DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
Change in Examiner
Please note that the Examiner for this application has changed.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 05/18/2026 has been entered.
Claim Objections
Claim 3 is objected to because of the following informalities: “CaCl2)” should be ““CaCl2”. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b), Indefiniteness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 3-4, and 6-8 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.
Claims 1 and 4 recite “80oC/70oC”; however, it is unclear if the “/” means temperatures ranging from 70-80oC, or if the temperature can be selected from either 70oC or 80oC, or if the relative activity is determined at both 70oC and 80oC. For the purposes of applying prior art, the Examiner has interpreted “80oC/70oC” to mean temperatures ranging from 70-80oC.
Claim 3 recites “(min)” in parentheses; however, it is unclear if what is recited in parentheses is part of the claimed invention, or a preferred embodiment. For the purposes of applying prior art, the Examiner has interpreted what is recited in parentheses to be a preferred embodiment.
Claims 6-8 are included in this rejection for depending on rejected independent claim 1 and failing to rectify the noted deficiency.
Claim Rejections - 35 USC § 112(a), Written Description
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 3-4, and 6-8 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Independent claim 1 recites “an alpha-amylase having at least 80% sequence identity” and “a protease having at least 80% sequence identity”. Regarding the alpha-amylase, the instant specification states “In an embodiment the alpha-amylase may be an enzyme having a degree of identity of at least 60%, e.g., at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% to any of the sequences shown in SEQ ID NO: 3 in WO 99/19467 or SEQ ID NO: 1 herein” (see, e.g., instant specification, pg. 8, lines 25-28). Regarding the protease, the instant specification states “In another embodiment the thermostable protease is one disclosed in SEQ ID NO: 13 herein or a protease having at least 80% identity, such as at least 85%, such as at least 90%, such as at least 95%, such as at least 96%, such as at least 97%, such as at least 98%, such as at least 99% identity to SEQ ID NO: 1 in US patent no. 6,358,726-B1 or SEQ ID NO: 13 herein” (see, e.g., instant specification, pg. 16, lines 7-10). The instant specification does not teach core structures and/or amino acids for the claimed alpha-amylase and the claimed protease. Moreover, claim 1 recites that the alpha-amylase can have at least 80% sequence identity to SEQ ID NO: 1, which accounts for up to 20% variation (up to 103 amino acid variation) in SEQ ID NO: 1. Additionally, claim 1 recites that the protease can have at least 80% sequence identity to SEQ ID NO: 1, which accounts for up to 20% variation (up to 82 amino acid variation) in SEQ ID NO: 13. Therefore, the instant specification fails to provide written description and guidance for which amino acids can be manipulated within SEQ ID NOs: 1 and 13 in order to maintain alpha-amylase activity and protease activity, especially when there can be up to 103 amino acid variation for SEQ ID NO: 1 and up to 82 amino acid variation for SEQ ID NO: 13. In regards to the core structures(s) and/or sequences, the instant specification does not provide written description and guidance related to core structures for the alpha-amylase and protease proteins; therefore, one of ordinary skill in the art would not have guidance for which amino acids one cannot manipulate in SEQ ID NOs: 1 and 13 in order to maintain enzyme activity.
Claim Rejections - 35 USC § 103, Obviousness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 3-4, and 6-7 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bhargava (US 2007/0184150; Date of Publication: August 9, 2007 – previously cited), as evidenced by Svendsen (U.S. Patent No. 6,187,576; Date of Publication: February 13, 2001 – previously cited), GenBank (alpha amylase [Geobacillus stearothermophilus]: AAB86961.1 – previously cited), and Chen (Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase; 1996 – newly cited), in view of Takakura (US 2002/0132335; Date of Publication: September 19, 2002 – newly cited), Smith (US 2008/0138871; Date of Publication: June 12, 2008 – previously cited), and Niehaus (Extremophiles as a source of novel enzymes for industrial application; 1999 – previously cited).
Bhargava’s general disclosure relates to “process of liquefying starch-containing material, with a bacterial alpha-amylase at a temperature in the range from 65-75oC for 1 to 2 hours” (see, e.g., Bhargava, abstract). Moreover, Bhargava discloses “The present invention provides an improved liquefaction process suitable as a step in processes for producing fermentation products such as especially ethanol or syrups such as glucose or maltose” (see, e.g., Bhargava, [0015]).
