DETAILED ACTION
Status of Application
Claims 1-14, and 16 are pending
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
A preliminary amendment of claims 1-3, 6-10, 13-14, and 16 and cancellation of claim 15 as submitted in a communication filed on 07/24/2026 is acknowledged.
Applicant’s election with traverse of Group 1, claims 1-10, drawn to a cleaning composition, comprising (a) at least one variant lipolytic enzyme; (b) at least one cellulase (c) at least one surfactant, as submitted in communication filed on 07/24/2026 is acknowledged.
Applicant’s traverse is on the grounds that it would not pose an undue burden on the Examiner nor constitute a non-coextensive search, to examine all the claims together, because the method and use claims do not introduce a separate inventive concept. Applicant’s arguments have been fully considered but not deemed persuasive to withdraw the restriction requirement. It is noted that the restriction is being made due to the technical feature of the inventions not making a contribution over the prior art and not meeting the requirement of unity of invention under PCT Rule 13.2. Thus, the requirement is deemed proper and therefore is made FINAL.
Claims 11-14 and 16 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made with traverse in the reply filed on 07/24/2026.
Applicant’s species election without traverse as submitted in communication filed on 07/24/2026 is acknowledged below:
Species Group 1: F207T
Species Group 2: 75%
Species Group 3: V14S-R40A-G59Y-G61D-T64V-S70E-T117L-Q 161H-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q- R256K-L258F
Species Group 4: PET
Claims 1-10 are at issue and will be examined to the extent they encompass the elected invention.
Priority
Acknowledgment is made of applicant’s claim for domestic priority under 35
U.S.C. 119 (e) to provisional Application No. 63/216557 filed on 06/30/2021.
This is the US national application which entered the national stage from
Application No. PCT/EP2022/067510 filed on 06/27/20222.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/19/2023
is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Objections
Claim 4 is objected to due to the spaces between/among amino acid substitutions (highlighted below). It should be amended to remove unnecessary spaces/gaps. Appropriate correction is required.
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Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA )
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.
Claim 9 is 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 9 is indefinite due to the recitation of “unit dose” for the following reasons: It is unclear because it lacks objective boundaries and the term is not well-defined in the art, making it unclear what ingredient dosage meets the limitation. For examination purposes, “unit dose” will be interpreted as any dose. Correction is required.
Claim Rejections - 35 USC § 112(a) or First Paragraph (pre-AIA )
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-10 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
As stated in MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow.
Claims 1-10 are directed in part to a cleaning composition, comprising (a) a genus of variant lipolytic enzymes, wherein said variant lipolytic enzymes comprise an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions: T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; (b) at least one cellulase; and (c) at least one surfactant, in an amount of 2 to 30 wt.%; wherein said variant lipolytic enzyme has any structure.
As indicated in MPEP § 2163, the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show that Applicant was in possession of the claimed genus. In addition, MPEP § 2163 states that a representative number of species means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
The claims encompass a large genus of enzymes which are structurally unrelated or substantially unrelated. A polypeptide having at least 70 % sequence identity with the polypeptide of SEQ ID NO: 2 allows for any combination of 77 amino acid modifications within SEQ ID NO: 2 (77.4 = 0.3x258; SEQ ID NO: 2 has 258 amino acids). The total number of variants of a polypeptide having a specific number of amino acid substitutions can be calculated from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference polypeptide and A is the number of allowed substitutions. Thus, the total number of variants having at least 70% sequence identity with the polypeptide of SEQ ID NO: 2 that result from amino acid substitutions is 258!x1977/(258-77)!/77! or 3.136239 × 10165 variants with exception of the recited substitutions. A sufficient written description of a genus of lipolytic enzyme may be achieved by a recitation of a representative number of enzymes defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of lipolytic enzymes recited in the claims, or the recited structural feature, i.e., 70% sequence identity to SEQ ID NO: 2 with the recited substitutions, is not representative of all the members of the genus of enzyme recited since there is no information as to which are the structural elements within the enzyme variants of SEQ ID NO: 2 with the recited substitutions that is essential for lipolytic activity, which are the remaining structural elements required in the recited enzymes in addition to those recited in the claims such that the desired lipolytic activity is displayed, or a correlation between structure and function which would provide those unknown structural features. Furthermore, while one could argue that the few species disclosed are representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate (Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol. 183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98% amino acid sequence identity catalyze two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the few species disclosed are representative of the structure of all the lipolytic enzymes in the claimed composition.
