Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Detailed Action
Applicant’s species election without traverse of SEQ ID NO: 2 and variant W68E in the reply filed on 10/24/25 is acknowledged.
Claims 1-20 are currently pending and are under examination.
3. Species withdrawn:
SEQ ID NO: 3 and non-elected variant are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Priority
Applicant’s claim for domestic priority under 35 U.S.C. 119(e), filed 03/07/2005, is acknowledged.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-20 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 refers to non-elected phytase having SEQ ID NO: 3. As noted in the Restriction Requirement, SEQ ID NO: 2 and NO: 3 do not share a common structure and function and therefore it is not clear why these sequences are presented in the alternative in the same claim.
Claim 1 is drawn to in step: (a) adding a variant polypeptide comprising an amino acid sequence that is at least 85% identical to the amino acid sequence as set forth in amino acid residues 23-434 of SEQ ID NO:2 or that is at least 85% identical to the amino acid sequence as set forth in SEQ ID NO:3 to an ethanol processing fluid in an ethanol production facility, wherein the ethanol processing fluid comprises phytic acid, wherein the addition of the phytase variant polypeptide improves ethanol production efficiency comprising one or more of:
The claim is confusing in referring to “wherein the addition of the phytase variant polypeptide”, a reference to previous “variant polypeptide”, which lack antecedent basis.
Rewriting the 1st part of claim 1 as recite: Claim 1 is drawn to in step: (a) adding a phytase variant polypeptide comprising an amino acid sequence that is at least 85% identical to the amino acid sequence as set forth in amino acid residues 23-434 of SEQ ID NO:2 or that is at least 85% identical to the amino acid sequence as set forth in SEQ ID NO:3 to an ethanol processing fluid in an ethanol production facility, wherein the ethanol processing fluid comprises phytic acid, wherein the addition of the phytase variant polypeptide improves ethanol production efficiency comprising one or more of:
Claim 1 refers to the phytase being “at least 85% identical” to SEQ ID NO: 2, for example. One thing is identical to another or it is not. The proper term should be --- sequence identity ---.
Claim 1 does not provide a comparison for the improved ethanol production efficiency variables listed therein.
Claim 2 lists parts of an ethanol production facility without any connections, that is, if feedstock is sitting in a barn outside, it is unclear how the feedstock impacts the efficiency of ethanol production by yeast or even in the overall ethanol production in the ethanol production facility.
Claim 5 is not clear because a commercially available phytase is not defined.
Claim 9 is unclear because a dose of 0.5 gallons per yeast propagator does not provide a concentration per gallon of phytase or the amount of yeast propagator.
Claim 10 refers to decreasing the fouling rate of a pressure, a temperature, and of a position. It is not understood how pressure, temperature, or position are fouled.
Claim 13 lists wood shavings and sawdust twice.
6. Claims 1-20 are rejected under the judicially-created basis that it contains an improper Markush grouping of alternative. See In re Harnisch, 631 F.2d 716, 721-722 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. and Int. 1984). The improper Markush grouping includes species of the claimed invention that do not share both a substantial structural feature and a common use that flows from the substantial structural feature. The members of the improper Markush grouping do not share a substantial feature and/or common use that flows from the substantial structural feature and/or common use that flows from the substantial structural feature for the following reasons:
Claim 1 refers to non-elected phytase having SEQ ID NO: 3. As noted in the Restriction Requirement, SEQ ID NO: 2 and NO: 3 do not share a common structure and function and therefore it is not clear why these sequences are presented in the alternative in the same claim.
In response to this rejection, Applicant should either amend the claim(s) to recite only individual species or groupings of species that share a substantial structural feature as well as a common use that flows from the substantial structural feature, or present a sufficient showing that the species recited in the alternative of the claims in fact share a substantial structural feature as well as a common use that flows from the substantial structural feature. This is a rejection on the merits and may be appealed to the Board of Patent Appeals and Interferences in accordance with 35 USC 134 and 37 CFR 41.31 (a)(1).
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1-20 is/are rejected under 35 U.S.C. 102a1 as being anticipated by Solbak et al. (January 20, 2015; USP 8,936,924).
Solbak et al. teach phytase having SEQ ID NO: 2 comprising 10 mutations when compared to instant SEQ ID NO: 2: Trp68Gln, Gln84Trp, Ala95Pro, Lys97Cys, Ser168Glu, Arg181Tyr, Asn226Cys, Tyr 277Asp, Met298Lys, and Ala 299Thr. While mutations are not set form in the claims, these mutations are found in Phytase Variants PV001 through PV021 at pages 12-15, and are variously included in PV022-PV079 at pages 15-24, wherein PV021 is SEQ ID NO: 2 of Solbak et al.