Regarding claim 1 pertaining to producing fermentation products from starch-containing materials, Bhargava teaches “a process of liquefying starch-containing material, comprising treating the starch-containing material with a bacterial alpha-amylase at a temperature in the range from 65-75oC for 1 to 2 hours (see, e.g., Bhargava, [0007]). Bhargava teaches “A liquefaction process of the invention may be carried out at pH 4.5-6.5, in particular at a pH between 5 and 6” (see, e.g., Bhargava, [0008]). Bhargava teaches “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, e.g., Bhargava, [0046] & [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). Genebank 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. Furthermore, Bhargava teaches that the saccharification step can be performed with a glucoamylase (see, e.g., Bhargava, [0037]), and the saccharified material can be fermented using a fermenting microorganism (see, e.g., Bhargava, [0033]). The Examiner has interpreted the limitation(s) following the phrase “optionally” to not be required as part of the claimed invention.
Regarding claim 3 pertaining to the alpha-amylase, Bhargava, as evidenced by Svendsen and GeneBank, teach the same alpha-amylase as instantly claimed; therefore, the alpha-amylase taught by Bhargava, Svendsen, and GeneBank would inherently have a T1/2 (min) at pH 4.5, 85oC, 0.12 mM CaCl2 for at least 10 (MPEP 2112.01(I)).
Regarding claim 7 pertaining to the glucoamylase, Bhargava teaches that the glucoamylase can be added during liquefaction (see, e.g., Bhargava, [0018]). Moreover, Bhargava teaches that the glucoamylase used can be a glucoamylase of fungal or bacterial origin, or variants of Aspergillus glucoamylases (see, e.g., Bhargava, [0051]). Bhargava teaches “Other Aspergillus glucoamylase variants include variants to enhance the thermal stability: G137A and G139A (Chen et al. (1996), Prot. Eng. 9, 499-505); D257E and D293E/Q (Chen et al. (1995), Prot. Engng. 8, 575-582); N182 (Chen et al. (1994), Biochem. J. 301, 275-281); disulphide bonds, A246C (Fierobe et al. (1996), Biochemistry, 35, 8698-8704; and introduction of Pro residues in position A435 and S436 (Li et al. (1997), Protein Engng. 10, 1199-1204” (see, e.g., Bhargava, [0052]). Chen is cited solely as evidence that the Aspergillus glucoamylase variant G137A and G139A (Chen et al. (1996), Prot. Eng. 9, 499-505), as referenced in Bhargava, has stability at pH 5.5 (see, e.g., Chen, GA thermostability, pg. 503) and at temperatures above 70oC (see, e.g., Chen, Conclusion, pg. 504).
However, Bhargava does not teach: a protease having at least 80% sequence identity to SEQ ID NO: 13 and having a thermostability value of more than 50% determined as Relative Activity at 80°C/70°C (claim 1); or wherein the protease has a thermostability of more than 90% determined as Relative Activity at 80°C/70°C (claim 4); or wherein the protease is derived from a strain of Pyrococcus (claim 6).
Takakura’s general disclosure relates to “A hyperthermostable protease having the amino acid sequence represented by the SEQ ID NO:1 of the Sequence Listing or a sequence derived therefrom by deletion, substitution, insertion or addition of one to several amino acid residues, a gene encoding the hyperthermostable protease, and a process for preparing the protease, aiming at providing by genetic engineering techniques a hyperthermophile protease which is advantageous for industrial use” (see, e.g., Takakura, abstract).
Regarding claims 1, 4, and 6 pertaining to the protease, Takakura teaches SEQ ID NO: 1, which has 100% sequence identity to instant SEQ ID NO: 13 and is derived from Pyrococcus furiosus (see, e.g., Takakura, [0011] & Office Action Appendix). Moreover, since Takakura’s protease is identical to the instantly claimed protease, the protease taught by Takakura would inherently have a thermostability value of more than 50% determined as Relative Activity at 80°C/70°C and would have a thermostability of more than 90% determined as Relative Activity at 80°C/70°C (see, e.g., MPEP 2112.01(I)).