Claims 1-10 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a cleaning composition, comprising at least one variant lipolytic enzyme having the amino acid sequence of SEQ ID NO: 2 with the recited substitutions, does not reasonably provide enablement for a cleaning composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2 having the recited substitutions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows: 1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3) the presence and absence of working examples, 4) the nature of the invention, 5) the state of prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art, and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the specification fails to teach how to make and/or use the claimed invention without undue experimentation, are addressed in detail below.
The breadth of the claims. Claims 1-10 broadly encompass a cleaning composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO:2 while having the recited substitutions. The enablement provided is not commensurate in scope with the claims due to the lack of knowledge regarding the structural features that are representative of all the members of the genus of lipolytic enzyme variants having any structure, and having at least 70% sequence identity to the polypeptide of SEQ ID NO: 2 with the recited substitutions.
The amount of direction or guidance presented and the existence of working examples. The specification discloses SEQ ID NO: 2 and lists substitutions corresponding to SEQ NO: 2. However, the specification fails to provide any clue as to the structural elements required in any lipolytic enzyme having 70% identity with SEQ ID NO: 2 with the recited substitutions corresponding to SEQ ID NO: 2.
The state of prior art, the relative skill of those in the art, and the predictability or unpredictability of the art. The structure of an enzyme determines its structural and functional properties. While the art discloses a limited number of lipolytic enzymes or SEQ ID NO: 2 polypeptide variants, neither the specification nor the art provides a correlation between structure and function such that one of skill in the art can envision the structure of an enzyme or any SEQ ID NO: 2 polypeptide variant that can be a lipolytic enzyme. The art clearly teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate (Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol. 183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98% amino acid sequence identity catalyze two different reactions: deamination and dehalogenation, therefore having different function (Abstract).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of determining the function and activity of enzyme variants were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of enzymes and SEQ ID NO: 2 variants to find an enzyme or SEQ ID NO: 2 variant with the desired lipolytic activity. In the absence of (i) a rational and predictable scheme for selecting the enzyme or SEQ ID NO: 2 variant most likely to have the desired features, (ii) a correlation between structure and function, one of skill in the art would have to test an infinite number of enzymes and SEQ ID NO: 2 variants.
Therefore, taking into consideration the extremely broad scope of the claim, the lack of guidance, the amount of information provided, the lack of knowledge about a correlation between structure and the desired function, the high degree of unpredictability in the prior art regarding enzymatic activity and polypeptide variance, one of ordinary skill in the art would have to go through the burden of undue experimentation in order to practice the claimed invention. Thus, Applicant has not provided sufficient guidance to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the scope of the claims.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-7 and 9-10 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Adams et al. (US 2024/0150738 A1 published 03/09/2024, filed 03/17/2021; hereby “Adams”).
Claims 1-7 and 9-10 as interpreted are directed in part to a cleaning composition, comprising (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions: T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; (b) at least one cellulase; and (c) at least one surfactant in an amount of 2 to 30 wt%, further comprising at least one further enzyme in an amount of 0.001 to 1 wt%, and at least one further enzyme in an amount of 0.001 to 1 wt%, more preferably 0.005 to 0.5 wt% ;-ands (d) at least one performance polymer in an amount of 0.05 to 5 wt%; wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75% and 90% identity to the full-length amino acid sequence of SEQ ID NO:2; wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of R40T- T64V-T 117L-G175E-T 177N-F180P-Y 182A-R190L-S205G-F207L-S212D-F226L-Y239I- L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D- F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N- I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-G175A-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET), wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt%, wherein the cellulase is contained in the composition in an amount of from 0.00001 to 1 wt.%; wherein (i) the cleaning composition further comprises at least one additional ingredient selected from the group consisting of; builders, bleaching agents, bleach activators, water- miscible organic solvents, sequestering agents, electrolytes, pH regulators, optical brighteners, graying inhibitors, foam regulators, dyes and fragrances and combinations thereof; and/or (ii) it has a pH of 7.0 to 11.0 as measured in 1 wt.% aqueous solution at 20°C; and/or (iii) it is present in solid or liquid form; and/or (iv) it is in unit dose.
