187 lack a peptide inhibitor selected from the group consisting of a compound of formula (I) Z-A-NH-CH(R)-C(O)-X, compound formula (II) Y-B1-B0-X, and combinations thereof; optionally present together with a salt of formula (III) (CE+)p(DF-)q (relevant to instant claim 5); wherein A is selected from Ala, Gly, Val, Ile, Leu, Phe, and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6Hs, -CH2-C6Hs, and - CH2-CH2-C6Hs; Z is selected from methyl, ethyl, or benzyl carbamate groups, methyl, ethyl or benzylurea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl group, ethyl group or benzyl amidophosphate group;B0 is a D or L amino acid functional group selected from Tyr, m-tyrosine, 3,4- dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile, and Nle; B1 is an amino acid functional group having an optionally substituted small aliphatic pendent group; Y is B2, B3-B2, Z-B2, Z-B3-B2, where B2 and B3 are, in each case independently of one another, an amino acid functional group and Z is an N-capping functional group, wherein the N-capping functional group is as defined in formula (I), where B2 is selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie; and combinations thereof (relevant to instant claim 6). The patent claims of Weber ‘187 lack a phenylboronic acid derivative that has the general structure of formula (IV) (relevant to instant claim 7); and wherein the derivative is 4-FPBA (relevant to instant claim 8). The patent claims of Weber ‘187 lack at least one stabilizer compound is selected from the group consisting of 4-FPBA, boric acid, peptide inhibitor, a combination of 4-FPBA and boric acid, a combination of 4-FPBA and peptide inhibitor, a combination of boric acid and peptide inhibitor, and a combination of 4-FPBA and boric acid and peptide inhibitor; wherein the peptide inhibitor is selected from a recited group (relevant to instant claim 9). The patent claims of Weber ‘187 lack a cleaning or washing agent wherein there occurs at least one condition from the group consisting of: when the at least one stabilizer compound is a peptide inhibitor, said peptide inhibitor is present in the washing or cleaning agent in an amount ranging from 0.01 to 15 wt.% based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is a phenylboronic acid derivative, said phenylboronic acid derivative is present in the washing or cleaning agent in an amount ranging from 0.0005 to 2.0 wt.%, based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is boric acid, said boric acid is present in the washing or cleaning agent in an amount ranging from 0.05 to 5.5 wt.%, based on the total weight of said washing or cleaning agent; and combinations thereof (relevant to instant claim 10). The patent claims of Weber ‘187 lack a washing or cleaning agent further comprising at least one further enzyme selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, (3-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipase, and combinations thereof (relevant to instant claim 11). The patent claims of Weber ‘187 lack a washing or cleaning agent according to further comprising a dishwashing detergent (relevant to instant claim 12).
However, Wieland teaches protease variant 3 is SEQ ID NO: 1 with the “G12L” [sic. Q12L], I21V, M122L and A222S substitutions (SEQ ID NO: 6). See [0098]. Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with boric acid, non-ionic surfactant and 4-formylphenylboronic acid (i.e. 4-FPBA a phenylboronic acid derivative). See example 1 in paragraphs [0105] and [0106]. Mussman suggests that the combination of a protease with 4-formylphenylboronic acid are not only stable in storage, but are distinguished by higher enzymatic cleaning performance. See [0014] (relevant to instant claims 1, 3 part (viii), 7, and 8). Mussmann teaches a cleaning agent with protease at 0.005 to 1.0 wt %. See claims 2-3 and paragraph [0096] (relevant to instant claim 4). O’Connell teaches detergents with at least one enzyme stabilizer selected from formulas (I) Z-A-NH-CH(R)-C(O)-X, and (II) (II) Y-B1-B0-X. See claim 1 of O’Connell (relevant to instant claim 5). O’Connell teaches A is selected from Ala, Gly, Val, lle, Leu, Phe and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6H5, CH2, -C6H5, and -CH2-CH2-C6H5; and/or Z is selected from methyl, ethyl or benzyl carbamate groups, methyl, ethyl or benzyl urea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl, ethyl or benzylamidophosphate group. See claim 3 of O’Connell. Furthermore, O’Connell teaches B0 is a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, lle and Nle; B1 is an amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. Y B2 , B3-B 2 , Z-B2 , ZB3 -B2, where B2 and B3 are each independently an amino acid residue and Z is an N capping residue, where the N capping residue is as defined in claim 1 under (I). See claim 4 of O’Connell (relevant to instant claim 6). O’Connell teaches at least one enzyme stabilizer selected from a group that includes Cbz-Arg-Ala-Tyr-H, e.g. a peptide inhibitor. See paragraph [0035] and claim 7 of O’Connell (relevant to instant claim 9). Mussmann teaches formulas a cleaning agent comprising a proportion by weight of 4-FPBA that is 0.0005 to 2 wt%. See claim 4 and paragraph [0096] (relevant to instant claim 10). Mussmann teaches at least one further enzyme other than protease, wherein the enzyme is at least one from amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases or a lipase and the mixtures thereof. See claims 1 and 5 of Mussmann (relevant to instant claim 11). Mussmann suggests that the cleaning agents may assume a combination of solid and liquid presentations [0084] (relevant to instant claim 12).
