DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 02/16/2026 has been entered.
Priority
Applicant’s claim to priority from PCT/EP2015/058497 filed 04/20/2015 is hereby acknowledged. This application is a Divisional of US Application No.15/568,098 filed 10/20/2017.
Application Status
Amendments to claims filed 10/08/2025 are hereby acknowledged. Claim 1 is amended, claims 2-4 and 10 are cancelled. Claims 1, 5-9 and 11-13 are pending and under examination in this office action.
Any objection or rejection not reiterated herein has been overcome by Applicant’s amendments and is withdrawn. Applicant’s amendments and arguments have been thoroughly reviewed, but are not persuasive to place the claims in condition for allowance for the reasons that follow.
The following rejections are new:
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1, 6-9 and 12-13 under 35 U.S.C. § 103 as being unpatentable over Lorenz (Lorenz, M.G. US 7,893,251 B2, published February 22, 2011), Peytavi (Peytavi et al. US 8,481,265 B2 published July 9, 2013; cited previously), Bougnoux (Bougnoux, M-E. et al. Journal of clinical Microbiology, Vol. 37 (1999), pp: 925-930; cited previously), Sikorskaite (Sikorskaite, S. et al. “Protocol: Optimised methodology for isolation of nucleic from leaves of species in the Solanaceae and Rosaceae families”. Plant Methods, Vol. 9 (2013), p: 31; cited previously) and Cayley (Cayley, S. et al. “Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity”. Journal of Molecular Biology, Vol. 222 (1991), pp: 281-300; cited previously).
Regarding claim 1, it recites “A lysis solution for selectively lysing animal cells in the presence of microbial and/or plant cells containing less than 2M of chaotropic substances, the lysis solution comprising at least one saponin; a water-soluble salt selected from the group consisting of acetates, glutamates, and any mixture thereof; and a viscosity modifying agent selected from the group consisting of sucrose, glucose, and a mixture thereof, wherein the at least one saponin is present in a total saponin amount ranging from about 2 to about 15% (w/v) based on the whole lysis solution, wherein the viscosity modifying agent is present in a concentration ranging from 300 to 1,000 mM, wherein the aforementioned concentration range of the viscosity modifying agent refers to the total amount of the viscosity modifying agent based on the whole lysis solution, wherein the water-soluble salt is present in a concentration ranging from 50 to 850mM, wherein the aforementioned concentration range of the water-soluble salt refers to the total amount of the water-soluble salt based on the whole lysis solution, wherein the lysis solution is useful for selectively lysing animal cells in the presence of microbial and/or plant cells while leaving the microbial and/or plant cells essentially intact.”
The instant Specification teaches that “essentially” is defined as “shall be understood in a way that in any case more than 50% of the considered trait is obtained, preferably at least 60%, more preferably at least 70%, even more preferably at least 75%, 80 %, 85 %, 90 %, or 95 % and most preferably at least 98 %. “Essentially” can also represent 100%.” (see page 5, lines 23-26).
Regarding claim 1, Lorenz teaches a method for selective isolation of nucleic acids from microbial cells present in samples containing higher eukaryotic cells and/or tissues” (see title). Lorenz teaches that the first step of the method comprises “ a) carrying out lysis of the higher eukaryotic cells and/or tissues, wherein the microbial cells substantially remain intact” (see column 7, lines 30-32).
Lorenz further teaches that “The latter remain substantially intact, i.e. the outer boundary of these cells (cell wall or similar structures) is not disrupted by the mode of lysis employed in step a) of the method” (see column 9, lines 65-67). Lorenz also teaches that “According to a particularly preferred embodiment, the proportion of the lysed microbial cells in the first step is less than 40%, 30%, 20%, 10%, 5%, wherein less than 3% or less than 1% is particularly preferred” (see column 10, lines 38-45).
Lorenz teaches in claim 1 the selective lysis of higher eukaryotic cells and/or tissues, wherein the microbial cells remain intact; wherein said lysis is carried out by adding one or more chaotropic agents; and the addition of a nuclease capable of degrading DNA in the presence of one or more chaotropic agents (see a) and b) of claim 1, column 27, lines 5-11).
