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 .
DETAILED ACTION
Claims 2 and 13-15 are canceled. Claims 1 and 3-12 are pending.
Priority
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1 and 3-12 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 1 recites “a washing or cleaning agent with a surfactant comprising” in line 2, which is indefinite because it is unclear whether the agent or the surfactant is required to comprise the (i) at least one protease and (ii) at least one stabilizer elements.
Claim 1 requires “at least one amino acid substitution at at least one of the positions corresponding to the positions 12, 43, 122, 127, 154, 156, 160, 211, 212, or 222…[and] wherein at least one of the at least one amino acid substitution is selected from the group consisting of Q12L, I43V, M211N, M211L, P212D, P212H, or A222S”. The required substitution is unclear because the Markush group of substitutions (i.e. Q12L…A222S) does not reference positions 122, 127, 154, 156, or 160 as recited earlier in the claim. Consequently, there are multiple reasonable interpretations of the claim. In the first interpretation, the claim encompasses any substitution at positions 122, 127, 154, 156, or 160, because the Markush group only limits the substitutions at positions 12, 43, 211, 212 and 222. In other words, in this first interpretation claim 1 encompasses M122X, D127X, N154X, T156X and G160X substitutions. In the second interpretation, the claim requires at least one substitution selected from the group consisting of Q12L, I43V, M211N, M211L, P212D, P212H, or A222S, such that there is at least at one amino acid substitution at, at least one of the positions corresponding to positions 12, 43, 211, 212 or 222. However, in this interpretation the claim does not encompass substitutions at positions 122, 127, 154, 156, or 160. To obviate this rejection, claim 1 can be amended to delete “122, 127, 154, 156, 160” from line 6, or claim 1 can be amended, such that the Markush group of substitutions references position 122, 127, 154, 156, and 160.
Claims 3-12 depend from claim 1 and are rejected for the reason set forth above.
Response to Arguments
Applicant's arguments filed 12/08/2025 have been fully considered but they are not persuasive.
The maintained §112(b) rejection of claims 1 and 3-12
Applicant argues that the amendment overcomes the rejection. See the first paragraph on page 13 of the remarks.
This argument is not persuasive because the claim amendment does not rectify the indefinite issue discussed above. It is unclear whether claim 1 encompasses (a) at least one amino acid substitution selected from Q12L, I43V, 122, 154, 156, 160, M211N, M211L, P212D, P212H, or A222S; or (b) at least one amino acid substitution selected from Q12L, I43V, M211N, M211L, P212D, P212H, or A222S and optional additional mutations at positions 122, 154, 156, and/or 160.
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 a “composition” in line 1. Therefore, the claims are directed to a composition of matter, which is one of the statutory categories (Step 1: Yes).
Claim 1 recites “a washing or cleaning agent” in the preamble, which merely describes the intended use for the composition without structurally limiting the composition in anyway. See MPEP211.02(II). Claim 1 requires a surfactant comprising 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 and has at least one amino acid substitution at at least one of the positions corresponding to the positions 12, 43, 122, 127, 154, 156, 160, 211, 212, or 222. As discussed above, claim 1 may reasonably be interpreted as encompassing any substitution at positions 122, 127, 154, 156, or 160. The AprBG (S5VEF0_9BACI) protein from Alkalicoccobacillus gibsonii strain DSM 8722 is a 90.5% identity match to instant SEQ ID NO: 1 and includes a T154S mutation relative to instant SEQ ID NO: 1. See the office action appendix for the alignment and see Uniprot for the S5VEF0_9BACI sequence (reference U on page 1 of the PTO-892 form). Nielsen discloses that the source of the DSM 8722 is soil. See the first passage in the right column on page 1759 and table 1. Compared to the closest naturally occurring counterpart, there is no structural difference between the natural AprBG protein and the instantly claimed protease, which encompasses substitutions at the T154X residue relative to instant SEQ ID NO: 1.