Adams teaches variant lipolytic enzymes comprising an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2, comprising one or more substitutions at positions selected from the group consisting of 14, 70, 117, 161, 175, 212, 226, 236, 239, 252, 254, 256, and 258, where the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and where the variant has hydrolytic activity on a polyester. In one embodiment, the disclosure provides variant lipolytic enzymes comprising one or more substitutions selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, Q161H, G175A, R190L, S212D, F226L, A236P, Y239I, L249P, S252L, E254Q, R256K, and L258F, where the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2 [0007]. It is noted that SEQ ID NO: 2 of Adams is 100% identical to SEQ ID NO: 2 of the instant case (see attachment below).
Adams teaches variant lipolytic enzymes comprising an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2, where the lipase variant comprises one, two, three, four, or more substitutions selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, where the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, where the variant has esterase activity [008].
Adams teaches the variant lipolytic enzyme of any of the preceding embodiments, wherein the variant comprises the substitutions, or combination of substitutions, selected from the group consisting of R40T-T177N-F180P-S205G, V025T- R40T-T177N-F180P-S205G, R40T-T064V-T177N-F 180P-S205G, R40T-T177N-F180P-Y182L-S205G, R40T-T177N-F180P-R190L-S205G, R40T-T177N-F180P-S205G-L249P, R40T-T064V-T177N-F180P-Y182L-S205G, R40T-T064V-T177N-F180P-R190L-S205G, R40T-T064V-T177N-F180P-S205G, R40T-T177N-F180P-Y182L-R190L-S205G, R40T-T177N-F180P-Y182L-S205G-L249P, R40T-T177N-F180P-R190L-S205G-L249P, R040T-T064V-T177N-F180P-Y182L-R190L-S205G-L249P, V025T-R40T-T064V-T177N-F180P-Y182L-R190L-S205G-L249P, R040T-T064V-T177N-F180P-Y182L-R190L-S205G-L249P, R040T-T064V-T177N-F180P-Y182A-R190L-S205G-L249P, V25T-R040T-T064V-T177N-Fl 80P-Y182L-R190L-S205G-L249P, R040T-T064V-T177N-F180P-Y182L-R190L-S205G-L249P, R040T-T064V-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-Y239I-L249P-S252I-L258F, R040A-T064V-T117L-T177N-I178L-F180P-Y182A-
R190L-S205G-F207T-S212D-F226L-Y239I-L249P-S252I-L258F, R040T-T064V-T117L-
T177R-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-Y239I-L249P-S252I-
L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2 [00145].
Adams teaches a variant lipolytic enzyme, or an active fragment thereof, compnsing: (a) an amino acid sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, (b) two or more substitutions at positions selected from i) a substitution at position 61 and at least one additional substitution from a position selected from: 14, 40, 59, 64, 66, 70, 161, 175, 180, 182, 190, 205, 212, 226, 236, 239, 249, 252, 254, 256, and 258, ii) a substitution at position 180 and at least one additional substitution at a position selected from 14, 40, 59, 61, 64, 66, 70, 161, 175, 182, 190, 205, 212, 226, 236, 239, 249, 252, 254, 256, and 258; iii) a substitution at position 182 and at least one additional substitution at a position selected from 14, 40, 59, 61, 64, 66, 70, 161, 175, 180, 190, 205, 212, 226, 236, 239, 249, 252, 254, 256, and 258; or iv) a substitution at position 205 and at least one additional substitution at a position selected from 40, 59, 61, 64, 66, 70, 161, 180, 182, 190, 212, 226, 236, 239, 249, 252, 254, 256, and 258; wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant lipolytic enzyme has esterase activity [00146].