At Col. 134, Solbek et al teach that the phytase enzymes of invention can be used in or included/integrated at any stage of any biomass conversion process, e.g., at any one step, several steps, or included in all of the steps of Alcohol Fermentation: fuel alcohol is produced by converting cellulosic mass and/or starch to sugar, fermenting the sugar to alcohol, then separating the alcohol water mixture by distillation (Col. 135, line 15+, Claim 1). While Solbek et al. do not specify how phytase improves the ethanol production efficiency, the method taught by Solbek et al. and that claimed are the same and therefore it is inherent that the phytase increases yeast cell count, yeast budding or yeast viability; increases ethanol yield, decreases glycerol levels, or decreases total sugar levels; decreases fouling rate; increases phosphorous levels; and increases operation time of the ethanol production facility.
At Col. 139, line 55+, Solbek et al. teach that the phytases can be used in processing distillers dried grains for alcohol production--alcohol as in "spirits", e.g., beer or whiskey production (in addition to use in processing biomass for making biofuels). Phytases of this invention of this invention can be used in ethanol plants, e.g. for processing grains such as corn. Distillers dried grains can be made by first grinding a grain (e.g., corn) to a coarse consistency and adding to hot water. After cooling, yeast is added and the mixture ferments for several days to a week. The solids remaining after fermentation are the distillers grains. Phytases of this invention of this invention can be used at any step of this process. Therefore, Solbek et al. teach that the ethanol production facility is an ethanol production plant, a spirit or drinkable alcohol production plant, or a fuel ethanol plant (Claim 12).
FIG. 14, which looks like instant Figure 1, illustrates an exemplary alcohol process that can incorporate use of phytases of this invention.
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Therefore, Solbek et al. teach that the ethanol production facility comprises a feedstock, a hammer mill, a slurry tank, a jet cooker, a liquefaction, a mash cooker, a yeast mix tank, a yeast propagator, a fermentation tank, a beer, a distillation system, a whole stillage, a centrifuge, a thin stillage, an evaporator, a condensate, a syrup, a wet grain, a drum dryer, a dried distiller's grains with soluble, a condensed distiller's soluble, a dried distiller's grain, a wet distiller's grains with soluble, or any combination thereof (Claim 2). The alcohol is separated with distillation, as shown in Figure 14 as “Distillation System” (Claim 14).
Because Solbek et al. teach that the phytase enzymes of invention can be used in or included/integrated at any stage of any biomass conversion process, e.g., at any one step, several steps, or included in all of the steps of Alcohol Fermentation, then as shown in Figure 14, the phytase can be added prior to fermentation (Claim 6), to the mash cooker (Claim 7), in the yeast mix tank (Claim 8) or yeast propagator (Claim 9), which is where the yeast is grown before being added to the fermentation tank/vessel for the production of ethanol and shown in Figure 14 as “Yeast”.
The inherent decrease in fouling rate by the presence of the phytase at a beer feed valve of the beer vessel, represented/shown in Figure 14 as “Beer” (Claim 10).
At Col. 135, line 19+, Solbek et al. teach that feedstocks such as corn, wheat, barley, potatoes, switchgrass, Miscanthus, poplar wood, rice straw, corn stover, wheat straw, sugarcane bagasse, rice hulls, corn fiber, sugar beet pulp, citrus pulp, and citrus peels, hardwood and softwood thinnings, hardwood and softwood residues from timber operations, wood shavings, sawdust, paper fraction of municipal solid waste, municipal wood waste, municipal green waste, saw mill waste, pulp mill waste, construction waste, demolition waste, wood shavings, and sawdust, waste paper or other materials containing sugar, starch, and/or cellulose can be converted to sugars and then to alcohol by fermentation with yeast (Claim 14).
At Col. 16, line 9+, Solbek et al. teach that the phytase activity comprises: catalysis of phytate (myo-inositol-hexaphosphate) to inositol and inorganic phosphate; or, the hydrolysis of phytate (myo-inositol-hexaphosphate) (Claim 16).
