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
The preliminary amendment filed 10/10/2024 is entered. Claims 1-5, 7, 9-10, 14, 18, 21, 25-26, 28-29, and 31-42 are canceled. Claims 6, 8, 11-13, 15-17, 19-20, 22-24, 27, and 30 are pending and under consideration in this action.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. The instant claims are entitled to an effective filing date of 09/03/2021.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Browser-executable codes can be found on page 34 in lines 22, 23 and 24 of the amended specification filed 02/28/2024.
The use of the terms “Teknova”(p. 36 line 14), “Tide” (p. 36 line 18; p. 39 lines 13, 14), and “Eppendorf” (p. 38 line 1) which are trade names or marks used in commerce, have been noted in this application. The terms should be accompanied by the generic terminology; furthermore the terms should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Claim Objections
Claims 8 and 22 are objected to because of the following informalities:
Claim 8 recites “of at least…or greater compared” in lines 3 and 5, which is redundant. As such, the claim can be amended to succinctly recite “of at least 5% compared”, or “of 5% or greater compared”.
Claim 22 recites “at least one additional polypeptide, wherein the at least one additional polypeptide is an enzyme” in lines 2-3, which is repetitive and can be shortened to “at least one additional enzyme”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
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 6, 8, 11-13, 15-17, 19-20, 22-24, 27, and 30 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 claims contain 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor, at the time the application was filed, had possession of the claimed invention.
The claims are drawn to a genus of polypeptides that are at least an 80% sequence identity to SEQ ID NO: 11 and have nuclease activity. SEQ ID NO: 11 is a nuclease from Aspergillus clavatus NRRL 1 that is 174 residues in length. See p. 35 line 4 of the amended specification. As such, the claims encompass polypeptides that vary by approximately 35 residues because 174 residues x 20% = 34.8 residues. Claim 6 entails a correlation between the genus of polypeptides and preventing, reducing or removing a biofilm from a textile or hard surface. Claims 8, 11, 12, 15-17, and 19-20 depend from claim 6 but do not recite further structural limitations of the polypeptide. Claim 13 depends from claim 6 and requires the polypeptide to have at least 85% sequence identity to SEQ ID NO: 11, such that claim 13 encompasses polypeptides that vary by 26 residues compared to SEQ ID NO: 11. Claim 22 is drawn to a detergent composition comprising the genus of polypeptides. Claims 23-24 depend from claim 22 but do not further limit the structure of the polypeptide. Claim 27 and dependent claim 30 entail a correlation between the genus of polypeptides and reducing malodor associated with a textile or hard surface. The specification does not disclose a representative number of species of the claimed genus by reduction to practice, and does not provide adequate guidance with regard to the structural features of the polypeptide that are required to provide the recited properties. Therefore, one of skill cannot immediately envision which polypeptides will have the required functional characteristics, and one could not conclude that Applicant was in possession of the claimed genus of polypeptides at the time the filing, as discussed more fully below.
For claims drawn to a genus, MPEP § 2163(3)(a)(ii) indicates 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 the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. 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.
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The instant specification reduces to practice one species, a polypeptide that is 100% identical to instant SEQ ID NO: 11 and capable of dispersing Pseudomonas fluorescens biofilm. In example 2, P. fluorescens (ATCC strain 700830) biofilm is formed on 96-well round bottom plates. See p. 36 lines 12-13. The biofilm buildup in plates is treated with enzyme solution at 20 ppm or at 100 ppm, prepared in a 1:1200 dilution of Tide™ Original liquid detergent (the solution alone is used as a negative control). SEQ ID NO: 14, also referred to as BciNuc1, is included for comparison. See p. 36 lines 17-19. After treatment, biofilm is stained by crystal violet solution. The biofilm bound crystal violet is dissolved in 30% acetic acid and the biofilm signal is monitored in terms of absorbance at 590 nm using a spectrophotometer. See p. 37 lines 1-5. As shown in figures 1 and 2, AclNuc1 (i.e. SEQ ID NO: 11) removed more biofilm than the benchmark SEQ ID NO: 14 at 100 ppm enzyme and 20 ppm enzyme dose. See p. 36 lines 6-7 and figures 1-2 below. Thus, the specification indicates that SEQ ID NO: 11 is capable of dispersing Pseudomonas fluorescens biofilm better than Tide™ Original liquid detergent and the benchmark BciNuc1 (SEQ ID NO: 14).