Adams teaches a variant lipolytic enzyme, or an active fragment thereof, comprising: (a) an amino acid sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, (b) a combination of mutations selected from the group consisting of (i) a combination of mutations G061D-Y182A/L and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (ii) a combination of mutations G061D-S205G and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (iii) a combination of mutations F180P-Y182A/L and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (iv) a combination of mutations F180P-S205G and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, Y182A/L, R190L, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (v) a combination of mutations Y182A/L-S205G and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, R190L, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (vi) a combination of mutations V014S-R040A and at least one additional mutation selected from the group consisting of G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (vii) a combination of mutations V014S-R256K and at least one additional mutation selected from the group consisting of R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, and L258F, (viii) a combination of mutations R040A-E254Q and at least one additional mutation selected from the group consisting of V014S, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, R256K, and L258F, (ix) a combination of mutations R040A-S205G and at least one additional mutation selected from the group consisting of V014S, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (x) a combination of mutations G059Y-A236P and at least one additional mutation selected from the group consisting of V014S, R040A/T, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xi) a combination of mutations G059Y-E254Q and at least one additional mutation selected from the group consisting of V014S, R040A/T, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, R256K, and L258F, (xii) a combination of mutations R040A-F180P and at least one additional mutation selected from the group consisting of V014S, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xiii) a combination of mutations G061D-F226L and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xiv) a combination of mutations G061D-R256K and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, and L258F, (xv) a combination of mutations T064V-F226L and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xvi) a combination of mutations A066D-F226L and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xvii) a combination of mutations A066D-L249P and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, S252I, E254Q, R256K, and L258F, (xviii) a combination of mutations S070E-L258F and at least one additional mutation selected from the group consisting of V014S, R010A 1, G059Y, G061D, T064V, A066D, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, and R256K, (xix) a combination of mutations T117L-S205G and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K, and L258F, (xx) a combination of mutations T117L-L249P and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, S252I, E254Q, R256K, and L258F, (xxi) a combination of mutations Y182A/L-L249P and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, S252I, E254Q, R256K, and L258F, (xxii) a combination of mutations Q161H-Y239I and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, G175A, T177N/R, I178L, F180P, YI82A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P. L249P, S252I, E254Q, R256K, andL258F, and (xxiii) a combination of mutations G175A-A236P and at least one additional mutation selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, Y239I, L249P, S252I, E254Q, R256K, and L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant lipolytic enzyme has esterase activity [00146].
Adams teaches that the composition comprises from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% lipase by weight composition [00110].
Adams teaches that the composition comprises from about 0.00001% to about 10%, 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% cellulase by weight of composition [00113].
Adames teaches cleaning compositions or detergent compositions comprising a variant lipolytic enzyme as disclosed herein and at least one adjunct selected from the group consisting of surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, preservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tamish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and pH control agents [0014].
Adams teaches that the laundry detergent compositions comprise from about 0.1% to about 60%, about 1% to about 50%, or about 5% to about 40% surfactant by weight of the composition [0092].
Adams teaches that the composition may additionally include one or more detergent builders or builder systems, a complexing agent, a polymer, a bleaching system, a stabilizer, a foam booster, a suds suppressor, an anti-corrosion agent, a soil-suspending agent, an anti-soil redeposition agent, a dye, a bactericide, a hydrotope, an optical brightener, a fabric conditioner, perfume and include additional enzymes selected from proteases, amylases, cellulases, lipases, mannanases, nucleases, pectinases, xyloglucanases, or perhydrolases, as provided in more detail herein [0095].
Adams teaches that the variant lipolytic enzyme comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full length amino acid sequence of SEQ ID NO: 2 [00140].
Adams teaches that the cleaning or detergent compositions comprise adjunct materials including, but not limited to, surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, preservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tarnish and/or anticorrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and pH control agents [0089].