Lorenz teaches that the lysing agents can be in buffers such as TRIS, MOPS or HEPES, with chelating agents such as EDTA or EGTA. Lorenz teaches that the solution can comprise other substances. The lysing agents can be one or more chaotropic agents and/or one or more surfactants, such as chaotropic salts, e.g., guanidine hydrochloride, sodium iodide, guanidine isothiocyanate (i.e., water-soluble salts) or mixtures thereof. Lorenz also teaches that 1M guanidine salts and 1 wt.% surfactants are preferred with the use of the endonuclease I from Escherichia coli (see column 11, lines 33-44; see column 15, Examples A, lines 6-21, Figure 7).
Lorenz teaches that the surfactants are sodium dodecyl sulfate , Brij40®, Triton®-X100 and/or Tween®-20 (see columns 6 and 7, lines 1-12; column 28, claim 21).
Lorenz teaches sucrose in a separate Buffer 5 used after “pelleting” debris from the blood cells lysis and wash steps (see column 15, Example B, lines 25-67; column 16, lines 1-16).
While Lorenz does not teach acetates, glutamates, nor saponin, Peytavi teaches a lysis solution that lyse blood cells, i.e. animal cells, and allow the recovery of microorganisms, therefore a lysis solution that is useful for selectively lysing animal cells in the presence of microbial cells (see title and abstract; and see column 8, lines 46-52).
Peytavi teaches the preparation and the use of a saponin formulation for the isolation of microorganisms and/or microorganisms nucleic acids from a bodily fluid that may comprise or may be suspected to comprise microorganisms and /or host cells and/or host cells debris (see column 6, lines 48-54). Peytavi teaches the use of saponin in a lysis buffer in a final concentration ranging from about 20 to about 100 mg/ml (i.e. about 2% to 10%) (see column 5, lines 56-61). Peytavi teaches a lysis step that requires a saponin solution added at the equivalent of 3 blood volumes with a final concentration of 75 mg/mL, which is 7.5% w/v (see column 12, lines 45-50) or a final concentration of 100 mg/mL, which is 10% w/v (see column 12, lines 53-56).
Peytavi also teaches that the saponin formulation may be prepared using buffer containing phosphate buffer saline (PBS 1X: 137 mM NaCl (i.e. water-soluble salt), 10 mM Phosphate, 2.7 mM KCl (i.e. water-soluble salt)) or a TE buffer (10mM Tris, 1mM EDTA (see column 7, lines 44-53). However, the mixing of saponin under powder form might takes several hours (see column 12, lines 11-23). Peytavi also teaches that a buffer to solubilize saponin containing ethyl acetate and/or glacial acetic acid need to be used, since saponin is not water-soluble (see column 4, lines 11-14). Therefore, in adding saponin to a lysis buffer, one may also add acetic acid to the buffer.
Peytavi is silent on chaotropic agents in the lysis buffer. Therefore, Examiner interprets that Peytavi did not use any chaotropic agent.
Peytavi teaches that the “invention may comprise the steps of lysing bodily fluids (host) cells while protecting (preserving) microbial cells and their nucleic acids using a solution which may comprise saponin (…)” (column 5, lines 53-66). Peytavi teaches that the protocol is efficient for obtaining viable and/or metabolically active microbial cells ( see column 6, lines 6-7). Peytavi teaches that the invention results in 80-500-fold concentration of the microorganisms that are viable and/or metabolically active (see column 9, lines 49-54). Peytavi also teaches a recovery of viable Escherichia coli at an average of 106% +/-27% and 117% +/-19% from the number initially inoculated, and after the final step 85% +/- 18% (see column 22, lines 19-24).
Peytavi also teaches that “A person skilled in the art knows fluid displacement means as well as other ways to achieve separation and harvesting of soluble and insoluble fractions” and that alternative means, ways and devices designed to move fluids and /or separate recuperable soluble and insoluble fractions are within the scope of the invention (see column 13, lines 47-53).
