DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
Response to Amendments
Applicant's amendments filed 10/7/2025 to claim 1 has been entered. Claims 1, 3-4, 6-9, 11-12, 14 and 16-19 remain pending, of which claims 1, 3-4, 6-8 and 18 are being considered on their merits. Claims 9, 11-12, 14, 16-17 and 19 remain withdrawn from consideration. Any rejections of record not particularly addressed below are withdrawn in light of the claim amendments and applicant’s comments.
Claim Objections
Claim 18 is objected to because of the following informalities: claim 18 improperly uses the status indicator “New”, when the claim has been previously presented. Appropriate correction is required.
Claim Rejections - 35 USC § 103
The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made.
Claims 1, 3-4, 6-7 and 18 remain rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bhargava et al (U.S. PGPUB 2007/0184150; 3/6/2020 IDS) as evidenced by Svendsen et al (U.S. Patent 6,187,576) and GenBank (alpha amylase [Geobacillus stearothermophilus]: AAB86961.1), and in view of Smith et al (U.S. PGPUB 2008/0138871; 3/6/2020 IDS), Niehaus et al (1999, Appl Microbiol Biotechnol, 51: 711-729; 3/6/2020 IDS) and Takakura et al (1998, WO9856926A1).
Regarding claim 1, Bhargava teaches a process of industrial fermentation to produce ethanol comprising liquefaction of ground corn using alpha-amylase in a liquefaction step at a pH of 5.4, with temperatures of 85, 70, and 50 degrees Celsius, with 85 degrees Celsius being the “standard condition” (see Example 1 in paragraph [0073], paragraph [0015] and Figure 1).
Regarding claims 1, 3 and 18, Bhargava teaches in the example that the alpha-amylase is “Bacillus stearothermophilus alpha-amylase variant with double deletion corresponding to I181 & G182, and N193F substitution as disclosed in U.S. Pat. No. 6,187,576 and available on request from Novozymes” (see paragraphs [0046] and [0063]); the instant specification reveals that applicant’s alpha-amylase is a Bacillus stearothermophilus alpha-amylase which may by the alpha-amylase disclosed in U.S. Pat. No. 6,187,576). U.S. Pat. No. 6,187,576 is cited solely as evidence that the Bacillus stearothermophilus alpha-amylase variant with double deletion corresponding to I181 & G182, and N193F substitution, has more than 80 percent sequence identity to instant SEQ ID NO: 1 (see col. 12, lines 22-25, and SEQ ID NO: 3). Genbank is cited solely as evidence that prior to the double deletion corresponding to I181 & G182, and N193F substitution, the sequence of Bacillus stearothermophilus alpha-amylase has 100 percent sequence identity to instant SEQ ID NO: 1, meaning after the mutations it has 100 percent sequence identity to instant SEQ ID NO: 22.
Regarding claim 1, Bhargava teaches it is common to use a liquefying temperature above the initial gelatinization temperature (see paragraph [0016]). Regarding claims 1 and 7, Bhargava teaches following liquefaction, glucoamylase is added for a saccharification step (see Example 1 in paragraph [0074]), and Bhargava also teaches that the glucoamylase can be added sooner for pre-saccharification (see paragraph [0037]); reads on adding during liquefaction. Bhargava teaches following the glucoamylase treatment, the samples are inoculated with yeast for fermentation of the sample (see Example 1 in paragraph [0074]).
Bhargava does not teach the properties of the glucoamylase (claims 1 and 7), or the properties of the alpha-amylase (claim 3). Bhargava does not teach including a protease in the method (claims 1, 4 and 6), that the protease is a variant of the metallo protease derived from a strain of Pyrococcus (claim 6). Bhargava does not teach the properties of the protease (claims 4).
Smith is drawn to industrial methods of producing fermentation products from starch-containing material (see paragraphs [0001]-[0003]). Regarding claims 1, 4 and 6, Smith teaches that protease treatment may advantageously be carried out simultaneously with liquefaction (see Smith paragraph [0028]), and that protease dosing during fermentation increases the overall final product yield (see Smith paragraph [0027]). Regarding claims 1, 4 and 6, Smith teaches simultaneous liquefaction of starch and protein degradation during a fermentation method by addition of a protease in the liquefaction step (see Example 2 in paragraph [0150]). Regarding claims 4 and 6, Smith teaches an embodiment the protease is a Thermoascus metalloprotease (see paragraph [0066]).