Smith’s general disclosure relates to industrial methods of producing fermentation products from starch-containing material (see paragraphs [0001]-[0003]), wherein said method comprises “liquefying said starch-containing material with an alpha-amylase; treating with a protease; saccharifying in the presence of a carbohydrate-source generating enzyme; fermenting in the presence of a fermenting organism” (see, e.g., Smith, abstract).
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]). 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]).
Niehaus’ general disclosure relates to a review discussing “the biotechnological significance of extreme thermophilic (optimal growth 70–80 °C) and hyperthermophilic (optimal growth 85–100 °C) archaea and bacteria. In particular, we will focus on selected extracellular-polymer-degrading enzymes, such as amylases, pullulanases, cyclodextrin glycosyltransferases, cellulases, xylanases, chitinases, proteinases and other enzymes such as esterases, glucose isomerases, alcohol dehydrogenases and DNA-modifying enzymes with potential use in food, chemical and pharmaceutical industries and in environmental biotechnology” (see, e.g., Niehaus, abstract).
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). 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). 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). 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).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to liquefy a starch-containing material using alpha-amylase, as taught by Bhargava, wherein the liquefication step also comprises using a protease, as taught by Takakura, Smith, and Niehaus. One would have been motivated to do so because Bhargava teaches that liquefication of a starch-containing material typically occur at temperatures above 85oC in order to thin the starch-containing slurry (see, e.g., Bhargava, [0016]) and Takakura teaches that instant SEQ ID NO: 1 encodes a hyperthermostable protease that has thermostable protease activity (see, e.g., Takakura, [0011]) and that is obtained from thermophilic bacteria grown at temperatures upwards of 90-100oC (see, e.g., Takakura, [0006]). 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. Therefore, based on the teachings of Bhargava, Takakura, Smith, and Niehaus, it would have been obvious to use a protease corresponding to instant SEQ ID NO: 1 during the liquefication process because the liquefication process occurs at temperatures upwards of 85oC and the protease is thermostable at high temperatures and using the protease during fermentation will increase the overall yield of the final product. One would have expected success because Bhargava, Takakura, Smith, and Niehaus all teach bacterially-derived enzymes for use in biological methods.
Claim 8 rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bhargava, Takakura, Smith, and Niehaus, as applied to claims 1, 3-4, and 6-7 above, and further in view of Lantero (US 2005/0100996; Date of Publication: May 12, 2005 – previously cited).
The references of Bhargava, Takakura, Smith, and Niehaus are discussed above.
However, the references does not teach: wherein a pullulanase is present during liquefaction and/or saccharification (claim 8).
Lantero’s general disclosure relates to “the production of desired end-products of in vitro and/or in vivo bioconversion of biomass-based feed stock substrates, including but not limited to such materials as starch and cellulose’ (see, e.g., Lantero, abstract). Moreover, Lantero discloses means for the production of ethanol directly from granular starch (see, e.g., Lantero, [0005]).
Regarding claim 8 pertaining to the pullulanase, Lantero teaches that pullulanases can be added during saccharification because pullulanases “remove successive glucose units from the non-reducing ends of the starch. This enzyme is capable of hydrolyzing both the linear and branched glucosidic linkages of starch, amylose and amylopectin” (see, e.g., Lantero, [0102]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to liquefy a starch-containing material using an alpha-amylase and protease, followed by saccharifying the liquefied starch-containing material using a glucoamylase, as taught by Bhargava, Takakura, Smith, and Niehaus, wherein the saccharification step further comprises a pullulanase, as taught by Lantero. One would have been motivated to do so because Lantero teaches that pullulanases “hydrolyze α-1,6-glucosidic bonds. Thus, during the saccharification of the liquefied starch, pullulanases remove successive glucose units from the non-reducing ends of the starch. This enzyme is capable of hydrolyzing both the linear and branched glucosidic linkages of starch, amylose and amylopectin” (see, e.g., Lantero, [0102]). Moreover, Bhargava teaches saccharification of a starch-containing material in order to obtain a fermentation product, preferably ethanol (see, e.g., Bhargava, [0029]), wherein prior to saccharification, the starch-containing material is first liquefied using a alpha-amylase and protease in order to increase the overall yield of the final product, as taught by Bhargava (see, e.g., Bhargava, col. 12, lines 22-25, and SEQ ID NO: 3), Takakura (see, e.g., Takakura, abstract & [0011]), Smith (see, e.g., Smith, [0027]-[0028]), and Niehaus (see, e.g., Niehaus, col. 2 on page 711). Therefore, based on these teachings, it would have been obvious to include a pullulanase during the saccharification process, following liquefication, in order to hydrolyze the linear and branched glucosidic linkages of the starch-containing material in order to produce a fermentation product. One would have expected success because Bhargava, Takakura, Smith, Niehaus, and Lantero all teach enzymes that can be used during various biological processes. Additionally, Bhargava and Lantero both teach saccharification of starch-containing materials.