Adams teaches the detergent compositions may be utilized at a temperature of from about 10°C to about 60°C [00104].
Adams teaches that the cleaning compositions have a pH of from 7.4 to pH 11.5, or pH 7.4 to pH 11.0, or pH 7.5 to pH 11.5, or pH 7.5 to pH 11.0, or pH 7.5 to pH 10.5, or pH 7.5 to pH 10.0, or pH 7.5 to pH 9.5, or pH 7.5 to pH 9.0, or pH 7.5 to pH 8.5, or pH 7.5 to pH 8.0, or pH 7.6 to pH 11.5, or pH 7.6 to pH 11.0, or pH 7.6 to pH 10.5, or pH 8.7 to pH 10.0, or pH 8.0 to pH 11.5, or pH 8.0 to pH 11.0, or pH 8.0 to pH 10.5, or pH 8.0 to pH 10.0 [00102].
Adams teaches the variant has lipolytic activity on a polyester on polyethylene terephthalate (PET) [00171].
Adams teaches that the compositions can be liquid or solid [00101].
Adams teaches that the composition comprises one or more additional enzymes [00107].
Adams teaches that the compositions provided herein comprise a variant lipolytic enzyme in combination with one or more amylases. In one embodiment, the composition comprises from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% amylase by weight composition [00109].
Therefore, the teachings of Adams anticipate the instant claims as written/interpreted.
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The applied reference has a common inventor with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed in the reference and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement.
Claim Rejections - 35 USC § 103 (AIA )
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.
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claims 1-10 are rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (US 2024/0150738 A1 published 03/09/2024, filed 03/17/2021; hereby “Adams”), in view of Naganthran et al. (Molecules 22.9 (2017): 1577; hereby “Naganthran”).
The teachings of Adams are discussed above.
Adams teaches the composition comprises from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% lipase by weight composition [00110].
Adams teaches the composition comprises from about 0.00001% to about 10%, 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% cellulase by weight of composition [00113].
Adams does not explicitly the weight ratio of the at least one variant lipolytic enzyme and the at least one cellulase in the range of 1 :25 to 25:1.
Naganthran teaches that lipases are added to detergents to improve soil removel and incorporation of more than one enzyme, like cellulase increases washing efficacy (Page 2 [1]).
Naganthran teaches that cellulase can enhance fabric appearance as well as featuring softening, soil removal and color brightening (Page 2 [1]).
Naganthran teaches that the lowest possible enzyme level with good efficiency used in the detergent formulation is considered economical for future application (Page 5, 2.3. Efficiency of Individual Enzyme Concentration).
Naganthran teaches that the addition of lipase into protease-containing detergents improved the washing efficiency and removal of fatty stains, demonstrating that combinations of more than two enzymes may be a better option (Page 5, 2.3. Efficiency of Individual Enzyme Concentration).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to optimize the ratio of the lipolytic enzyme and cellulase within the cleaning composition of Adam to arrive at a ratio of 1:25 to 25:1. A person of ordinary skill in the art is motivated to have this ratio because Adams teaches overlapping concentration ranges for the lipase and cellulase components, each being present in amounts ranging from about 0.00001% to about 10% by weight. Furthermore, optimizing the ratio of enzymes through routine experimentation would be obvious because the lowest possible enzyme level with good efficiency used in detergent formulation is considered economical for future application as taught by Naganthran. Accordingly, one of ordinary skill would have found it obvious to select and optimize the amount of lipase and cellulase within the recited ranges of Adams to arrive at the claimed ratios through routine experimentation, as the ratio needed would depend on the overall formulation of the cleaning composition and the cleaning efficiency needed. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
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 1-6 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 7-8 of copending Application No. 18/571816 (‘816), in view of Naganthran et al. (Molecules 22.9 (2017): 1577; hereby “Naganthran”).