MPEP 2163(3)(a)(ii) states that “the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation. Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date”. Considering the lack of guidance provided in the specification, one would appraise support from the state of the art to extrapolate the correlation between polypeptide structure nuclease function for biofilm prevention, reduction or removal, and malodor reduction.
With respect to the state of the art on biofilms and malodor, Gjermansen (US 2018/0187175) discloses that a biofilm may include one or more microorganisms, including gram-positive and gram-negative bacteria, algae, protozoa, and/or yeast or filamentous fungi and viruses and/or bacteriophage. See [0004]. The presence of bacteria implies that the laundry items become sticky and therefore soil adheres to the sticky areas. This soil has shown difficult to remove by commercially available detergent compositions. Further, these bacteria are a source of bad odor. Malodor is difficult to remove and the reason for this bad odor is adhesion of bacteria to the textile surface. See [0005]. Gjermansen suggests that the dense and protected environment of a biofilm allows bacteria within the biofilm to cooperate and interact in various ways. This environment can show increased resistance to detergents and antibiotics, as the outerlayer of cells protect the interior of the community. On laundry biofilm producing bacteria can be found among the following species: Acinetobacter, Aeromicrobium, Brevundimonas, Microbacterium, Micrococcus luteus, Pseudomonas, Staphylococcus epidermidism and Stenotrophomonas. See [0041]. Wang (Biofilms Microbiomes 9, 63 (2023)), a past filing date reference, discloses that in practice most enzymatic biofilm eradication assays are carried out by in vitro testing against monomicrobial biofilms instead of multispecies-based biofilms that occur in nature. Thus, advancing research of biofilm-dispersing enzymes is bottlenecked by the lack of reliable biofilm models that mimic the true complexity of microbial colonization in humans and the world we live in. See p. 10 para. 1. Wang discloses that DNase I is an endonuclease that digests DNA and can disrupt the formation of both mono- and polymicrobial biofilm. However, DNase I is more effective towards the destruction of rapidly growing biofilms. Whereas mature biofilms exhibit resistance to DNase I degradation. This is likely due to the mature biofilms being strengthened by other substances such as exopolysaccharides and exoproteins, additionally, mature biofilms produce proteolytic exoenzymes that can locally inactivate DNase I. See p. 63 left column last passage. Thus, Gjermansen and Wang illustrate the unpredictability of using any one nuclease to prevent, reduce or remove any mono- or polymicrobial biofilm, or its associated malodor.
In view of the prior art, the instant disclosure does not satisfy the written description requirement because the species disclosed do not adequately represent the substantial variation within the claimed genus. As discussed above, the breadth of potential structures embraced by the claims is substantial. The instant specification reduces to practice one example of a polypeptide that is 100% identical to SEQ ID NO: 11 and capable of dispersing Pseudomonas fluorescens biofilm. Considering the unpredictability in the art, as evidenced by Gjermansen and Wang, one of skill in the art at the time of filing could not have reasonably predicted which polypeptides commensurate in scope with the instant claims would be capable of preventing, reducing or removing any biofilm, and capable reducing malodor associated with a textile or hard surface. Consequently, one of skill could not conclude that Applicant was in possession of the claimed genus of polypeptides at the time the application was filed.