Examiner’s Response to Arguments
Applicant's arguments filed 05/18/2026 have been fully considered but they are not persuasive.
Regarding Applicant’s argument pertaining to Bhargava teaching away from liquefaction at 85oC using its own alpha-amylase (remarks, pages 2-4), this argument is not persuasive because Bhargava teaches "Liquefaction is usually carried out using a bacterial alpha-amylase at temperatures above 85oC" [0016]. The reference teaches when decreasing the temperature during liquefaction to around 70oC the ethanol yield after simultaneous saccharification and fermentation (SSF) was improved (see Example 1)." Example 1 teaches: The results show that 70oC liquefaction produces ethanol at a faster rate than the standard 85oC liquefaction material. At 42 hours there is a 20% higher ethanol level using the 70oC liquefied corn mash. Bhargava does not teach away from using a temperature of 85oC as argued by applicant. Bhargava does not state any deleterious effects of using 85oC. Rather the references states that after 42 hours ethanol yield is better at about 70 compared to 85oC. Note MPEP 2123: Disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments. Thus, the preferred embodiment is not a teaching away from the general and standard temperature range and Bhargava teaches multiple temperatures by which the alpha-amylase can perform at, such as 70 and 85oC. Moreover, based on Bhargava’s teachings, one of ordinary skill in the art would be motivated to manipulate or optimize the temperature range for the alpha-amylase. Furthermore, Smith also states on para 42 "the exact temperature of gelatinization depends on the specific starch, and can readily be determined by the skilled artisan. Thus, the initial gelatinization temperature may vary according to the plant species, to the particular variety of the plant species as well as with the growth conditions." Clearly Smith teaches the general state of the art where it is recognized the temperature varies based on the specific conditions used in the process. Niehaus teaches the advantageous use of a specific protease and Takakura teaches instant protease with optimal temperature at 80-95. Thus, the manipulation of the temperature based on the specific enzymes used in the process is within the skill of an artisan. Again, Bhargava does not teach away from 85 degrees Celsius and rather teaches after 42 hours the ethanol yield is less than the process using about 70 degrees C. However, the motivation to use the instant protease as taught by Smith is to increase ethanol yield and Takakura teaches that the instant protease is stable with optimal temperature at 80-95oC.
Regarding Applicant’s arguments pertaining to the Soong Declaration/Exhibit A and unexpected results (remarks, pages 4-5), Applicant’s results are not commensurate in scope with the claimed invention. In Exhibit A, Applicant is relying on specific materials, percentages, concentrations, pH, times, doses, volumes, etc., all of which are not part of the instantly claimed invention. Therefore, these results are not commensurate in scope with the claimed invention. Moreover, as stated in the rejection above, it would have been obvious to include a protease in light of the teachings of Smith because a 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]). Therefore, the results of the Declaration pertaining to the instant invention increasing yield through inclusion of a protease would be expected or obvious since Smith teaches that addition of a protease increases yield during fermentation, and one of ordinary skill in the art would be motivated to include the protease in order to increase yield during fermentation.
Regarding Applicant’s argument pertaining to Bhargava not teaching addition of a glucoamylase during liquefaction (remarks, page 7), this argument is not persuasive because Bhargava teaches that the glucoamylase can be added during liquefaction (see, e.g., Bhargava, [0018]). Therefore, the glucoamylase is indeed taught to be present during liquefaction.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 3-4, 6-8 and 18 are 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, 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, 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.
Examiner’s Response to Arguments
Regarding Applicant’s arguments pertaining to the double patenting rejections (remarks, page 8), Applicant does not provide any arguments for the double patenting rejections; therefore, these rejections have been maintained.
Conclusion
Claims 1, 3-4, and 6-8 are rejected.
No claims are allowed.
Correspondence Information
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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