Besides the instantly claimed protease, claim 1 requires “a surfactant” and “at least one stabilizer compound selected from the group consisting of phenylboronic acid, boric acid, a peptide inhibitor and combinations thereof”. The surfactant is not limited and encompasses natural surfactants such as saponins from the sapindus trees/shrubs, as evidenced by Ariza (2025, reference U on the PTO-892 form). See page 9 paragraph 2. 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. For support that Actinomycetes is a naturally occurring microorganism, see the abstract of Ngamcharugchit (Molecules, 28(15), 5915, 2023, as mailed 12/04/2024). Because there is no indication in the record that the instantly disclosed protease with boric acid and/or a protease inhibitor have markedly different characteristics in structure, function, or other properties as compared to their natural counterparts (AprBG from A. gibsonii DSM 8722, 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 ( AprBG from A. gibsonii DSM 8722, surfactant and boric acid and/or antipain), claim 1 does not require any additional elements that could integrate the natural product into a practical application. 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) (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 12/08/2025 have been fully considered but they are not persuasive.
The maintained § 101 rejection of claim 1, 4 and 10-12
Applicant argues that “a washing or cleaning agent” is a non-natural composition discussed at least in paragraph [0082] of the specification. It is not an intended use. Therefore, the claim passes revised step 2A as it does not recite a natural phenomenon or product. See the second to last full paragraph on page 13 of the remarks.
This argument is not persuasive because MPEP 2111.01(II) states that “[t]hough understanding the claim language may be aided by explanations contained in the written description, it is important not to import into a claim limitations that are not part of the claim”. In the instant case, the specification does not define a washing or cleaning agent in a way that is inconsistent with the plain meaning. Paragraph [0082] discloses that the washing or cleaning agents “may be in the form of powdered solids, in further-compacted particulate form, as homogeneous solutions or suspension, may contain, in addition to a protease and a stabilizer compound, all known ingredients conventional in such agents. The agents can in particular contain surfactants”. However, this description does not limit the structure of the claimed composition. As such, the answer to step 2A prong 1 is yes because the claim recites a natural product.
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).
Regarding claims 1 and 3, 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, and A222S. See claim 1. SEQ ID NO: 1 of Wieland is 100% identical to instant SEQ ID NO: 1. See the alignment below. Wieland teaches a preferred liquid washing agent that comprises (all figures in percentage by weight): 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% non-ionic surfactants, and 1% boric acid. See [0029]. In example 2, Wieland teaches adding protease variant 3 to a powdered washing agent base formulation. See [0102] and table 1. Protease variant 3 is SEQ ID NO: 1 with the “G12L” [sic. Q12L], I21V, M122L and A222S substitutions (SEQ ID NO: 6). See [0098]. The washing agent base formulation includes: 10% linear alkylbenzene sulfonate (sodium salt), 1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium hydrogen carbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxohydrate, 4.0%. TAED, 3.0% polyacrylate, 1.0% carboxymethyl cellulose, 1.0% phosphonate, 27% sodium sulfate, remainder: foam inhibitors, optical brightener, fragrances. See [0101]. After washing, the whiteness of the textiles is measured using a spectrometer. See [0103]. Batch 3, comprising protease variant 3, shows a relative performance of 250% compared to the 100% of the Bacillus gibsonii DSM 14391 alkaline protease SEQ ID NO: 1 standard. See table 1. Thus, Wieland teaches a protease variant with Q12L, M122L and A222S substitutions (relevant to instant claim 3 part (viii)) and suggests a liquid washing agent comprising boric acid and non-ionic surfactants.
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Wieland does not teach the instantly claimed washing or cleaning agent comprising at least one stabilizer compound selected from a group consisting of a phenylboronic acid derivative, boric acid, a peptide inhibitor and combinations thereof with sufficient specificity, because Wieland does not explicitly teach combining the protease variant 3 in example 2 with the specific liquid washing agent comprising boric acid.