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 6, 8, 11-13, 15-17, 19-20, 23-24, 27 and 30 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 6 recites “preventing, reducing or removing a biofilm” in line 1, which renders the claim indefinite because the way in which an existing biofilm can be prevented is unclear. Since claim 6 recites reducing or removing a biofilm from a textile or hard surface, claim 6 indicates that a biofilm is present on the textile or hard surface prior to the required contact step. The term “preventing” renders the scope of claim 6 indefinite because in one interpretation the claim encompasses preventing additional biofilm formation on the textile or hard surface that has a biofilm present; and, under an alternative interpretation the claim encompasses preventing any biofilm from forming on a textile or hard surface such that no biofilm is present prior to the recited contact step. To obviate this claim 6 can be amended to recite “A method for reducing or removing a biofilm”, so that the textile or hard surface clearly requires a biofilm to be present prior to the contact step. Claim 6 further recites “a polypeptide having nuclease activity or a composition comprising a polypeptide having nuclease activity; and (ii) optionally rinsing the textile or surface, wherein said polypeptide” in lines 2-5, which renders the claim indefinite for two reasons. The first reason is that it is unclear whether the wherein clause starting in line 4 is optional or required, because the wherein clause is recited after the term “optionally”. The second reason is that it is unclear whether the “surface” recited in line 4 is limited to the hard surface, because the term surface is broader in scope compared the hard surface.
Claims 8, 11-13, 15-17, and 19-20 depend from claim 6 and are rejected for the same reasons.
Claim 11 recites “0.002 to 10,000 mg of protein, 0.005 to 5000 mg of protein, 0.01 to 5000 mg of protein, 0.05 to 5000 mg of protein, 0.05 to 1300 mg of protein, 0.1 to 1300 mg of protein, 0.1 to 500 mg of protein, 0.1 to 100 mg of protein, per liter of wash liquor, or in the amount of at least 0.002 ppm active nuclease” in lines 4-7, which is indefinite for three reasons. The first reason is that it is unclear whether the term “protein” is the polypeptide or a separate protein. The second reason is that it is unclear whether the “per liter of wash liquor” limitation in line 6 applies to all of the recited ranges or only the last range 0.1 to 100 mg or protein. The third reason is that it is unclear whether the “active nuclease” recited in line 7 is the polypeptide with nuclease activity or a separate active nuclease.
Claim 15 recites time ranges using the phrase “between [lower limit] to [upper limit]”, which renders the required amount of time indefinite. Specifically, claim 15 recites “an amount of time of 5 minutes to 10 days, 5 minutes to 400 minutes, between 5 minutes to 300 minutes, between 5 minutes to 250 minutes, between 5 minutes to 200 minutes, between 5 minutes to 150 minutes, between 5 minutes to 100 minutes, between 5 minutes to 50 minutes, or between 5 minutes to 30 minutes” in lines 2-8. In one interpretation claim 15 requires an amount of time between a lower limit and an upper limit because the claim recites “an amount of time…between”. However, the claim also recites “between [lower limit] to [upper limit]”, rather than between [lower limit] and [upper limit]. Therefore, under an alternative interpretation the claim requires a time range from [the lower limit] to [the upper limit]. To obviate this rejection, claim 15 can be amended to recite “The method of claim 6, wherein the contacting step takes place for an amount of time between 5 minutes and 10 days”.
Claim 16 recites “a temperature of 10˚ to 60˚ C, between 15˚ to 55˚ C, between 20˚ to 50˚C or between 20˚ to 45˚ C” in lines 2-4, which renders the claim indefinite because it is unclear whether the claim requires one temperature or a temperature range. Since claim 16 recite “a temperature…between”, claim 16 can reasonably be interpreted as requiring one temperature selected from within the recited ranges. However, claim 16 specifically recites “between [lower limit] to [upper limit]” rather than between [lower limit] and [upper limit]. Therefore, claim 16 can also reasonably be interpreted as requiring the contact step to take place at one of the recited temperature ranges “of 10˚ to 60˚ C…15˚ to 55˚ C… 20˚ to 50˚C or…20˚ to 45˚ C”. To obviate this rejection, claim 16 can be amended to recite “The method of claim 6, wherein the contacting step takes place at a temperature range of 10˚ to 60˚ C”; or “The method of claim 6, wherein the contacting step takes place at a temperature between 10˚ and 60˚ C”.