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to mutate SEQ ID NO: 3 of Weber ‘187 in view of protease variant 3 of Wieland, and to further combine it with the peptide inhibitor of O’Connell or the 4-FPBA of Mussmann, and the non-ionic surfactant and boric acid of Mussmann; and to further optimize the weight percentages of each component in order to arrive at a washing or cleaning agent.
Claims 1 and 3-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 11104867 (hereafter Mussmann ‘867) in view of Mussmann (US 2015/0175939) and O’Connell (WO 2017/07546).
Claim 1 of Mussmann ‘867 recites a dishwashing agent comprising a source of hydrogen peroxide comprising sodium percarbonate, a bleach catalyst and a protease, wherein the bleach catalyst comprises a complex of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me-TACN), and wherein the protease has an amino acid sequence that is at least 98% identical to the amino acid sequence listed in SEQ ID NO. 2 [99.9% identical to instant SEQ ID NO: 1 the only difference is the I43V mutation], wherein the agent exhibits improved cleaning on tea stains compared to an agent containing just the sodium percarbonate and bleach catalyst but not the protease.
Claim 2 of Mussmann ‘867 recites the dishwashing agent according to claim 1, wherein the protease has an amino acid sequence identical to the amino acid sequence listed in SEQ ID NO. 2.
Claim 3 of Mussmann ‘867 recites the dishwashing agent according to claim 1, wherein the agent comprises the hydrogen peroxide source in an amount of 2 to 30 wt. %, the bleach catalyst in an amount of 0.0025 to 1 wt. %, and the protease in an amount of 1×10−8 to 10 wt. % based on the total protein content of the protease.
The patent claims of Mussmann ‘867 lack a surfactant, and at least one stabilizer compound selected from the group consisting of a phenylboronic acid derivative, boric acid, a peptide inhibitor, and combinations thereof; and wherein the washing or cleaning agent exhibits increased protease activity after storage compared to a control preparation which differs from the washing or cleaning agent only due to the absence of the at least one stabilizer compound (relevant to instant claim 1). The patent claims of Mussmann ‘867 lack a proportion by weight of the at least one protease with respect to the total weight of the washing or cleaning agent, based on active protein, ranges from 0.005 to 5.0 wt.% (relevant to instant claim 4). The patent claims of Mussmann ‘867 lack a peptide inhibitor selected from the group consisting of a compound of formula (I) Z-A-NH-CH(R)-C(O)-X, compound formula (II) Y-B1-B0-X, and combinations thereof; optionally present together with a salt of formula (III) (CE+)p(DF-)q (relevant to instant claim 5); wherein A is selected from Ala, Gly, Val, Ile, Leu, Phe, and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6Hs, -CH2-C6Hs, and - CH2-CH2-C6Hs; Z is selected from methyl, ethyl, or benzyl carbamate groups, methyl, ethyl or benzylurea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl group, ethyl group or benzyl amidophosphate group;B0 is a D or L amino acid functional group selected from Tyr, m-tyrosine, 3,4- dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, Ile, and Nle; B1 is an amino acid functional group having an optionally substituted small aliphatic pendent group; Y is B2, B3-B2, Z-B2, Z-B3-B2, where B2 and B3 are, in each case independently of one another, an amino acid functional group and Z is an N-capping functional group, wherein the N-capping functional group is as defined in formula (I), where B2 is selected from Val, Gly, Ala, Arg, Leu, Phe, and Thr, and/or B3 is selected from Phe, Tyr, Trp, phenylglycine, Leu, Val, Nva, Nle and Iie; and combinations thereof (relevant to instant claim 6). The patent claims of Mussmann ‘867 lack a phenylboronic acid derivative that has the general structure of formula (IV) (relevant to instant claim 7); and wherein the derivative is 4-FPBA (relevant to instant claim 8). The patent claims of Mussmann ‘867 lack at least one stabilizer compound is selected from the group consisting of 4-FPBA, boric acid, peptide inhibitor, a combination of 4-FPBA and boric acid, a combination of 4-FPBA and peptide inhibitor, a combination of boric acid and peptide inhibitor, and a combination of 4-FPBA and boric acid and peptide inhibitor; wherein the peptide inhibitor is selected from a recited group (relevant to instant claim 9). The patent claims of Mussmann ‘867 lack a cleaning or washing agent wherein there occurs at least one condition from the group consisting of: when the at least one stabilizer compound is a peptide inhibitor, said peptide inhibitor is present in the washing or cleaning agent in an amount ranging from 0.01 to 15 wt.% based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is a phenylboronic acid derivative, said phenylboronic acid derivative is present in the washing or cleaning agent in an amount ranging from 0.0005 to 2.0 wt.%, based on the total weight of said washing or cleaning agent; when the at least one stabilizer compound is boric acid, said boric acid is present in the washing or cleaning agent in an amount ranging from 0.05 to 5.5 wt.%, based on the total weight of said washing or cleaning agent; and combinations thereof (relevant to instant claim 10). The patent claims of Mussmann ‘867 lack a washing or cleaning agent further comprising at least one further enzyme selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, (3-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipase, and combinations thereof (relevant to instant claim 11). The patent claims of Mussmann ‘867 lack a washing or cleaning agent according to further comprising a dishwashing detergent (relevant to instant claim 12).
However, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with boric acid, non-ionic surfactant and 4-formylphenylboronic acid (i.e. 4-FPBA a phenylboronic acid derivative). See example 1 in paragraphs [0105] and [0106]. Mussman suggests that the combination of a protease with 4-formylphenylboronic acid are not only stable in storage but are distinguished by higher enzymatic cleaning performance. See [0014] (relevant to instant claims 1, 7, 8). Mussmann teaches a cleaning agent with protease at 0.005 to 1.0 wt. %. See claims 2-3 and paragraph [0096] (relevant to instant claim 4). O’Connell teaches detergents with at least one enzyme stabilizer selected from formulas (I) Z-A-NH-CH(R)-C(O)-X, and (II) (II) Y-B1-B0-X. See claim 1 of O’Connell (relevant to instant claim 5). O’Connell teaches A is selected from Ala, Gly, Val, lle, Leu, Phe and Lys; R is selected from methyl, iso-propyl, sec-butyl, iso-butyl, -C6H5, CH2, -C6H5, and -CH2-CH2-C6H5; and/or Z is selected from methyl, ethyl or benzyl carbamate groups, methyl, ethyl or benzyl urea groups, methyl, ethyl or benzylsulfonamide groups, and a methyl, ethyl or benzylamidophosphate group. See claim 3 of O’Connell. Furthermore, O’Connell teaches B0 is a D- or L-amino acid residue selected from Tyr, m-tyrosine, 3,4-dihydroxyphenylalanine, Phe, Val, Met, Nva, Leu, lle and Nle; B1 is an amino acid residue with an (optionally substituted) small aliphatic side group, preferably Ala, Cys, Gly, Pro, Ser, Thr, Val, Nva or Nle. Y B2 , B3-B 2 , Z-B2 , ZB3 -B2, where B2 and B3 are each independently an amino acid residue and Z is an N capping residue, where the N capping residue is as defined in claim 1 under (I). See claim 4 of O’Connell (relevant to instant claim 6). O’Connell teaches at least one enzyme stabilizer selected from a group that includes Cbz-Arg-Ala-Tyr-H, e.g. a peptide inhibitor. See paragraph [0035] and claim 7 of O’Connell (relevant to instant claim 9). Mussmann teaches formulas a cleaning agent comprising a proportion by weight of 4-FPBA that is 0.0005 to 2 wt%. See claim 4 and paragraph [0096] (relevant to instant claim 10). Mussmann teaches at least one further enzyme other than protease, wherein the enzyme is at least one from amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases or a lipase and the mixtures thereof. See claims 1 and 5 of Mussmann (relevant to instant claim 11). Mussmann suggests that the cleaning agents may assume a combination of solid and liquid presentations [0084] (relevant to instant claim 12).
It would have been obvious to a person of ordinary skill in the art prior to the effective filing date of the instantly claimed invention to combine the SEQ ID NO: 2 of Mussmann ‘867 with the peptide inhibitor of O’Connell or the 4-FPBA and the non-ionic surfactant and boric acid of Mussmann; and to further optimize the weight percentages of each component in order to arrive at a washing or cleaning agent.
Response to Arguments
Applicant's arguments filed 05/19/2026 have been fully considered but they are not persuasive.
Non-statutory Double Patenting Rejections
Applicant argues claims 1 and 3-12 stand provisionally rejected under the judicially created doctrine of obviousness-type double patenting as being unpatentable over: the patent claims of U.S. Patent No. 10,941,371 to Herbst in view of Mussmann ‘939 and O’Connell (see the remarks p. 19 para. 2); the patent claims of U.S. Patent No. 9,260,706 to Wieland in view of Mussmann ‘939 and O’Connell (see the remarks p. 19 para. 4); the patent claims of U.S. Patent No. 7,449,187 to Weber, in view of Wieland ‘763, Mussmann ‘939 and O’Connell (see the remarks p. 20 para. 1); and the patent claims of 11,104,867 to Mussmann in view of Mussmann ‘939, and O’Connell (see the remarks p. 20 para. 3). Applicant defers responding to the provisional rejections until claims in the present application are otherwise allowable, and it is determined whether this provisional rejection becomes an actual rejection. See the remarks p. 19 paragraphs 3 and 5, and p. 20 paragraphs 2, and 4.
The double patenting rejections are not provisional rejections because the claims of U.S. Patent Nos: 10941371 (Herbst ‘371), 9260706 (Wieland ‘706), 7449187 (Weber ‘187), and 11104867 (Mussmann ‘867) have been patented. Furthermore, a deferral does not constitute as a response. As such, the double patenting rejections of record have been maintained as no response to these rejections has been filed by Applicant at this time.
Conclusion
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/K.C.B./Examiner, Art Unit 1657
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