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 replace the washing agent base formulation in example 2 of Wieland with the liquid washing agent comprising boric acid and non-ionic surfactant. Doing so is merely substituting known prior art equivalents. One would be prompted to replace the solid washing base formulation in example 2 with the preferred liquid washing agent because Wieland suggests that the solid and liquid forms are interchangeable (see [0089]). One would be motivated to use the liquid formulation comprising boric acid in particular, because Wieland suggests that it is a preferred liquid formulation. There would be a reasonable expectation of success because Wieland demonstrates washing textiles with a protease variant 3 containing Q12L, M122L and A222S substitutions and a solid washing agent base formulation; and Wieland further suggests that solid formulations are interchangeable with liquid formulations, such as the liquid formulation comprising 1% boric acid.
Regarding claim 4, Wieland a protease applied in an amount from 40 μg to 4 g per application. See claim 12. Wieland teaches proteases in an amount from 40 μg to 4 g, preferably from 50 μg to 3 g, particularly preferably from 100 μg to 2 g and most particularly preferably from 200 μg to 1 g. See [0091]. Wieland teaches further enzymes that are advantageously contained in the agent in an amount from 1×10−8 to 5 wt. %, relative to an active protein. Each further enzyme is increasingly preferably contained in agents in an amount from 1×10−7 to 3 wt. %, from 0.00001 to 1 wt. %, from 0.00005 to 0.5 wt. %, from 0.0001 to 0.1 wt. % and particularly preferably from 0.0001 to 0.05 wt. %, relative to 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 variant 3 in the washing agent. 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 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 in an appropriate concentration for the effectiveness of the agent. 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, both concentrates and agents intended for use in undiluted form, for use on a commercial scale, in washing machines or for hand washing or cleaning. They include for example washing agents for textiles, carpets or natural fibers for which the term washing agent is used. They also include for example dishwashing agents for automatic dishwashers or hand dishwashing agents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, coated surfaces, plastics, wood or leather, for which the term cleaning agent is used, i.e. in addition to hand and automatic dishwashing agents for example also scouring agents, glass cleaners, toilet fresheners, etc. See [0083].
Claims 1, 3-4, 7-8 and 10-12 are rejected under 35 U.S.C. 103 as being unpatentable over Mussmann (US 2015/0175939) in view of Weber (US 2005/0003504).
Regarding claim 1, Mussmann teaches protease- and amylase- containing cleaning agents which are sufficiently stable in storage and have improved amylolytic activity. See [0004]. Mussmann teaches a cleaning agent comprising a) at least one protease which comprises an amino acid sequence which is at least 80% identical over its entire length of SEQ ID NO: 1 and has a glutamic acid at position 99 according to the numbering of SEQ ID NO: 1, b) 4-formylphenylboronic acid, c) at least one further enzyme other than the protease. See claim 1. In example 1, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with boric acid, a protease preparation, 4-formylphenylboronic acid (i.e. 4-FPBA a phenylboronic acid derivative) and nonionic surfactant C8-C10 fatty alcohol ethoxylate with 22 ethylene oxide units (EO). See [0105] and [0106]. The enzyme phase is combined for various test batches with preparations of proteases, such as E1: protease, wherein the E1 protease is SEQ ID NO: 1 with a glutamic acid [instead of arginine] in position 99. See paragraphs [0108]-[0109]. SEQ ID NO: 1 of Mussmann is an 80.8% identity match to instant SEQ ID NO: 1, and SEQ ID NO: 1 of Mussmann with an E residue at position 99 (i.e. the E1 protease) is an 80.4% identity match to instant SEQ ID NO: 1. See the alignment provided in the office action appendix mailed 12/04/2024. Moreover, SEQ ID NO: 1 of Mussmann is from Bacillus lentus and includes the instantly claimed M211L substitution with respect to instant SEQ ID NO: 1. Mussmann suggests that preferred proteases have the amino acid leucine (L) at position 211 according to the numbering of SEQ ID NO: 1. See [0017].
Mussmann does not teach at least one 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.