At Col. 16, line 23+, Solbek et al. teach that the phytases are useful either alone or in combination with other reagents (including but not limited to enzymes, such as proteases, amylases and the like) (Claim 18)--are used in the processing of foodstuffs, e.g., for prevention of the unwanted corn sludge, and in other applications where phytate hydrolysis is desirable. Further, the phytases are used to eliminate or decrease the presence of unhydrolyzed phytate, especially where unhydrolyzed phytate leads to problematic consequences in ex vivo processes including--but not limited to--the processing of foodstuffs. In one aspect, phytase molecules of the invention are used in procedures including steps in the processing of corn and sorghum kernels whereby the hard kernels are steeped in water to soften them. Water-soluble substances that leach out during this process become part of a corn steep liquor, which is concentrated by evaporation. Unhydrolyzed phytic acid in the corn steep liquor, largely in the form of calcium and magnesium salts, is associated with phosphorus and deposits an undesirable sludge with proteins and metal ions. This sludge is problematic in the evaporation, transportation and storage of the corn steep liquor. Phytase molecules of the invention are used to hydrolyze this sludge; Solbak et al. Claim 7 further teaches the phytic acid is phytate in the form of calcium salts, magnesium salts, metal ions, proteins, unhydrolyzed phytate sludge, or myo-inositol-hexaphosphate. (Claim 16).
At Col. 139, line 4+, the phytases can be used with glucanases, (or cellulases), mannanases, xylanases, amylases, xanthanases and/or glycosidases, e.g., cellobiohydrolases, mannanases and/or beta-glucosidases can be used in the conversion of biomass to fuels, and in the production of ethanol. Glucanases (or cellulases), mannanases, xylanases, amylases, xanthanases and/or glycosidases, e.g., cellobiohydrolases, mannanases and/or beta-glucosidases, can be used in combination with phytase (e.g., enzymes of the invention) to produce fermentable sugars and glucan-containing biomass that can be converted into fuel ethanol. Amylases, glucoamylases, pullanases, glucoisomerase, alpha-glucosidase, and the like can be used in combination with phytase (e.g., enzymes of the invention) to convert starch to fermentable sugars or ethanol (Claim 14).
Solbek et al. Claim 10 teaches that the phytase retains activity under conditions from pH 2.5 to pH 12 (Claim 19)
Claims 3, 4, 5, and 13 are included in this rejection because the phytase is a variant of the phytase having SEQ ID NO: 2 and therefore must improve ethanol production efficiency compared to a production process where no phytase is added,
Improve the ethanol production efficiency compared to a production process where a wild-type phytase is added, and improve the ethanol production efficiency compared to a production process where a commercially available phytase or Novozyme 50160 or U.S. Water PhytOUT is added.
Claim 11 is included in this rejection because heating and cooling times of the mash and beer are inherently part of alcohol fermentation and therefore must be included in the operation time.
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 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 1-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over Claims 1-11 of U.S. Patent No. 8,936,924, which inventorship comprises Arne Solbek. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Instant Claim 1-20 are drawn to as follows:
1. A method for improving efficiency of ethanol production by yeast, the method comprising: (a) adding a variant polypeptide comprising an amino acid sequence that is at least 85% identical to the amino acid sequence as set forth in amino acid residues 23-434 of SEQ ID NO:2 or that is at least 85% identical to the amino acid sequence as set forth in SEQ ID NO:3 to an ethanol processing fluid in an ethanol production facility, wherein the ethanol processing fluid comprises phytic acid, wherein the addition of the phytase variant polypeptide improves ethanol production efficiency comprising one or more of:
increased yeast cell count, yeast budding or yeast viability;
increased ethanol yield, decreased glycerol levels, or decreased total sugar levels;
decreased fouling rate;
increased phosphorous levels; and
increased operation time of the ethanol production facility when compared to a production process wherein a wild-type phytase consisting of the amino acid sequence as set forth in Seq ID No: 2 amino acid residues 23-434 of Seq ID No: 2 is added to the ethanol processing liquid.
2. The method of claim 1, wherein said variant polypeptide having phytase activity is added anywhere in the alcohol production process wherein said alcohol production process comprises a feedstock, a hammer mill, a slurry tank, a jet cooker, a liquefaction, a mash cooker, a fermentation, a beer, a distillation system, a whole stillage, a centrifuge, a thin stillage, an evaporator, a condensate, a syrup, a wet grain, a drum dryer, a dried distiller's grains with soluble, a condensed distiller's soluble, a dried distiller's grain, a wet distiller's grains with soluble, or any combination thereof.