Claim 24 recites “about 0.1% to about 60%, about 1% to about 50%, or about 5% to about 40%” in lines 2-3, which renders the claim indefinite because the upper and lower limits of each range are unclear. The term “about” is a term of approximation. The specification does not provide any examples of percentages encompassed within the
Claim 30 recites “a said composition” in line 5, which renders the claim indefinite because it is unclear whether ‘a said composition’ encompasses any of the previously recited compositions or a specific composition.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 8, 23-24, and 30 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 8 fails to further limit claim 6 from which it depends. Independent claim 6 recites “reducing or removing a biofilm” in the preamble on line 1. Claim 8 recites “the biofilm is reduced or removed from said textile or hard surface in an amount of at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or greater compared to the amount of biofilm present on the textile or hard surface prior to contacting the textile or hard surface with said polypeptide or the composition comprising said polypeptide”. Under the broadest reasonable interpretation, claim 8 is merely a statement of purpose or intended use. As such, claim 8 does not further limit the method of claim 6.
Claims 23 and 24 broaden the scope of the composition required in claim 22. Independent claim 22 requires a detergent composition. Claims 23 and 24 depend from claim 22 and recite “The composition of claim 22” in line 1, and claim 24 further recites “the composition” in lines 1 and 3. Since a “composition” is broader in scope compared to a “detergent composition”, claims 23-24 fail to include all the limitations of the claim upon which they depend.
Claim 23 fails to further limit the surfactant required in claim 22 from which claim 23 depends. Claim 22 requires a surfactant (line 16). Claim 23 requires the surfactant to be selected from the group consisting of a non-ionic, ampholytic, semi-polar, anionic, cationic, zwitterionic, and combinations and mixtures thereof. Claim 23 does not further limit the surfactant of claim 22 because claim 23 encompasses every electrical charge classification. As such, claim 23 encompasses every surfactant.
Claim 30 fails to include all the limitations of claim 27 from which it depends. Claim 27 requires contacting a textile or hard surface with the detergent composition of claim 22. Claim 30 requires the malodor to be reduced by at least 5% compared to the amount of the malodor present prior to contacting the textile or hard surface with said polypeptide having nuclease activity or a said composition. Since claim 30 encompasses embodiments in which the textile or hard surface is contacted with “said polypeptide having nuclease activity or a said composition”, claim 30 does not require the same detergent composition contact step recited in claim 27. To obviate this rejection, claim 30 can be amended to recite “prior to contacting the textile or hard surface with the detergent composition”.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 22-24 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 22 recites a “detergent composition ” in line 1. Therefore, claims 22-24 are directed to a composition of matter, which is one of the statutory categories (Step 1:Yes).
Claim 22 further recites “(i) a polypeptide having nuclease activity… wherein the polypeptide having the nuclease activity is a polypeptide having at least 80% sequence identity to the amino acid sequence of SEQ ID NO: 11” in lines 1-2 and 17-18. The instant specification teaches identifying SEQ ID NO: 11 (AclNuc1) from Aspergillus clavatus NRRL 1. See p. 34 lines 21-25 and table 1. Nierman (NCBI accession number XM_001276395.1, deposited 26 Oct. 2006) teaches a protein sequence from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. Claim 22 further requires “(ii) a polypeptide having protease activity; (iii) at least one additional polypeptide, wherein the at least one additional polypeptide is an enzyme” (lines 2-3) selected from a group that includes: cellulases (line 7), proteases (line 13), and xylanases (line 15). Evidentiary reference Tremacoldi (World Journal of Microbiology and Biotechnology 20, 639–642, 2004) discloses that A. clavatus is a protease producer that can be isolated from soil. Furthermore, Tremacoldi discloses that Aspergillus is known for their cellulolytic, xylanolytic and proteolytic activities. See p. 639 left column last passage. Claim 22 further requires “(iv) a surfactant” (line 16). As evidenced by Mbachu (IAR J Agri Res Life Sci, 2021, 2(4), 30-35) Aspergillus clavatus produces biosurfactant. See, e.g. figure 4 caption. Therefore, the evidence of record indicates that the combination of (i) SEQ ID NO: 11, (ii) a protease, (iii) at least one additional enzyme and (iv) a surfactant is a natural product from Aspergillus clavatus. Compared to the closest naturally occurring counterpart, there is no structural difference between the natural product and the instantly claimed composition. Because there is no indication in the record that the instantly disclosed composition has a markedly different characteristic in structure, function, or other properties as compared to its natural counterpart claims 22-24 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. Claim 22 does not recite any additional elements besides the natural product that could integrate the judicial exception into a practical application. Claim 23 requires the surfactant to be selected from a group that consists of a non-ionic, ampholytic, semi-polar, anionic, cationic, zwitterionic and combinations and mixtures thereof. This claim element is recited with a high level of generality because it encompasses every electrical charge classification of surfactants. As such, claim 23 does not limit the judicial exception in a way that could integrate it into a practical application. Claim 24 requires the composition to comprise between about 0.1% to about 60% surfactant by weight of the composition. This limitation is merely an attempt to generally link the judicial exception to its field of use as a detergent. Therefore, the claim as a whole, does not integrate the judicial exception into a practical application (Step 2A Prong 2: No).