Regarding claims 1, 4 and 6, Niehaus teaches running industrial biotechnological processes at elevated temperature has many advantages as it influences the bioavailability and solubility of compounds (see col. 2 on page 711). Regarding claims 1, 4 and 6, Niehaus teaches the elevation of temperature is accompanied by a decrease in viscosity and an increase in the diffusion coefficient of organic compounds (see col. 2 on page 711). claims 1, 4 and 6, Niehaus teaches several species of extremophiles, including Pyrococcus, have been identified and that the enzymes isolated from these microorganisms show unique features, are extremely thermostable and usually resistant against chemical denaturants such as detergents, chemotropic agents, organic solvents and extremes of pH (see col. 2 on page 711). Regarding claims 1, 4 and 6, Niehaus teaches one of the enzymes identified as being valuable for industrial use because of its ability to catalyze reactions under extreme conditions (high and extremes of pH) temperatures is a protease from Pyrococcus furiosus and that this protease has an optimal working temperature of 85°C (see page 718).
Regarding claims 1, 4 and 6, Takakura teaches a hyperthermostable protease derived from Pyrococcus furiosus that is useful for industrial use, and has an amino acid sequence identical to SEQ ID NO: 13 (see abstract and pages 35-37).
Regarding the limitations of the relative activity of the enzyme in various conditions, these are inherent properties of the enzymes and therefore since Takakura teaches the same enzyme, Takakura’s enzymes sufficiently has these properties.
A person of ordinary skill in the art would have had a reasonable expectation of success in adding Takakura’s protease in Bhargava’s liquefaction step in Bhargava’s method of fermentation because Smith teaches that protease treatment may advantageously be carried out simultaneously with liquefaction. The skilled artisan would have been motivated to add Takakura’s protease to the liquefaction step because Smith teaches that protease dosing during fermentation increases the overall final product yield and both Niehaus and Takakura teach specific proteases with high thermo-stability that is useful for industrial applications. Additionally, Niehaus highlights the advantages of using higher temperatures for enzymatic reactions, and using Takakura’s protease would allow the reaction be optimized at a higher temperature.
A person of ordinary skill in the art would have had a reasonable expectation of success carrying out Bhargava’s liquefaction step at 85°C because Bhargava teaches that the step can be carried out at this temperature, and that this is a standard temperature used in the industry. The skilled artisan would have been motivated to carrying out Bhargava’s liquefaction step at 85°C because Niehaus teaches 85°C is the optimal temperature for protease from Pyrococcus furiosus, Takakura’s protease is from Pyrococcus furiosus.
Regarding the limitations of the relative activity of the protease, glucoamylase, and alpha-amylase in various conditions, the Patent and Trademark Office is not equipped to conduct experimentation in order to determine whether or not applicants' enzymes differ, and if so to what extent, from the glucoamylase and alpha-amylase discussed in Bhargava, and the proteases taught by Takakura. The prior art glucoamylase functions as a carbohydrate-source generating enzyme, and alpha-amylase functions to liquefy starch just as the instant glucoamylase and alpha-amylase respectively. Furthermore, a review of the specification reveals that the alpha-amylase used in the instant method is derived from the same source as Bhargava’s alpha-amylase. Takakura also teaches a protease with the exact same amino acid sequence, so it appears to be identical to the claimed protease. The cited art taken as a whole demonstrates a reasonable probability that the proteases, glucoamylase, and alpha-amylase of the prior art is either identical or sufficiently similar to the claimed glucoamylase and alpha-amylase that whatever differences exist are not patentably significant. Therefore, the burden of establishing novelty or unobviousness by objective evidence is shifted to applicants.
Merely because a characteristic of a known enzyme is not disclosed in a reference does not make the known enzyme patentable. The new enzymes possess inherent characteristics which might not be displayed in the tests used in Bhargava and Takakura. Clear evidence that the proteases, glucoamylase, and alpha-amylase of the cited prior art does not possess a critical characteristic that is possessed by the claimed proteases, glucoamylase, and alpha-amylase would advance prosecution and might permit allowance of claims to applicants' enzymes.
Claim 6 is a product-by-process claims. M.P.E.P. § 2113 reads, “Product-by-process claims are not limited to the manipulations of the recited steps, only the structure implied by the steps.” Once a product appearing to be substantially identical is found and an art rejection made, the burden shifts to the applicant to show an unobvious difference. In this case, the proteases taught by Takakura appears to be sufficiently similar, or identical to the protease of the instant application as both are appear to have the same functions as they are used for the same purpose. Furthermore, the product-by-process limitation of “derived from” is very broad, as it does not provide any guidance as to how similar the enzyme in the claim must be to those found it the species that it is taken from. For these reasons, the claimed proteases are rendered obvious in view of the proteases taught by Takakura.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill at the time the invention was made.