Weber teaches a washing or cleaning product comprising an isolated polypeptide comprising an amino acid sequence having at least 70% identity with SEQ ID NO: 2 or a fragment or derivative thereof. See claims 1 and 39. Weber teaches an isolated polypeptide comprising an amino acid sequence having at least 70% identity with SEQ ID NO: 2 or a fragment thereof produced by at least one insertion of mutagenesis, substitution mutagenesis, or fusion with at least one other protein or protein fragment. See claims 1 and 21. Weber teaches an isolated polypeptide comprising an amino acid sequence having at least 90% with SEQ ID NO: 2 in positions 115 to 384. See claim 5. Position 384 of SEQ ID NO: 2 is a stop codon and thus does not correspond to an amino acid. See [0083]. Residues 115-383 of SEQ ID NO: 2 are a 100% identity match to instant SEQ ID NO: 1. See the alignment in the office action appendix. In example 2, Weber teaches the homology of alkaline protease from Bacillus gibsonii (DSM 14391) to the most similar and further representative proteins. See [0342] and table 2. The amino acid sequences of these proteases are compared in the alignment in figure 1. See [0343]. The top sequence in figure 1 corresponds to SEQ ID NO: 3, a protease from B. gibsonii (DSM 14391) that is 100% identical to instant SEQ ID NO: 1. See paragraph [0041]. As shown in figure 1, the M211 residue of SEQ ID NO: 3 aligns with the L residues of SEQ ID NO: 5, a Savinase ® (SUBS_BACLE) from B. lentus, and SEQ ID NO: 6, subtilisin BL (SUBB_BACLE) from B. lentus. In example 6, Weber discloses that the protease of B. gibsonii DSM 14391 exhibits better washing performance on textiles than the established proteases B. lentus alkaline protease F49 and Savinase ®. See [0356]-[0361]. Weber notes that homologous regions of different proteins are those having comparable functions which can be recognized by identity or conserved exchanges in the primary amino acid sequence. See [0057]-[0058]. Furthermore, Weber discloses that, during storage, a protein may be protected by stabilizers from, for example, denaturing, decay or inactivation. See [0283]. Weber suggests that boric acid and para-substituted phenylboronic acids, or salts or esters thereof are examples of stabilizers. See [0284]. Thus, Weber teaches SEQ ID NO: 3, which is 100% identical to instant SEQ ID NO: 1, Weber suggests a M211L mutation with respect to SEQ ID NO: 3 in figure 1, and Weber suggests using stabilizers to protect proteins during storage.
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 substitute the M211 residue in SEQ ID NO: 3 of Weber with leucine in view of Mussman, and to further replace the E1 protease in the biphasic liquid automatic dishwashing agent of Mussman with the modified SEQ ID NO: 3 with the M211L mutation. Doing so is mere substitution. One would be motivated to substitute the M211 residue of Weber with leucine (L) because Mussman suggests that proteases containing L at position 211 are preferential in protease- and amylase- containing cleaning agents which are sufficiently stable in storage and have improved amylolytic activity. There would be a reasonable expectation of success because, according to the alignment of Weber, the 211 position of SEQ ID NO: 3 is not conserved across similar proteases from different species. One would be further prompted to use the modified protease of Weber and Mussman in the in the biphasic liquid automatic dishwashing agent of Mussman, because Weber discloses that the protease from B. gibsonii DSM 14391 (i.e. SEQ ID NO: 3) exhibits better washing performance on textiles than B. lentus alkaline protease. There would be a reasonable expectation of success because Webber suggests combining protease proteins with stabilizers such as boric acid and para-substituted phenylboronic acids; and the biphasic liquid automatic dishwashing agent of Mussman includes boric acid and 4-FPBA.