The additional elements fail to amount to an inventive concept. Gori (US 2017/0107457) teaches a detergent composition comprising a polypeptide having DNase activity (i.e. nuclease activity) and a detergent adjunct ingredient. See claim 34 of Gori. The detergent adjunct ingredient is selected from a group that includes enzymes, and surfactants. See claim 35 of Gori. Gori teaches detergent formulations that may contain one or more additional enzymes such as proteases (i.e. polypeptide having protease activity), lipases, cutinases, cellulases, xyloglucanases, pectinases, peroxidases, catalases and mannanases. See [0024]. Gori teaches one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic. See [0331]. Gori teaches that the surfactant is typically present at a level of from about 0.1% to 60% by weight. See [0331]. Thus, the additional limitations in claims 22-24 fail to amount to an inventive concept (Step 2B: No).
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 6, 8, 11-13, 15-17, 19-20, 22-24, 27, and 30 are rejected under 35 U.S.C. 103 as being unpatentable over Gori (US 2017/0107457) in view of Nierman (NCBI accession number XM_001276395.1, submitted 26-Oct-2006).
Regarding claim 6, Gori teaches a method for preventing, reducing or removing a biofilm from a textile, comprising treating the item with a polypeptide having deoxyribonuclease (DNase) (i.e. nuclease) activity, wherein the polypeptide is obtained from a fungal source. See claim 21 of Gori. In example 16, Gori teaches the effect of the presence of DNase in detergent on Pseudomonas aeruginosa biofilm on textile. Gori teaches adding a culture dilution to swatches of polyester (i.e. textile), and rinsing the swatches. See [0707]. The rinsed swatches with P. aeruginosa are placed in a tube to which a liquid detergent prepared with Aspergillus oryzae DNAse is added. See [0708]. The results show that the DNAse is able to reduce stickiness and/or reduce the amount of the P. aeruginosa biofilm on the textile. See [0710].
Gori does not teach a polypeptide that has at least 80% sequence identity to SEQ ID NO: 11.
Nierman teaches an endonuclease protein, accession number XM_001276395.1, from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. See p. 2 of Nierman and the office action appendix for the alignment.
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 Nierman’s polypeptide having nuclease activity for Gori’s deoxyribonuclease (DNase) (i.e. nuclease). One of ordinary skill in the art would have been motivated to do so because Gori suggests that the polypeptide having DNase activity can be obtained from Aspergillus (see [0072]). There would have been a reasonable expectation of success because Gori demonstrates reducing a biofilm from a polyester textile by contacting the textile with a nuclease from Aspergillus; and Nierman teaches a nuclease from Aspergillus. Therefore, the nuclease of Nierman reasonably serves the same function compared to the nuclease of Gori.
Regarding claim 8, Gori, in example 16, discloses that the Aspergillus oryzae DNAse reduces the stickiness and/or reduces the amount of the P. aeruginosa biofilm on the textile. See [0710]. Gori suggests that the A. oryzae DNase has a deep cleaning effect. See [0658]. The term “deep cleaning” is the disruption or removal of a biofilm or components of a biofilm. See [0022].