Claims 1-6, of the instant case, as interpreted are directed in part to a cleaning composition, comprising (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions: T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; (b) at least one cellulase; and (c) at least one surfactant, in an amount of 2 to 30 wt%; wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75% or 90 % identity to the full-length amino acid sequence of SEQ ID NO:2; wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of R40T- T64V-T 117L-G175E-T 177N-F180P-Y 182A-R190L-S205G-F207L-S212D-F226L-Y239I- L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D- F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N- I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-G175A-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2. U.S; wherein the variant lipolytic enzyme has lipolytic activity on a polyethylene terephthalate (PET); wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt%
Claim 1 of ‘816 as interpreted is directed in part to a cleaning composition comprising: (a) a variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions T064V-T117L-T177N/R-I178L-F180P-Y182A- R190L-S205G- S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; (b) at least one surfactant, in an amount of 2 to 30 wt.%; (c) optionally at least one further enzyme, in an amount of 0.001 to 1 wt.%; (d) optionally at least one performance polymer, in an amount of 0.05 to 5 wt.%; and (e) optionally at least one organic solvent, in an amount of 0.1 to 10 wt.
Claim 2 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1 of ‘816; wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 80% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 3 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1 of ‘816; wherein the variant lipolytic enzyme is derived from a parent enzyme comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2
Claim 4 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1 of ‘816; wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G-F207L- S212D-F226L-Y239I-L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N- I178L-F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P- S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V- S70E-T 117L-T 177N-I178L-F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L- F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q- L258F, R40T-T64V-S70E-T117L-G175A-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T 177N-I178L-F180P-Y 182A-R 190L-S205G-F207T-V210I-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P- Y182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q- L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T- S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2.
Claim 7 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1 of ‘816; wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET).
Claim 8 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1 of ‘816; wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt%.
It is noted that SEQ ID NO: 2 of both cases are identical (see alignment below).
Claims 1-4, 7-8 of ‘816 do not teach a cleaning composition having at least one cellulase.
However, Naganthran teaches that incorporation of cellulase increases washing efficacy by enhancing fabric appearance as well as perform the softening, soil removal and color brightening of fabric (Page 2 [1]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate a cellulase into ‘816. A person of ordinary skill in the art is motivated to incorporate a cellulase into the cleaning composition of ‘816 because it improves washing efficacy, as taught by Naganthran. Thus, adding cellulase to a cleaning composition would make said cleaning composition more effective. Therefore, although the claims at issue are not identical, they are not patentably distinct from each other, in view of Naganthran. This is a provisional nonstatutory double patenting rejection.
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Claims 1-6 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of copending Application No. 18/571,882 (‘882) in view of Naganthran et al. (Molecules 22.9 (2017): 1577; hereby “Naganthran”).
The interpretation of claims 1-6 of this instant case is discussed above.
Claim 1 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition, comprising, (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and (b) at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof.
Claim 2 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition of Claim 1 of ‘882, wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 3 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition of Claim 1 of ‘882, wherein the variant lipolytic enzyme is derived from a parent enzyme comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 4 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition of Claim 1 of ‘882, wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of: R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G- F207L-S212D-F226L-Y239I-L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L- T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I- L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A- T64V-S70E-T117L-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N- I178L-F 180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-G175A-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T 177N-I178L-F 180P-Y 182A-R 190L-S205G-F207T-V210I-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L- S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L- S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L- F180P-Y 182A-R 190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-R256K-L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2.
Claim 5 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition of Claim 1 of ‘882; wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET).
Claim 6 of ‘882 as interpreted is directed in part to a cleaning or fabric conditioning composition of Claim 1 of ‘882, wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt%.
It is noted that SEQ ID NO: 2 of both cases are identical (see alignment below).
Claims 1-6 of ‘882 do not teach a cleaning composition, comprising at least one cellulase and a surfactant in an amount of 2 to 30 wt %.