Peytavi does not teach a viscosity modifying agent, e.g. sucrose or glucose, nor a water-soluble salt that is either an acetate or a glutamate.
However, Peytavi refers to Bougnoux (see column 5, lines 12-22). Bougnoux teaches a lysis solution to lyse blood cells, i.e. animal cells, in presence of Candida cells, i.e. microbial cells.
Bougnoux teaches a method of lysing blood cells requiring the use of a solution called “blood cell lysis buffer” (see page 926, page 926, column 1, paragraph 5). Bougnoux is also silent about chaotropic substance. However, Bougnoux teaches a lysis solution comprising 0.32 M sucrose ( 320 mM sucrose), 10 mM Tris-HCl, 5 mM MgCl2 (a water soluble salt) and 1% Triton™ X-100.
Bougnoux further uses a buffer named “TEG” buffer after a first step of centrifugation to resuspend the pellet, containing 50 mM glucose, 25 mM Tris-HCl and 10 mM EDTA (i.e. acetate) and 1% SDS (see page 926, lines 28-40).
Sikorskaite teaches a lysis buffer to isolate plant cells’ nuclei by protecting the membranes from high concentrations of detergents or prolonged exposure to detergents, by adding a viscosity modifying agent such as sucrose (see page 2 of 9, left column, second paragraph, line 11). Since claim 1 of instant disclosure is drawn to a lysis buffer for lysing animal cells in the presence of microbial and/or plant cells, and since both microbial cells and plant cells present with cell walls and organelles sensitive to detergents, Sikorskaite’s teachings are relevant.
Cayley teaches about osmolarity of the cytoplasm of a microorganism in function of external osmolarity (see title and abstract). Therefore, the teachings of Cayley provides insights for adjusting the osmolarity of buffers and adding osmolytes to a solution that is supposed to maintain the integrity of microorganisms’ cell membranes, proteins and nucleic acids. Cayley teaches that NaCl, i.e. a water-soluble salt, is a plasmolyzing agent (see abstract, line 9), that can be used to adjust extracellular osmolarity (see page 283, left column, second para, lines 4-5). However, Cayley also teaches a role as osmo-protectant for glutamate (see page 288, left column, last sentence). Cayley teaches that a normal adaptive response for microorganisms under plasmolysis conditions is potassium and glucose uptake from solution and biosynthesis of trehalose (from glucose) and glutamate (see page 289, left column, third para). Cayley teaches that potassium and glutamate are the only significant cytoplasmic osmolytes in the cytoplasm of cells, contributing to osmoregulation (see abstract, line 18). Cayley also teaches a negative impact of macromolecular crowding due to increase osmolarity of external solution on proteins’ stability, activities and their interactions with nucleic acids (see summary page 297). Cayley incidentally teaches the need for glucose [or sucrose (source of glucose)] for this microorganism’s osmoregulation (see page 289, left column, third para).
It would have been obvious to one with ordinary skills in the art, before the effective filing date of the claimed invention to have modified the ingredients of Lorenz’s lysis buffer and Peytavi’s lysis buffer, removing the chaotropic agent taught by Lorenz and substituting it with a solution with saponin as taught by Peytavi, and adding a viscosity modifying agent such as sucrose (at 320 mM) as taught by Lorenz/Bougnoux. All the three references Lorenz, Peytavi and Bougnoux teach about lysing red blood cells in the presence of microorganisms. Lorenz’s and Peytavi’s teachings suggest that other substances may be added, and other ways to preserve and protect the microbial cells and their nucleic acids may be used. Sikorskaite confirms that sucrose protects microorganism/ plant cells’ membranes and nuclei. Lorenz teaches that other substances can be comprised within the lysis buffer. Therefore, adding a viscosity modifying agent to the lysis solution taught by Lorenz/Peytavi to favor the protection of microbial cells’ nuclei is within the scope of Lorenz/Peytavi’s invention.