3. The method of claim 1, wherein said alcohol production process is in an ethanol production plant; a spirit or a drinkable alcohol production plant; or a fuel ethanol plant.
4. The method of claim 2, wherein said feedstock is selected from the group consisting of: corn, wheat, barley, potatoes, switchgrass, Miscanthus, poplar wood, rice straw, corn stover, wheat straw, sugarcane bagasse, rice hulls, corn fiber, sugar beet pulp, citrus pulp, citrus peels, hardwood, softwood thinnings, hardwood and softwood residues from timber operations, wood shavings, sawdust, paper fraction of municipal solid waste, municipal wood waste, municipal green waste, saw mill waste, pulp mill waste, construction waste, demolition waste, wood shavings, sawdust, waste paper, materials containing sugar, starch, and/or cellulose.
5. The method of claim 2, wherein the fermentation converts sugar, starch, or cellulose to alcohol with a yeast, and the alcohol is separated with distillation.
6. The method of claim 1, wherein said variant polypeptide having phytase activity hydrolyzes phytate to inositol and free phosphate with release of minerals from the phytic acid.
7. The method of claim 1, wherein the phytic acid is phytate in the form of calcium salts, magnesium salts, metal ions, proteins, unhydrolyzed phytate sludge, or myo-inositol-hexaphosphate.
8. The method of claim 1, wherein said variant polypeptide having phytase activity can be used in combination with one or more other enzymes.
9. The method of claim 8, wherein said one or more other enzymes comprises an amylase, a glucoamylase, a glucanase, a cellulase, an endoglucanase, a mannase, a xylanase, a xanthanase, a glycosidases, a cellobiohydrolase, a beta-glucosidase, a pullanase, a glucoisomerase, a alpha-glucosidase.
10. The method of claim 1, wherein said variant polypeptide having phytase activity retains phytase activity under conditions from pH 2.5 to pH 12.0.
11. The method of claim 1, wherein said variant polypeptide having phytase activity improves production of ethanol from starch.
Patented claims 1-20 are drawn to as follows:
1. A method for eliminating or reducing phytic acid and salts of phytic acid in an alcohol production process comprising: (a) providing a variant polypeptide comprising an amino acid sequence that is at least 95% identical to the amino acid sequence as set forth in SEQ ID NO: 2 and one single amino acid substitution to the amino acid sequence of SEQ ID NO: 2, wherein said one single amino acid substitution is selected from the group consisting of: A47F, T136F, N159V, N159E, T163R, D164R, G179R, V233W, Q275V, R289A, and T349Y; wherein said variant polypeptide has phytase activity and; (b) providing a composition comprising a phytic acid or a salt of phytic acid; and (c) contacting said variant polypeptide of (a) with said composition of (b), wherein said variant polypeptide hydrolyzes the phytic acid or salt of phytic acid.
2. The method of claim 1, wherein the ethanol production facility comprises a feedstock, a hammer mill, a slurry tank, a jet cooker, a liquefaction, a mash cooker, a yeast mix tank, a yeast propagator, a fermentation tank, a beer, a distillation system, a whole stillage, a centrifuge, a thin stillage, an evaporator, a condensate, a syrup, a wet grain, a drum dryer, a dried distiller's grains with soluble, a condensed distiller's soluble, a dried distiller's grain, a wet distiller's grains with soluble, or any combination thereof.
3. The method of claim 1, wherein addition of the variant polypeptide improves ethanol production efficiency compared to a production process where no phytase is added.
4. The method of claim 1, wherein addition of the variant polypeptide improves ethanol production efficiency compared to a production process where a wild-type phytase is added.
5. The method of claim 1, wherein addition of the variant polypeptide improves ethanol production efficiency compared to a production process where a commercially available phytase is added, and wherein the commercially available phytase is selected from Novozyme 50161TM and U.S. Water PhytOUT TM.
6. The method of claim 1, wherein the variant polypeptide is added to the ethanol processing fluid prior to fermentation.
7. The method of claim 1, wherein the ethanol production facility comprises a mash cooker and the phytase variant polypeptide is added to the ethanol processing fluid in the mash cooker.
8. The method of claim 1, wherein the ethanol production facility comprises a yeast mix tank and a yeast propagator and the phytase variant polypeptide is added to the ethanol processing fluid in a yeast mix tank, and wherein the ethanol processing fluid proceeds from the yeast mix tank to a yeast propagator.