However, Naganthran teaches that incorporation of cellulase increases washing efficacy by enhancing fabric appearance as well as perform the softening, soil removal and color brightening of fabric (Page 2 [1]). Naganthran teaches the efficiency of formulated detergent; wherein the detergent contained 7% surfactant (Figure 1).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the teachings of Naganthran into ‘816. A person of ordinary skill in the art is motivated to incorporate a cellulase into the cleaning composition of ‘816 because it improves washing efficacy, as taught by Naganthran. A person of ordinary skill in the art is motivated to incorporate 7% surfactant into the cleaning composition of ‘816 because it is involved in formulating efficient detergent, as taught by Naganthran. Thus, adding cellulase and 7% surfactant to a cleaning composition would make said cleaning composition more effective. Therefore, although the claims at issue are not identical, they are not patentably distinct from each other, in view of Naganthran.
This is a provisional nonstatutory double patenting rejection.
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Claims 1-5 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5, 7, and 13 of copending Application No. 18/569,808 (‘808), in view of Naganthran et al. (Molecules 22.9 (2017): 1577; hereby “Naganthran”).
Claims 1-5, of the instant case, as interpreted are directed in part to a cleaning composition, comprising (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions: T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; (b) at least one cellulase; and (c) at least one surfactant, in an amount of 2 to 30 wt%; wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75% or 90 % identity to the full-length amino acid sequence of SEQ ID NO:2; wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of R40T- T64V-T 117L-G175E-T 177N-F180P-Y 182A-R190L-S205G-F207L-S212D-F226L-Y239I- L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D- F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N- I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-G175A-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2; wherein the variant lipolytic enzyme has lipolytic activity on a polyethylene terephthalate (PET);
Claim 1 of ‘808 as interpreted is directed in part to a variant lipolytic enzyme comprising an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2, comprising the substitutions T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207TL/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant has esterase activity.
Claim 2 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808, wherein the variant comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%,97%, 98%, or 99% identity to the full length amino acid sequence of SEQ ID NO: 2.
Claim 3 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808 the variant lipolytic enzyme of claim 1 or 2, wherein the variant is derived from a parent enzyme comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%,97%, 98%, or 99% identity to the full length amino acid sequence of SEQ ID NO: 2.
Claim 4 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808, wherein the variant comprises a combination of substitutions selected from the group consisting of R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G-F207L-S212D-F226L-Y239I-L249P-S252I-L258F, R40T-G61D-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-Q161H-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-G175A-T177N-1178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-1178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61D-T64V-A66D-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61D-T64V-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61D-T64V-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A-G59Y-G61D-T64V-A66D-S70E-T117L-Q161H-G175A-T177R-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2.
Claim 5 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808, wherein the variant has one or more improved properties when compared to a parent or reference lipolytic enzyme, wherein the improved property is selected from improved stability, improved hydrolytic activity on a polyester, or combinations thereof.
Claim 7 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808, wherein the variant has hydrolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, poly(ethylene adipate) (PEA), and combinations thereof.
Claim 13 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim 1 of ‘808, wherein the composition further comprises at least at least one additional enzyme selected from the group consisting of: acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, feruloyl esterase, galactanases, glucoamylases, hemicellulases, hexosaminidases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, metalloproteases, nucleases (e.g. deoxyribonucleases and ribonucleases), oxidases, oxidoreductases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, perhydrolases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, polyesterases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, xylosidases, and any combination or mixture thereof.
It is noted that SEQ ID NO: 2 of both cases are identical (see alignment below).
The claims of ‘808 do not teach that the variant lipolytic enzymes are used for cleaning and include surfactants.
The teachings of Naganthran are discussed above. Additionally, Naganthran teaches that lipases are used in dishwashing detergent and said lipases are the most stable in surfactants (abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the variant lipolytic enzymes in cleaning products and add surfactants to said product. A person of ordinary skill in the art is motivated to use the enzymes of ‘808 in cleaning products and add surfactants to said product because the claims ‘808 disclose a composition with lipolytic enzymes and surfactants together which is shown to improve washing efficiency, as taught by Naganthran. Therefore, although the claims at issue are not identical, they are not patentably distinct from each other, in view of Naganthran.
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Conclusion
No claim is in condition for allowance.
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/S.L.S./Examiner, Art Unit 1652
/ROBERT B MONDESI/Supervisory Patent Examiner, Art Unit 1652
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