It would also be obvious to one with ordinary skills in the art, before the effective filing date of the claimed invention to try and limit the amount of plasmolyzing agent taught by Cayley, in the lysis buffer taught by Lorenz/Peytavi modified by Bougnoux, to further protect microorganism cells and their content. The teachings of Cayley suggest compensating the need for buffering water-soluble salts by substituting NaCl for potassium salts and glutamate, or potassium glutamate, to better equip the microorganisms with means for osmoregulation.
One with ordinary skills in the art motivated in adding means/levels of protection to microbial cells and their nuclei/nucleic acids, would have added sucrose to the lysis buffer as well as a glutamate salt or potassium glutamate, as taught by Sikorskaite and as suggested by Cayley. One with ordinary skills in the art could have performed these modifications and arrived at the claimed invention with a reasonable expectation of success.
Regarding claim 6, Peytavi is silent on chaotropic agents. Bougnoux teaches a chaotrope-free lysis solution that comprises a non-ionic surfactant, Triton™- X100, in an amount of 1%.
Regarding claim 7, Lorenz teaches Brij®40, as a component of Lysis buffer, which is a hydrophilic polyoxyethylene ether (see column 6, line 10).
Regarding claim 8, Peytavi teaches multiple kits comprising a lysis solution (see column 5, lines 9-26). Peytavi also teaches a kit comprising a lysis solution containing saponin for isolating microorganisms from a body fluid that may comprise host cells and/or host cells debris (see column 6, line 34-42).
A kit is a mere collection of products/compositions presented together; therefore, the combination of Peytavi and Bougnoux renders the kit of claim 8 obvious.
Regarding claim 9, Bougnoux teaches washing buffers (see page 926, left column, “DNA extractions” section).
Regarding claims 12 and 13, Peytavi teaches about other types of kits and methods comprising a filtration step for separating blood cells using a 0.22 µm pore size filter to retain microbial cells on the filter membrane (see column 3, lines 21-26).
In KSR Int 'l v. Teleflex, the Supreme Court, indicated that “The principles underlying [earlier] cases are instructive when the question is whether a patent claiming the combination of elements of prior art is obvious. When a work is available in one field of endeavor, design incentives and other market forces can prompt variations of it, either in the same field or a different one. If a person of ordinary skill can implement a predictable variation, § 103 likely bars its patentability”. KSR Int'l v. Teleflex lnc., 127 S. Ct. 1727, 1740 (2007).
Therefore, the combination of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cayley renders the claimed elements obvious.
Claims 5 is rejected under 35 U.S.C. § 103 as being unpatentable over Lorenz (Lorenz, M.G. US 7,893,251 B2, published February 22, 2011), Peytavi (Peytavi et al. US 8, 481,265 B2 published July 9, 2013; cited previously), Bougnoux (Bougnoux, M-E. et al. Journal of clinical Microbiology, Vol. 37 (1999), pp: 925-930; cited previously), Sikorskaite (Sikorskaite, S. et al. “Protocol: Optimised methodology for isolation of nucleic from leaves of species in the Solanaceae and Rosaceae families” Plant Methods, Vol. 9 (2013), p: 31; cited previously) and Cayley (Cayley, S. et al. “Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity”. Journal of Molecular Biology, Vol. 222 (1991), pp: 281-300; cited previously), as applied to claim 1 above, and in further view of Talebpour (Talebpour. S. et al. US 2014/0154687 A1, published June 5, 2014; cited previously).
The rejection of claim 1 is described above. The combination of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cayley renders the elements of claim 1 obvious.
Regarding claim 5, Lorenz teaches anionic surfactants that are alkylbenzene sulfonates and alkane sulfonates (see column 6, lines 1-3). Lorenz teaches the use of surfactants up to 2 wt.% of the total mixture (see column 6, lines 27-29) or up to 20 wt.% without microbial cells being lysed (<40%) (see column 11, lines 40-42).