Gori and Nierman do not teach a biofilm that is reduced or removed from a textile or hard surface in an amount of at least 5% or greater compared to the amount of biofilm present on the textile or hard surface prior to contacting the textile or hard surface with said polypeptide or the composition comprising said polypeptide. However, Gori suggests that the A. oryzae DNase can remove biofilm, which is indicative of a 100% reduction of a biofilm.
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 Nierman’s polypeptide having nuclease activity for Gori’s DNase (i.e. nuclease), and to further adjust the concentration of Nierman’s polypeptide with nuclease activity based on Gori’s suggestion, and in the process remove a biofilm. One of ordinary skill in the art would have been motivated to adjust the concentration of Neirman’s polypeptide with nuclease activity, because Gori suggests that polypeptides with nuclease activity can have a deep cleaning effect that removes biofilm. There would have been a reasonable expectation of success because Gori demonstrates reducing the amount of a biofilm using a nuclease from Aspergillus.
Regarding claim 11, Gori teaches placing rinsed swatches with P. aeruginosa [biofilm] in a tube to which a liquid detergent prepared with Aspergillus oryzae DNAse at 0.1 ppm in wash liquor is added (i.e. at least 0.002 ppm active nuclease). See [0708].
Regarding claim 12, Gori teaches a wash liquor comprising a polypeptide having DNase activity or a detergent composition comprising the polypeptide. See [0121]. Gori teaches a pH of a liquid solution in a range of 1 to 11, such as in the range of 7 to 9. See [0125].
Regarding claim 13, Nierman teaches an endonuclease protein, accession number XM_001276395.1, from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. See p. 2 of Nierman and the office action appendix for the alignment.
Regarding claim 15, Gori teaches placing swatches with P. aeruginosa [biofilm] in a tube to which a liquid detergent prepared with Aspergillus oryzae DNAse is added. Washing is performed for 1 hour (i.e. contacting for an amount of time 5 minutes to 10 days). See [0708].
Regarding claim 16, Gori teaches placing swatches with P. aeruginosa [biofilm] in a tube to which a liquid detergent prepared with Aspergillus oryzae DNAse is added. Washing is performed for 1 hour at 30˚C (i.e. contacting at a temperature of 10˚ to 60˚C). See [0708].
Regarding claim 17, Gori teaches a detergent composition comprising a polypeptide having DNase activity and a detergent adjunct ingredient. See claim 34 of Gori. The detergent adjunct ingredient is selected from a group that includes surfactants. See claim 35 of Gori.
Regarding claim 19, Gori teaches a detergent composition comprising a polypeptide having DNase activity and a detergent adjunct ingredient. See claim 34 of Gori.
Regarding claim 20, Gori teaches detergent formulations that may contain one or more additional enzymes such as proteases, lipases, cutinases, cellulases, xyloglucanases, pectinases, peroxidases, catalases and mannanases. See [0024]. In example 6, Gori teaches adding protease to detergent containing A. oryzae DNase. See [0063]. The cleaning effects are investigated on Brevundimonas sp. swatches (i.e. biofilm containing textile). See [0664].
Regarding claim 22, Gori teaches a detergent composition comprising a polypeptide having DNase activity (i.e. nuclease activity) and a detergent adjunct ingredient. See claim 34 of Gori. The detergent adjunct ingredient is selected from a group that includes enzymes, and surfactants. See claim 35 of Gori. Gori teaches detergent formulations that may contain one or more additional enzymes such as proteases (i.e. polypeptide having protease activity), lipases, cutinases, cellulases, xyloglucanases, pectinases, peroxidases, catalases and mannanases. See [0024].
Gori does not teach a polypeptide that has at least 80% sequence identity to SEQ ID NO: 11.
Nierman teaches an endonuclease protein, accession number XM_001276395.1, from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. See p. 2 of Nierman and the office action appendix for the alignment.
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 Nierman’s polypeptide having nuclease activity for Gori’s polypeptide having DNase (i.e. nuclease) activity. One of ordinary skill in the art would have been motivated to do so because Gori suggests that the polypeptide having DNase activity can be obtained from Aspergillus (see [0072]). There would have been a reasonable expectation of success because Gori teaches detergent compositions comprising a polypeptide having DNase activity, protease, additional enzymes such as cellulases and surfactants; and Nierman teaches a polypeptide with nuclease activity. Therefore, the nuclease of Nierman reasonably serves the same function compared to the nuclease of Gori.