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Regarding claim 3, Mussmann teaches SEQ ID NO: 1 which includes M122L, D127P, N154S, T156A, G160S, and M211L substitutions with respect to instant SEQ ID NO: 1. See the office action appendix mailed 12/04/2024. Thus Mussmann suggests M122L, N154S and T156A substitutions (relevant to part (ii) of instant claim 3), and a G160S substitution (relevant to part (v) of instant claim 3)
However, SEQ ID NO: 1 of Mussman is not at least 85% identical to instant SEQ ID NO: 1 (relevant to instant claim 1).
Weber teaches SEQ ID NO: 3, which is 100% identical to instant SEQ ID NO: 1. See paragraph [0041] and figure 1. As shown in figure 1, the I43 residue in SEQ ID NO: 3 aligns with V residues of SEQ ID NOs: 10-16. Furthermore, the proteases from B. lentus, i.e. SEQ ID NOs: 5 and 6, include the following mutations with respect to SEQ ID NO: 3: M122L, D127P, N154S, T156A, G160S, and M211L. See figure 1 or the image above and paragraph [0041] of Weber.
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 replace any of the non-conserved amino acid residues in SEQ ID NO: 3 of Weber with a corresponding residue in figure 1 of Weber, and to further specifically select the M122L, D127P, N154S, T156A, G160S, and M211L substitutions in view of Mussmann. In the process, one would arrive at SEQ ID NO: 3 with the M122L, 154S and 156A substitutions (relevant to instant part (ii)), and a G160S substitution (relevant to instant part (v)). One would be prompted to substitute residues in accordance with figure 1 of Weber, because Weber suggests that homologous regions of different proteins have comparable functions ([0057]-[0058]). One would be particularly motivated mutate SEQ ID NO: 3 of Weber according to SEQ ID NOs: 5 and 6 of Weber (i.e. the M122L, D127P, N154S, T156A, G160S, and M211L substitutions present in the B. lentus proteases), because Mussman the same mutations in SEQ ID NO: 1 and suggests that SEQ ID NO: 1 can be used as a protease in protease-and amylase-containing cleaning agents that are sufficiently stable (e.g. see [0004]). There would be a reasonable expectation of success because Mussman and Weber teach proteases with M122L, D127P, N154S, T156A, G160S, and M211L mutations.
Regarding claim 4, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with a protease preparation at 3.5 weight percent [0106]. Furthermore, Mussmann teaches a cleaning agent with a proportion by weight of protease in the total weight of the cleaning agent relative to active protein amounts that is 0.005 to 1.0 wt. %. See claims 2-3 and paragraph [0096] for example formulas 1, 6 , 16, 26, and 31.
Mussmann does not explicitly teach a weight proportion of protease that ranges from 0.005 to 5 wt %. Weber does not teach a weight proportion of protease that ranges from 0.005 to 5 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 workable range of the protease weight proportion in the biphasic liquid automatic dishwashing agent of Mussman and Weber discussed above. Doing so is mere optimization through routine experimentation. There would be a reasonable expectation of success because Mussmann demonstrates a dishwashing agent comprising 3.5 wt. %, which is within the instantly claimed range. 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 claims 7-8, Mussmann a biphasic liquid automatic dishwashing agent comprising an enzyme phase with 4-formylphenylboronic acid (i.e. 4-FPBA, a phenylboronic acid derivative). See example 1 in paragraphs [0105] and [0106]. Evidentiary reference PubChem teaches the structure of 4-FPBA. As shown herein. The structure of 4-FPBA aligns with the structural formula (IV) of instant claim 7, where R is hydrogen.
Regarding claim 10, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with 4-FPBA (i.e. a phenylboronic acid derivative) at 0.02 wt %. See paragraph [0106]. Furthermore, 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] for formulas 1, 11, 16, 26, 21 and 31.
Regarding claim 11, Mussmann teaches a biphasic liquid automatic dishwashing agent comprising an enzyme phase with a protease preparation and an amylase preparation. See example 1 in paragraphs [0105] and [0106]. Furthermore, Mussmann teaches a cleaning agent comprising at least one protease which is at least 80% identical to SEQ ID NO:1 and has E at position 99 and 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.