Claim 8 remains rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bhargava et al (U.S. PGPUB 2007/0184150) as evidenced by Svendsen et al (U.S. Patent 6,187,576) and GenBank (alpha amylase [Geobacillus stearothermophilus]: AAB86961.1), and in view of Smith et al (U.S. PGPUB 2008/0138871), Niehaus et al (1999, Appl Microbiol Biotechnol, 51: 711-729) and Takakura et al (1998, WO9856926A1) as applied to claims 1, 3-4, 6-7 and 18 above, and further in view of Lantero et al (U.S. PGPUB 2005/0100996; 3/6/2020 IDS).
The teachings of Bhargava, Smith, Niehaus and Takakura are described and relied upon above.
Bhargava does not reach including a pullulanase during liquefaction and/or saccharification (claim 39).
Regarding claim 8, Lantero teaches that during the saccharification of the liquefied starch, pullulanases are useful in fermentation since they remove successive glucose units from the non-reducing ends of the starch (see paragraph [0102]).
A person of ordinary skill in the art would have had a reasonable expectation of success in adding pullulanases taught by Lantero to the saccharification step in Bhargava’s method of fermentation because Lantero teaches using pullulanases during saccharification. The skilled artisan would have been motivated to add the pullulanases taught by Lantero to the saccharification step in Bhargava’s method of fermentation because Lantero teaches that pullulanases are useful during fermentation since they can help break down the sugars.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill at the time the invention was made.
Response to Arguments
Applicant's arguments filed 10/7/2025 have been fully considered but they are not persuasive.
Highlights that Bhargava’s teaches a 16% increase in ethanol yield is achieved when liquefaction is performed at 70° C as compared to liquefaction at 85° C. Applicant concludes that because of this teaching, that Bhargava teaches away from liquefaction at 85° C, and that there is no motivation to use a temperature of 85° C. Applicant continues by also alleging that because Bhargava's alpha-amylase displayed the improved performance at 70°C, that it is incompatible with Niehaus/Takakura's protease which has an optimal working temperature of 85°C.
However, as discussed above Bhargava also teaches that 85° C is considered the standard temperature. There is no requirement that a reference may only be considered for a specific preferred embodiment. Furthermore, as stated above, Bhargava teaches using several temperatures, and in paragraph [0016] of Bhargava, Bhargava specifically teaches that there are different benefits/results with temperatures of either 70° C or 85° C, therefore rendering either temperature as obvious to use. Furthermore, the cited Niehaus reference teaches running industrial biotechnological processes at elevated temperature has many advantages as it influences the bioavailability and solubility of compounds. Niehaus teaches the elevation of temperature is accompanied by a decrease in viscosity and an increase in the diffusion coefficient of organic compounds. Applicant should also note that the rejection over the combination of references is over the obviousness to add Takakura’s Pyrococcus furious protease in Bhargava’s liquefaction step, and Niehaus teaches proteases from Pyrococcus furiosus with optimal working temperature of 85°C. Therefore, Bhargava is not incompatible with Niehaus/Takakura's protease which has an optimal working temperature of 85°C as Bhargava exemplifies this temperature, and the references specifically highlight other advantages to using this temperature. For any one of these three reasons it is obvious to carry out the liquefying step at a temperature of 85° C and this argument is not persuasive.
Applicant alleges that the claimed method has unexpected results, alleging (1) the amylase used with the claimed protease produces more ethanol than the amylase combined with Alcalase (ACL) which is one of the proteases discussed in the Smith, (2) the protease reduced lactic acid and glycerol concentrations when urea is added to the fermentation, and (3) combination of the claimed the amylase used with the claimed protease at a temperature of 85° C produced better results than the use of only the amylase at 85° C.
With respect to (1) and (3) above, applicant restates their position that the ACL protease taught by Smith is the closest prior art, and therefore that their showing of increased ethanol yield with Pfu over ACL protease sufficiently shows unexpected and superior results. However, the rejection above has been clarified to show that it was expected in the field that it would be advantageous to use a thermostable Pfu protease. Specifically, as stated above, the cited Niehaus reference teaches running industrial biotechnological processes at elevated temperature has many advantages as it influences the bioavailability and solubility of compounds. Niehaus teaches the elevation of temperature is accompanied by a decrease in viscosity and an increase in the diffusion coefficient of organic. Niehaus teaches several species of extremophiles, including Pyrococcus, have been identified and that the enzymes isolated from these microorganisms show unique features, are extremely thermostable and usually resistant against chemical denaturants such as detergents, chemotropic agents, organic solvents and extremes of pH. Niehaus teaches one of the enzymes identified as being valuable for industrial use because of its ability to catalyze reactions under extreme conditions (high and extremes of pH) temperatures is a protease from Pyrococcus furiosus and that this protease has an optimal working temperature of 85°C. Smith is relied upon for teaching it is known in the art that it is advantageous to include a protease during the liquefaction. Therefore as discussed above, the skilled artisan would have been motivated to optimize Bhargava’s liquefaction step at 85°C, the optimal temperature for protease from Pyrococcus furiosus, so that Takakura’s protease is from Pyrococcus furiosus can be beneficially added to the reaction. To simplify: it was known in the art that high temperatures can improve reactions, and that adding a thermostable protease with the amylase can improve yields. Therefore the art predicts improved results with the addition of a thermostable protease, and nothing in the applicant’s reply show that the state of the art was such that the addition of a thermostable protease and elevated temperature would not be expected to yield better results. Therefore this position is not persuasive.