Regarding claim 23, Gori teaches a detergent composition that may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic. See [0331].
Regarding claim 24, Gori teaches that the surfactant is typically present at a level of from about 0.1% to 60% by weight. See [0331].
Regarding claim 27, Gori teaches a method wherein malodor is removed from the textile. See claim 23 of Gori. Gori teaches a method comprising treating an item with a polypeptide having DNase activity. See claim 21 of Gori. Gori teaches a detergent composition comprising a polypeptide having DNase activity (i.e. nuclease activity) and a detergent adjunct ingredient. See claim 34 of Gori. The detergent adjunct ingredient is selected from a group that includes enzymes, and surfactants. See claim 35 of Gori. Gori teaches detergent formulations that may contain one or more additional enzymes such as proteases (i.e. polypeptide having protease activity), lipases, cutinases, cellulases, xyloglucanases, pectinases, peroxidases, catalases and mannanases. See [0024]. Furthermore, Gori discloses that E-2-nonenal is an unpleasant smelling compound. See [0070]. In example 13, Gori teaches preparing swatches (i.e. textile) with E-2-nonenal. See [0696]. Wash liquor is added to tubes containing swatches with E-2-nonenal. A. oryzae DNAse is added to one of the tubes (i.e. contact). See [0700].
Gori does not teach a polypeptide that has at least 80% sequence identity to SEQ ID NO: 11.
Nierman teaches an endonuclease protein, accession number XM_001276395.1, from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. See p. 2 of Nierman and the office action appendix for the alignment.
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 Nierman’s polypeptide having nuclease activity for Gori’s polypeptide having DNase (i.e. nuclease) activity. One of ordinary skill in the art would have been motivated to do so because Gori suggests that the polypeptide having DNase activity can be obtained from Aspergillus (see [0072]). There would have been a reasonable expectation of success because Gori demonstrates reducing malodor associated with textile swatches by contacting the swatches with a detergent and a DNase from Aspergillus; and Nierman teaches a nuclease from Aspergillus. Therefore, the nuclease of Nierman reasonably serves the same function compared to the nuclease of Gori.
Regarding claim 30, Gori, in example 13, teaches preparing swatches (i.e. textile) with E-2-nonenal. See [0696]. Wash liquor is added to tubes containing swatches with E-2-nonenal. A. oryzae DNAse is added to one of the tubes (i.e. contact). See [0700]. As shown in table 12, the wash liquor with DNAse reduced the intensity of E-2-nonenal by 23%, 27% and 37% when measured with an E-nose compared to wash liquor without the DNAse.
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.
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Claims 6, 8, 11-13, 15-17, 19-20, 22-24, 27, and 30 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4-6, and 8-21 of copending Application No. 17/616,033 in view of Nierman (NCBI accession number XM_001276395.1, submitted 26-Oct-2006).
Copending claim 1 recites a method for preventing, reducing or removing a biofilm on a textile comprising contacting the biofilm with a cleaning composition comprising a polypeptide having thermolysin activity, wherein the polypeptide having thermolysin activity is a polypeptide having at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 1.
Copending claim 4 recites the method of claim 1, wherein the cleaning composition comprises a polypeptide having thermolysin activity in an amount selected from the group consisting of 0.001 to 10,000 mg/L, 0.001 to 2000 mg/L, 0.01 to 5000 mg/L, 0.01 to 2000 mg/L, 0.01 to 1300 mg/L, 0.1 to 5000 mg/L, 0.1 to 2000 mg/L, 0.1 to 1300 mg/L, 1 to 5000 mg/L, 1 to 1300 mg/L, 1 to 500 mg/L, 10 to 5000 mg/L, 10 to 1300 mg/L, and 10 to 500 mg/L.
Copending claim 5 recites the method claim 1, wherein the cleaning composition is a laundry composition.