Regarding claim 12, Mussmann teaches detergent or cleaning agent with improved enzyme performance and, in particular, cleaning agents for automatic dishwashing and textile cleaning. See the title and paragraph [0002]. For example, Mussmann teaches a dishwashing agent comprising a protease preparation, 4-FPBA, and boric acid [0106]. Mussmann suggests that the cleaning agents may assume a combination of solid and liquid presentations [0084]. Cleaning agents added to the composition including nonionic surfactants which are interpreted as detergents, see paragraph [0031]. These nonionic surfactant cleaning agents are used in dishwashing methods, see paragraph [0049] and thus meet the limitation of a dishwashing detergent.
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 any of the dishwashing agents of Mussmann with the biphasic liquid automatic dishwashing agent of Mussman and Weber discussed above, such that the biphasic liquid automatic dishwashing agent further comprises a dishwashing detergent including surfactants. Doing so is merely combining known prior art elements. One would be motivated to further combine the biphasic liquid automatic dishwashing agent of Mussmann and Weber with an additional dishwashing agent/detergent because Mussmann suggests combining solid and liquid presentations and that dishwashing embodiments preferably further contain cleaning agents such as surfactants. There would be a reasonable expectation of success because Mussmann demonstrates formulating dishwashing agents with protease, 4-FPBA and boric acid.
Claims 1, 3, 5, 6 and 9 are rejected under 35 U.S.C. 103 as being unpatentable over O’Connell (WO 2017/207546, as provided in the IDS filed 1/21/2022) in view of Weber (US 2005/0003504).
Regarding claims 1, 3 and 5, O’Connell teaches identifying compounds that increase the protease stabilizer performance of peptide-based protease stabilizers and are suitable for use in detergents and cleaning agents. See [0011]. 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. O’Connell teaches agents containing surfactants. See [0073].
In example 1, O’Connell teaches storing proteases SEQ ID Nos 1-3 with a peptide inhibitor, methoxycarbonyl-Val-Ala-Leu-aldehyde. See paragraphs [0081]-[0103] and [0060]. SEQ ID NO: 1 of O’Connell is an 80.4% identity match with instant SEQ ID NO: 1 and includes the following substitutions with respect to instant SEQ ID NO: 1: M122L, D127P, N154S, T156A and M211L mutation. Thus, O’Connell suggests a M211L mutation (relevant to instant claim 1) and substitutions M122L, N154S and T156A (relevant to instant claim 3 part (ii)). See the office action appendix mailed 12/04/2024 for the alignments. Furthermore, O’Connell teaches the alkaline protease from Bacillus gibsonii DSM 14391 or an alkaline protease that is at least 70% identical thereto. See [0057].
O’Connell does not teach an amino acid sequence that is at least 85% identical to instant SEQ ID NO: 1.
Weber teaches the homology of alkaline protease from Bacillus gibsonii (DSM 14391) to the most similar and further representative proteins. See [0342] and table 2. The amino acid sequences of these proteases are compared in the alignment in figure 1. See [0343]. The top sequence in figure 1 corresponds to SEQ ID NO: 3, a protease from B. gibsonii (DSM 14391) that is 100% identical to instant SEQ ID NO: 1. See paragraph [0041]. As shown in figure 1, the proteases from B. lentus, i.e. SEQ ID NOs: 5 and 6, include the following mutations with respect to SEQ ID NO: 3: M122L, D127P, N154S, T156A, G160S, and M211L. See figure 1 or the image above and paragraph [0041] of Weber. In example 6, Weber discloses that the protease of B. gibsonii DSM 14391 exhibits better washing performance on textiles than the established proteases B. lentus alkaline protease F49 and Savinase ®. See [0356]-[0361].