However, Lorenz does not give an example of polyanionic sulfonate nor a molar concentration.
Regarding claim 5, the combination of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cayley does not teach a specific polyanionic sulfonate.
However, Talebpour teaches a method to selectively lyse animal cells in the presence of microbial cells (abstract). Talebpour further resolves the deficiency of the combination of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cayley as far as inclusion of a polyanionic sulfonate, in methods for the treatment of a cell sample (Abstract).
Talebpour provides for a cell lysis solution comprising saponin and a polyanionic sulfonate (e.g., sodium polymetholsulfonate), wherein Talebpour states:
“As stated above, the presence of blood cell lysis reagent 22 in mixture 30 causes the selective lysis of blood cells. In one example implementation, blood cell lysis reagent 22 may be an aqueous liquid including at least the following components: saponin, sodium polyanetholesulfonate (a sodium salt of polyanetholesulfonic acid, known as SPS), and an antifoaming agent, such as poly(propylene glycol) (PPG, e.g. with a molecular weight of approximately 2000). In some embodiments, the saponin is purified saponin. Example methods for purifying saponin are disclosed in U.S. Pat. No. 3,883,425, titled "Detoxification of Saponins", which is incorporated herein in its entirety. It has been found that without saponin purification blood cell lysis is less efficient and a gel-like substance is formed upon centrifugation.” (see ¶ [0075]).
Talebpour teaches various concentrations for SPS, notably a concentration within the range of 1.5 to 60 mg/mL Since SPS molecular weight is 251.26 g/mol, Talebpour teaches a range from 5.9 mM to 238 mM.
It would have been obvious to one with ordinary skills in the art, before the effective filing date to have modified Lorenz/Peytavi/Bougnoux/Sikorskaite/Cayley, by adding to the lysis buffer the polyanetholesulfonic acid taught by Talebpour. Talebpour teaches that a lysis buffer can contain more than one surfactant ([0075]). Therefore, one with ordinary skills in the art could have performed this modification with a reasonable expectation of success and arrived at the claimed invention, because Lorenz/Peytavi, Bougnoux, Sikorskaite, Cayley and Talebpour, all teach solutions for cell preparation before nucleic acid analysis.
Claim 11 is rejected under 35 U.S.C. §103 as being unpatentable over Lorenz (Lorenz, M.G. US 7,893,251 B2, published February 22, 2011), Peytavi (Peytavi et al. US 8, 481,265 B2 published July 9, 2013; cited previously), Bougnoux (Bougnoux, M-E. et al. Journal of clinical Microbiology, Vol. 37 (1999), pp: 925-930; cited previously), Sikorskaite (Sikorskaite, S. et al. “Protocol: Optimised methodology for isolation of nucleic from leaves of species in the Solanaceae and Rosaceae families” Plant Methods, Vol. 9 (2013), p: 31; cited previously) and Cayley (Cayley, S. et al. “Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity”. Journal of Molecular Biology, Vol. 222 (1991), pp: 281-300; cited previously), as applied to claims 1 and 8 above, and in further view of Benzonase® (Benzonase® Nuclease. 1999. Novagen™, p1-4. see ‘Information Disclosure Statement’, filed on 14 April 2020; herein “BENZONASE” and cited previously).
The rejections of claims 1 and 8 are discussed above. As described above, the elements of claim 1 and claim 8 are rendered obvious by the combination of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cayley.
Regarding claim 11, Lorenz teaches the use of endonuclease I (EndA) from Escherichia coli in the lysis buffer (see column 4, lines 1-4). Lorenz teaches that this nuclease does not have RNAse activity under the conditions comprising chaotropic agents (see column 3, and Figure 3; column 15, lines 6-21).
Lorenz’s teachings suggest that the endonuclease BENZONASE can be used, but has less efficacy in presence of chaotropic agents (see column 3, lines 48-60; column 15, lines 16-21; and column 4, lines 55-58).