9. The method of claim 1, wherein the variant polypeptide is added at a dose of 0.5 gallons per yeast propagator.
10. The method of claim 1, wherein the decreased fouling rate comprises fouling rate in one or more of beer/mash heat exchanger inlet pressure, beer feed temperature, and beer feed valve position.
11. The method of claim 1, wherein the operation time comprises one or both of beer/mash heat exchanger online time and beer feed pre-heater exchanger online time.
12. The method of claim 1, wherein the ethanol production facility is in an ethanol production plant; a spirit or a drinkable alcohol production plant; or a fuel ethanol plant.
13. The method of claim 2, wherein the feedstock is selected from the group consisting of: corn, wheat, barley, potatoes, switchgrass, Miscanthus, poplar wood, rice straw, corn stover, wheat straw, sugarcane bagasse, rice hulls, corn fiber, sugar beet pulp, citrus pulp, citrus peels, hardwood, softwood thinnings, hardwood and softwood residues from timber operations, wood shavings, sawdust, paper fraction of municipal solid waste, municipal wood waste, municipal green waste, saw mill waste, pulp mill waste, construction waste, demolition waste, wood shavings, sawdust, waste paper, materials containing sugar, starch, and cellulose.
14. The method of claim 2, wherein the ethanol production facility comprises a fermentation tank and a distillation system, wherein said fermentation tank comprises yeast cells which convert sugar, starch, or cellulose to ethanol, and the ethanol produced in the fermentation tank is separated by the distillation system.
15. The method of claim 1, wherein the variant polypeptide hydrolyzes phytate to inositol and free phosphate with release of minerals from the phytic acid.
16. The method of claim 1, wherein the phytic acid is phytate in the form of calcium salts, magnesium salts, metal ions, proteins, unhydrolyzed phytate sludge, or myo-inositol-hexaphosphate.
17. The method of claim 1, wherein the variant polypeptide is used in combination with one or more other enzymes.
18. The method of claim 17, wherein the one or more other enzymes comprise an amylase, a glucoamylase, a glucanase, a cellulase, an endoglucanase, a mannase, a xylanase, a xanthanase, a glycosidases, a cellobiohydrolase, a beta-glucosidase, a pullanase, a glucoisomerase, an alpha-glucosidase, or a combination thereof.
19. The method of claim 1, wherein the variant polypeptide retains phytase activity under conditions from pH 2.5 to pH 12.0.
20. The method of claim 1, wherein the variant polypeptide comprises the full length amino acid sequence set forth in SEQ ID NO: 2 and at least one single amino acid substitution selected from the group consisting of: A47F, T48F, T48H, T48I, T48K, T48L, T48M, T48V, T48W, T48Y, L50W, M51A, M51G, M51L, G67A, W68E, Y79H, Y79N, Y79S, Y79W, Q84W, Q86H, A95P, K97C, K97E, K97V, P100A, P102A, P102Y, I107H, I107P, I108A, I108Q, I108R, I108S, I108Y, A109V, E113P, L126R, T136H, Q137F, Q137L, Q137V, Q137Y, D139Y, P145L, L146R, L146T, F147Y, N148K, N148M, N148R, P149L, P149N, l150Tl, l150Y, K151H, K151P, C155Y, L157C, L157P, N159V, N159Q, N161K, V162L, V162T, T163R, T163P, D164R, L167S, S168R, S168E, G171M, G171S, S173G, S173H, S173V, I174F, G179R, R181Y, V191A, L192F, F194L, S197G, S208P, S211H, L216T, P217D, P217G, P217L, P217S, S218I, S218Y, N226D, N226C, A232P, V233W,Q275V, A236H, A236T, L244S, Q246W, Q247H, A248L, A248T, P254S, G257A, G257R, H263P, W265L, N266P, L269I, L269T, L269P, H272W, A274F, A274I, A274L, A274T, A274V, Q275V, Y277D, T282H, R289A, T291V, T291W, L296T, M298K, A299T Q309P, N339E, T341D, P343E, P343I, P343L, P343N, P343R, P343V, N348K, N348W, T349Y, G353C, L363P, Q377R, L379S, L379V, Q381S, S389H, S389V, G395E, G395I, G395L, G395Q, G395T, V422M, I427G, I427S, I427T, A429P, and any combination thereof, wherein said variant polypeptide has phytase activity.
Given the fact pattern of the instant APPLICATION as well as the PATENT, the genus (broad) claims of the instant application are anticipated by the species/narrower patented claims.