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 replace any of the non-conserved amino acid residues in SEQ ID NO: 3 of Weber with a corresponding residue in figure 1 of Weber, to specifically select the M122L, D127P, N154S, T156A and M211L substitutions in view of O’Connell, to use that modified protease in the composition of example 1 taught by O’Connell and to further add a surfactant. In the process, one would arrive at SEQ ID NO: 3 with a M211L substitution (relevant to instant claim 1), the M122L, 154S and 156A substitutions (relevant to instant part (ii)), and a G160S substitution (relevant to instant part (v)) in a with a composition with the peptide inhibitor, methoxycarbonyl-Val-Ala-Leu-aldehyde. One would be prompted to substitute residues in accordance with figure 1 of Weber, because Weber suggests that homologous regions of different proteins have comparable functions ([0057]-[0058]). One would be particularly motivated mutate SEQ ID NO: 3 of Weber according to SEQ ID NOs: 5 and 6 of Weber (i.e. the M122L, D127P, N154S, T156A, G160S, and M211L substitutions present in the B. lentus proteases), because O’Connell suggests that a protease with said substitutions, i.e. SEQ ID NO: 1 of O’Connell, can be stabilized with the compounds and peptide inhibitors taught by O’Connell. There would be a reasonable expectation of success because O’Connell and Weber both teach the protease from B. gibsonii (DSM 14391) and the M122L, D127P, N154S, T156A, G160S, and M211L substitutions. One would be further motivated to use the modified protease of O’Connell and Weber in the composition of O’Connell because Weber suggests that the protease from B. gibsonii DSM 14391 exhibits better washing performance on textiles. There would be a reasonable expectation of success because O’Connell teaches the protease from B. gibsonii DSM 14391 and sequences that are at least 70% identical thereto. One would be motivated to combine the composition of O’Connell and Weber with a surfactant because 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 O’Connell explicitly teaches agents that can contain surfactants.
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 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 12/08/2025 have been fully considered but they are unpersuasive.
The maintained §103 rejections over Mussmann or O’Connell combined with Weber
Applicant states that the Mussmann and O’Connell references were previously cited for now overcome §102 anticipation rejections. Applicant reiterates and reincorporates by reference prior arguments regarding Mussmann and O’Connell. See the second paragraph on page 15 of the remarks.
This argument is not persuasive because it is unclear which arguments Applicant intends to reiterate and reincorporate. In the final rejection mailed 05/02/2025, claims 1, 3, 7-8 and 10-11 were rejected under 102(a)(1) as being anticipated by Mussmann, and claims 1, 3, 5, 6 and 9 were rejected under 102(a)(1) as being anticipated by O’Connell. Applicant arguments concerning these previous rejections were addressed on pages 24-25 of this final action mailed 05/02/2025.
Applicant asserts that Weber does not cure the deficiencies of Mussmann or O’Connell because Weber provides no teaching or disclosure of the claimed substitutions. See the second paragraph on page 15 of the remarks. Furthermore, Applicant argues that Weber only proves a generic homology discussion but does not teach editing B. gibsonii at the precise claimed positions (12, 43, 122, 127, 154, 160, 211, 212, and 222). See the second to last paragraph on page 16 of the remarks. Applicant argues that the mutation “transfer” rationale is too generic. The office relies on Weber’s alignment and generic homology asserts to suggest borrowing residues from other Bacillus proteases into B. gibsonii. See the first paragraph on page 17 of the remarks.
This argument is not persuasive because Weber is not relied upon for teaching the claimed substitutions alone. Rather, Mussmann is relied upon for teaching the M211L substitution of instant claim 1, because SEQ ID NO: 1 of Mussmann includes (L) at position 211 and Mussmann suggests that preferred proteases have leucine at position 211. See [0017] of Mussmann. Furthermore, O’Connell is relied upon for teaching the M211L substitution of instant claim 1 because SEQ ID NO: 1 of O’Connell includes that substitution.