Regarding claim 11, Bougnoux teaches the addition of DNase I to the lysis buffer ( see page 926, left column, “DNA extractions” section, line 9). Peytavi teaches DNAse I as it refers to Bougnoux (see column 5, lines 9-22).
However, regarding claim 11, the combination of references does not render obvious the specific element, “an endonuclease capable of degrading both RNA as well as DNA, or comprising a mixture of at least one DNAse and at least one RNAse” in the lysis buffer.
While the combination of Lorenz, Peytavi, Bougnoux , Sikorskaite and Cayley does disclose a lysis solution comprising the inclusion of an endonuclease that digests DNA, BENZONASE describes Benzonase® nuclease which is an endonuclease that attacks and degrades all forms of DNA and RNA (single stranded, double stranded, linear, circular) and is effective in a wide range of operating conditions (p1, 1st ¶). BENZONASE indicates an application for the described nuclease is for the removal of nucleic acid contaminants and can be applied in combination with a lysis method (p2, Applications Section; ¶ bridging p2-3).
In view of the teachings of Lorenz/Peytavi/Bougnoux , Sikorskaite, Cayley and BENZONASE, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have optionally included Benzonase® nuclease as described by BENZONASE in the disclosed lysis solution of Lorenz/Peytavi modified by Bougnoux, Sikorskaite and Cayley. BENZONASE provides one in the art some teaching, suggestion, or motivation to utilize Benzonase® nuclease to attack and degrade all forms of nucleic acids (i.e., DNA and RNA) in order to remove nucleic acid contaminants and that it can be applied in combination with a lysis method. Additionally, Lorenz, Peytavi, Bougnoux, Sikorskaite and BENZONASE are directed to lysis solutions, while Lorenz directly suggest the use of BENZONASE in absence of chaotropic agents, and, thus, are drawn to the same purpose and/or outcome. One with ordinary skills in the art motivated in collecting a nucleic acid-free lysate fraction to analyze proteins only would make this modification, adding Benzonase® nuclease to the solution, with a reasonable expectation of success and arrived at the claimed invention.
Response to Applicant’s Arguments
Applicant's arguments filed 10/08/2025 have been fully considered but they are not persuasive.
Applicant states “Claim 1 is amended to clarify that the lysis solution is useful for
selectively lysing animal cells in the presence of microbial and/or plant cells while leaving the microbial and/or plant cells essentially intact.
In view of the foregoing remarks and amendments to the claims, Applicant believes that all claims as currently pending are in condition for allowance.”
In response, Lorenz specifically teaches a method using a lysis buffer comprising among other substances, an endonuclease, chaotropic agents, anionic sulfonates, and water-soluble salts, allowing for selective lysis of red blood cells, while leaving a proportion of lysed microbial cells that is less than 40%, 30%, 20%, 10%, 5%, or less than 3% or less than 1% is particularly preferred” (see column 10, lines 38-45).
One with ordinary skills in the art could have modified and substituted the chaotropic agents taught by Lorenz, with a saponin solution as taught by Peytavi with a reasonable expectation of success since Peytavi also describes same or better outcome using a saponin solution: Peytavi teaches a recovery of viable Escherichia coli at an average of 106% +/-27% and 117% +/-19% from the number initially inoculated, and after the final step 85% +/- 18% (see column 22, lines 19-24).
Substituting a chaotropic agent for a saponin makes even more sense since Lorenz describes that a BENZONASE, i.e., a nuclease capable of digesting both RNA and DNA, is not efficient, even for DNA digesting, in a solution with chaotropic agents.
Claims 1, 6-9 and 12-13 are therefore rejected under 35 U.S.C. § 103 as unpatentable over the combination of references Lorenz, Peytavi, Bougnoux, Sikorskaite and Cailey. And elements claimed in claims 5 and 11 are further rendered obvious by the combinations of Lorenz, Peytavi, Bougnoux, Sikorskaite and Cailey, in further view of Talebpour, or in further view of BENZONASE.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/A.D./Examiner, Art Unit 1636
/NANCY J LEITH/Primary Examiner, Art Unit 1636