With respect to (2) above, it is unclear how any results showing a benefit of adding urea to the fermentation with protease from Pyrococcus furiosus is relavent to the claimed method as the claimed method does not limit to any addition of urea. ore this position is not persuasive.
Applicant again reiterates their position that because of Bhargava’s results at a temperature of 70° C, that it is improper to rely on Bhargava for teaching using a temperature of 85° C. However, as discussed at length in response to this argument above, it is the combination of the cited references that render it obvious to use a temperature of 85° C. Applicant also points to an unrelated Federal Circuit court case wherein the use of a temperature that was contrary to contrary to accepted wisdom was not deemed obvious, and concludes this case establishes Bhargava does not render it obvious to use a temperature of 85° C. However, as discussed above Bhargava specifically teaches that 85° C is considered the standard temperature and the references specifically establish the benefits of using this temperature. Therefore, the facts in the instant case are very different, and this position is not persuasive.
Applicant alleges that their prior arguments alleging unexpected results was improperly dismissed. However, as stated in the Non-Final Rejection mailed 5/7/2025, applicant’s previous arguments alleging unexpected results could not be properly evaluated for several reasons including because the image quality in the reply is too low to read, the detailed conditions are not provided so was is unclear how the “data” as “an illustrative comparison” were obtained, and the data was not presented in a declaration. Applicant now points to the attached declaration and again argues the amylase used with the claimed protease (PFU) produces more ethanol than the amylase combined with Smith’s Alcalase (ACL) protease. Applicant again alleges that Smith is the closest prior art, and although Smith’s ACL protease is taught to be useful at temperatures of 70°C, applicant only presents results wherein an elevated liquefaction temperature of 85°C (the optimal temperature of the optimal temperature of the PFU protease as taught by Niehaus and Takakura). Therefore, applicant’s results demonstrate that for liquefaction at 85°C, the use of a protease that is taught to have an optimal working temperature 70°C (Smith’s ACL) is less effective than using a protease that is taught to have an optimal working temperature 85°C (PFU as claimed and taught by Niehaus and Takakura). Given the optimal working temperatures of these two proteases, it is not unexpected that the one with a working temperature 85°C was more effective at a temperature of 85°C. Therefore, applicant’s alleged unexpected results are not persuasive.
Applicant points to the attached declaration wherein the inventor provides their opinion that a person of ordinary skill in the art would understand that pre-saccharification refers to a step that is after liquefaction but before saccharification, and not as part of the liquefaction process prior to saccharification. Based on this opinion, applicant concludes that Bhargava fails to disclose adding a glucoamylase during the liquefaction step. As an initial matter, it is noted that dependent claim 7 only limits the “optional” step of adding the glucoamylase during the liquefaction step, without requiring the optional step be included, and this dependent claim is broad to include the glucoamylase being added at any point during the liquefication step, including at the end of said step. It is also noted that the instant specification does not provide any specifical definitions of the liquefaction or saccharification steps. Therefore, given the breadth of dependent claim 7, since Bhargava teaches both the standard process wherein following liquefaction, the glucoamylase is added for the following step of saccharification, but also specifically teaches that the glucoamylase can be added sooner for pre-saccharification, this teaching reads on adding the glucoamylase during liquefaction since Bhargava specifically teaches it is added prior to the next step, which is saccharification. Again, as the timing of this optional step is very broadly claimed, this argument is not persuasive.
Applicant alleges that Lantero does not remedy the alleged deficiencies in Bhargava, Smith and Takakura. However, since applicant’s arguments above alleging deficiencies were not persuasive, this argument is not persuasive.