Applicant argues that Mussmann teaches proteases that keep Glu at position 99 protect co-formulated amylase in the presence of 4-FPBA. The text repeatedly stresses this E99 residue. Applicant references [0003], [0006], [0088], [0101], [0109] and claim 1 of Mussmann. See the last full paragraph on page 15 of the remarks. Applicant asserts that the DSM-1491 sequence of Webber retains the native Arg99, and Weber celebrates the native sequence for superior textile performance. Applicant references [0342]-[0361] of Weber. See the paragraph bridging pages 15-16 of the remarks. Applicant argues that substituting Weber’s Arg99 enzyme into Mussmann’s system would, on Mussmann’s own data abolish the very benefit sought. That is classic teaching away.
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”. Merck & Co. v. Biocraft Laboratories, 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert. denied, 493 U.S. 975 (1989). Mussmann does not teach or suggest that proteases without E99 would be inoperable as a protease. SEQ ID NO: 3 of Weber includes arginine (R) at position 99, and is 100% identical to instant SEQ ID NO: 1. However, instant claim 1 encompasses proteases with additional substitutions, because claim 1 only requires the protease sequence to be at least 85% identical to SEQ ID NO: 1.
Applicant argues that the combination of O’Connell and Weber do not provide a reasonable motivation for introducing the precise, finite set of claimed substitutions into the B. gibsonii protease, nor does it disclose a detergent embodiment that combines such a mutated B. gibsonii protease with O’Connell’s stabilizer system or 4-FPBA at the claimed levels. See the third and fifth paragraphs on page 16 of the remarks.
This argument is not persuasive because it is not commensurate in scope with the instant claims. Claim 1 is a product claim that requires a protease structure that has at least one amino acid substitution selected from a group that includes M211L. As such, the claim does not require an active step of introducing substitutions, as argued; nor does the claim require a set of claimed substitutions [i.e. a plurality of substitutions]. Applicant argues that O’Connell and Weber do not teach a stabilizer system or 4-FPBA at the claimed levels. However, it is unclear which claimed element is being referenced because claim 1 does not require the at least one stabilizer compound to be at any particular level. As such, O’Connell meets the at least one stabilizer limitation of claim 1 because O’Connell teaches a peptide inhibitor that is identical to formula (I) of instant claim 5. See claim 1 of O’Connell, specifically the Z-A-NH-CH(R)-C(O)-X formula.
The maintained §103 rejection over Wieland
Applicant argues that the mutations of Wieland are fundamentally different from claim 1. The protease of Wieland is anchored on an I21V substitution, which is not required in instant claim 1. Wieland does not teach or suggest edits at 43, 211, or 212 in B. gibsonii. Furthermore, Wieland’s core teachings begin at ≥70% identity, whereas the instant claims require at least 85% identity to instant SEQ ID NO: 1. See the paragraph bridging pages 17-18 of the remarks.
This argument is not persuasive because it is not commensurate in scope with the instant claims. The claims encompass additional substitutions not recited in the claims. Wieland teaches the claimed Q12L and A222S mutations. See claim 1 of Wieland. Furthermore, SEQ ID NO: 1 of Wieland is 100% identical to instant SEQ ID NO: 1.
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.
(Modified to address amendment) 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, hereafter Herbst ‘371 in view of Mussmann US 2015/0175939, 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 (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] (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 dishwashing 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, 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 (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] (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 dishwashing 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, 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 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 claims 1 and 3 part (viii)). 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] (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 formulate a dishwashing agent.
(Modified to address amendment) 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, 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 2 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 (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] (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 formulate a dishwashing agent.
Response to Arguments
Applicant's arguments filed 12/08/2025 have been fully considered but they are not persuasive.
Non-statutory Double Patenting Rejections
Applicant argues that the rejections are provisional. See paragraphs 2, 4, and 6 on page 18 and the first paragraph on page 19 of the remarks.
For clarity of the record, the double patenting rejections discussed above 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.
Applicant defers responding to the rejections until the claims in the present application are otherwise allowable. See paragraphs 3 and 5 on page 18, the paragraph bridging pages 18-19, and paragraph 2 on page 19 of the remarks.
This 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
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.
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/K.C.B./Examiner, Art Unit 1657