Claims 1-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over Claims 1-15 of U.S. Patent No. 11,447,757.
Instant genus claims are described above in paragraph 8.
Claims 1-15 of US Patent 11,447,757, species claims, are as follows:
1. A method for improving efficiency of ethanol production by fermentation in an ethanol production facility, said method comprising: adding a phytase variant polypeptide comprising an amino acid sequence as set forth in amino acid residues 23-434 of SEQ ID NO: 2 and having amino acid substitutions M298K and A299T to an ethanol processing fluid in the ethanol production facility, wherein the ethanol processing fluid comprises phytic acid, wherein the addition of the phytase variant polypeptide improves ethanol production efficiency comprising one or more of: increased yeast cell count, yeast budding or yeast viability; increased ethanol yield, decreased glycerol levels, or decreased total sugar levels; decreased fouling rate; increased phosphorous levels; and increased operation time of the ethanol production facility when compared to the ethanol production process wherein a wild-type phytase consisting of the amino acid sequence as set forth in amino acid residues 23-434 of SEQ ID NO: 2 is added to the ethanol processing fluid.
2. The method of claim 1, wherein addition of the phytase variant polypeptide improves ethanol production efficiency compared to a production process where a commercially available phytase is added, and wherein the commercially available phytase is selected from Novozyme 50161™ and U.S. Water PhytOUT™.
3. The method of claim 1, wherein the ethanol production facility includes a hammer mill for grinding feedstock, a slurry tank, a jet cooker, a liquefaction tank, a mash cooker, a yeast mix tank, a yeast propagator, a fermentation tank, a beer, a distillation system, centrifuge, an evaporator, a condensate, a syrup, a wet grain, a drum dryer, or any combination thereof.
4. The method of claim 3, wherein the ethanol production facility comprises a mash cooker and the phytase variant polypeptide is added to the ethanol processing fluid in the mash cooker.
5. The method of claim 3, wherein the ethanol production facility comprises a yeast mix tank and a Yeast propagator and the phytase variant polypeptide is added to the ethanol processing fluid in a yeast mix tank.
6. The method of claim 5, wherein the ethanol processing fluid proceeds from the yeast mix tank to ale yeast propagator.
7. The method of claim 3, wherein the wherein the ethanol production facility comprises a fermentation tank and a distillation system, wherein said fermentation tank comprises Yeast cells which convert sugar, starch, or cellulose to ethanol, and the ethanol produced in the fermentation tank is separated by the distillation system.
8. The method of claim 1, wherein the phytase variant polypeptide is added to the ethanol processing fluid prior to fermentation.
9. The method of claim 1, wherein the phytase variant polypeptide hydrolyzes phytic acid to inositol and free phosphate with release of minerals from the phytic acid.
10. The method of claim 9, wherein the phytic acid is phytate in the form of calcium salts, magnesium salts, metal ions, proteins, unhydrolyzed phytate sludge, or myo-inositol-hexaphosphate.
11. The method of claim 1, wherein the phytase variant polypeptide is used in combination with one or more other enzymes.
12. The method of claim 11, wherein the one or more other enzymes comprise an amylase, a glucoamylase, a glucanase, a cellulase, an endoglucanase, a mannase, a xylanase, a xanthanase, a glycosidases, a cellobiohydrolase, a beta-glucosidase, a pullanase, a glucoisomerase, an alpha-glucosidase, or a combination thereof.
13. The method of claim 1, wherein the phytase variant polypeptide retains phytase activity under conditions from pH 2.5 to pH 12.0.
14. The method of claim 1, wherein the ethanol is produced from a feedstock is selected from the group consisting of corn, wheat, barley, potatoes, switchgrass, Miscanthus, poplar wood, rice straw, corn stover, wheat straw, sugarcane bagasse, rice hulls, corn fiber, sugar beet pulp, citrus pulp, citrus peels, hardwood, softwood thinnings, hardwood and softwood residues from timber operations, paper traction of municipal solid waste, municipal wood waste, municipal green waste, saw mill waste, pulp mill waste, construction waste, demolition waste, wood shavings, sawdust, waste paper, materials containing sugar, starch, and cellulose.
15. The method of claim 1, wherein the ethanol production facility is in an ethanol production plant; a spirit or a drinkable alcohol production plant; or a fuel ethanol plant.
Given the fact pattern of the instant APPLICATION as well as the PATENT, the genus (broad) claims of the instant application are anticipated by the species/narrower patented claims.
No claim is allowed.
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/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940