Copending claim 6 recites the method of claim 1, further comprising rinsing the textile.
Copending claim 8 recites the method of claim 1 or claim 6, wherein the biofilm is reduced or removed from the textile.
Copending claim 9 recites the method of claim 1 or claim 6, wherein the biofilm is reduced or removed from the textile in an amount selected from the groups consisting of at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% and 100%, compared to the amount of the biofilm present on the textile prior to contacting the textile with the polypeptide having thermolysin activity or a composition comprising a polypeptide having thermolysin activity.
Copending claim 10 recites the method of claim 1 or claim 6, wherein the biofilm is measured by a method comprising: staining the biofilm with crystal violet; dissolving the crystal violet bound to the biofilm in an acetic acid solution; and measuring an optical density of the solution at 590 nm.
Copending claim 11 recites the method of claim 1 or claim 6, wherein the contacting step comprises the use of a polypeptide having thermolysin activity in an amount selected from the group consisting of 0.002 to 10,000 mg of protein, 0.005 to 5000 mg of protein, 0.01 to 5000 mg of protein, 0.05 to 5000 mg of protein, 0.05 to 1300 mg of protein, 0.1 to 1300 mg of protein, 0.1 to 500 mg of protein, and 0.1 to 100 mg of protein, per liter of wash liquor, or in the amount of at least 0.002 ppm active thermolysin.
Copending claim 12 recites the method of claim 1 or claim 6, wherein the cleaning composition has 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.
Copending claim 13 recites the method of claim 1 or claim 6, wherein the polypeptide having thermolysin activity is a polypeptide having at least 80%, 85%, 90%, 95%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 1.
Copending claim 14 recites the method of claim 1 or claim 6, wherein the contacting step occurs in a wash liquor.
Copending claim 15 recites the method of claim 1 or claim 6, wherein the contacting step takes place for an amount of time selected from the group consisting of about 5 minutes to about 10 days, about 5 minutes to about 400 minutes, between about 5 minutes to about 300 minutes, between about 5 minutes to about 250 minutes, between about 5 minutes to about 200 minutes, between about 5 minutes to about 150 minutes, between about 5 minutes to about 100 minutes, between about 5 minutes to about 50 minutes, and between about 5 minutes to about 30 minutes.
Copending claim 16 recites the method of claim 1 or claim 6, wherein the contacting step takes place at a temperature selected from the group consisting of between 10° to 60° C, between 15° to 55°C, between 20° to 50° C and between 20° to 45° C.
Copending claim 17 recites the method of claim 1 or claim 6, wherein the composition comprising a polypeptide having thermolysin activity further comprises a surfactant.
Copending claim 18 recites the method of claim 17, wherein the surfactant is selected from the group consisting of a non-ionic, ampholytic, semi-polar, anionic, cationic, zwitterionic, and combinations and mixtures thereof.
Copending claim 19 recites the method of claim 1 or claim 6, wherein the composition is a detergent composition.
Copending claim 20 recites the method of claim 1 or claim 6, wherein the contacting step further includes contacting the textile with one or more additional enzymes 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, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, metalloproteases, nucleases (e.g. deoxyribonucleases and ribonucleases), oxidases, oxidoreductases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, polyesterases, additional proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, xylosidases, and any combination or mixture thereof.
Copending claim 21 recites the method of claim 1 or claim 6, wherein the contacting step takes place in a washing machine or a dishwasher.
The copending claims lack a polypeptide having nuclease activity, wherein said polypeptide has at least 80% sequence identity to the amino acid sequence of SEQ ID NO: 11.
However, Nierman teaches an endonuclease protein, accession number XM_001276395.1, from Aspergillus clavatus NRRL 1 that is 100% identical to instant SEQ ID NO: 11. See p. 2 of Nierman and the office action appendix for the alignment.
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 Nierman’s polypeptide having nuclease activity for the polypeptide having thermolysin activity recited in the copending claims in order to prevent, reduce or remove a biofilm, and reduce malodor.
This is a provisional nonstatutory double patenting rejection.
Conclusion
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/K.C.B./ Examiner, Art Unit 1657
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