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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1, 3-4, 6-8 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 9,677,095. Although the claims at issue are not identical, they are not patentably distinct from each other. Patent 9,677,095 claims a method of producing a fermentation comprising liquefying starch-containing material with an alpha-amylase, glucoamylase, and protease,that is a pullulanase, followed by fermentation in the presence of a fermenting organism.
Patent 9,677,095 is silent as to the properties of the protease, glucoamylase, and alpha-amylase in various conditions.
Regarding the limitations of the relative activity of the protease, glucoamylase, and alpha-amylase in various conditions, and the sequence of the amylase, as recited in claims 1-4, 7, 18-19, and 21-25 the Patent and Trademark Office is not equipped to conduct experimentation in order to determine whether or not applicants' enzymes differ, and if so to what extent, from the protease, glucoamylase, and alpha-amylase discussed in Patent 9,677,095. The enzymes of Patent 9,677,095 are useful for the same processes as the instantly claimed enzymes, and therefore appear to be the significantly similar. Patent 9,677,095 taken as a whole demonstrates a reasonable probability that the proteases, glucoamylase, and alpha-amylase of Patent 9,677,095 is either identical or sufficiently similar to the claimed glucoamylase and alpha-amylase that whatever differences exist are not patentably significant.
Claims 1, 3-4, 6-8 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 15 and 16 of U.S. Patent No. 9,416,355 in view of in view of Smith et al (U.S. PGPUB 2008/0138871) and Takakura et al (1998, WO9856926A1).
Patent 9,416,355 claims a method of producing a fermentation comprising liquefying starch-containing material with an alpha-amylase and glucoamylase, followed by fermentation in the presence of a fermenting organism.
Patent 9,416,355 does not teach including a protease, and is silent as to the properties of the protease, glucoamylase, and alpha-amylase in various conditions.
Smith is drawn to industrial methods of producing fermentation products from starch-containing material (see paragraphs [0001]-[0003]). Smith teaches that protease treatment may advantageously be carried out simultaneously with liquefaction (see Smith paragraph [0028]), and that protease dosing during fermentation increases the overall final product yield (see Smith paragraph [0027]). Smith teaches simultaneous liquefaction of starch and protein degradation during a fermentation method by addition of a protease in the liquefaction step (see Example 2 in paragraph [0150]). Smith teaches an embodiment the protease is a Thermoascus metalloprotease (see paragraph [0066]).
Takakura teaches a hyperthermostable protease derived from thermophilic bacterium that is useful for industrial use, and has an amino acid sequence identical to SEQ ID NO: 13 (see abstract and pages 35-37).
A person of ordinary skill in the art would have had a reasonable expectation of success in adding a protease as taught by Smith, and using the protease taught by Takakura, to the liquefaction step in Patent 9,416,355’s method of fermentation because Smith teaches that protease treatment may advantageously be carried out simultaneously with liquefaction. The skilled artisan would have been motivated to add the protease taught by Takakura to the liquefaction step in Patent 9,416,355’s method of fermentation because Smith teaches that protease dosing during fermentation increases the overall final product yield and Takakura teaches a specific protease with high thermo-stability that is useful for industrial applications.
Regarding the limitations of the relative activity of the protease, glucoamylase, and alpha-amylase in various conditions, and the sequence of the amylase, as recited in claims 1-4, 7, 18-19, and 21-25 the Patent and Trademark Office is not equipped to conduct experimentation in order to determine whether or not applicants' enzymes differ, and if so to what extent, from the protease, glucoamylase, and alpha-amylase discussed in Patent 9,416,355, Smith, and Takakura. The enzymes of Patent 9,416,355, Smith, and Takakura are useful for the same processes as the instantly claimed enzymes, and therefore appear to be the significantly similar. Patent 9,416,355, Smith, and Takakura taken as a whole demonstrates a reasonable probability that the proteases, glucoamylase, and alpha-amylase of Patent 9,416,355, Smith, and Takakura is either identical or sufficiently similar to the claimed glucoamylase and alpha-amylase that whatever differences exist are not patentably significant.
Claims 1, 3-4, 6-8 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 13 and 15 of U.S. Patent No. 9,617,527 in view of in view of Smith et al (U.S. PGPUB 2008/0138871) and Takakura et al (1998, WO9856926A1), for the same reasons as stated above regarding Patent 9,416,355.
Response to Arguments
Applicant's arguments filed 10/7/2025 have been fully considered but they are not persuasive. Applicant does not provide arguments for any of the double patenting rejections.
Conclusion
No claims are free of art, no claims are 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Stephanie McNeil whose telephone number is (571)270-5250. The examiner can normally be reached Monday - Friday 9:30am - 5:30pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila Landau can be reached at 5712720614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/S.A.M/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653