DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 09/08/2025 has been entered.
Status of the Claims
Claims 1-29 were cancelled in a previous communication. Claim 30 has been cancelled. New claims 63-68 have been added.
Claims 31-68 are pending and currently under examination.
All rejections not reiterated have been withdrawn.
Claim Rejections - 35 USC § 112
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 31-68 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 31 recites “wherein an enzyme blend comprising at least two hemicellulases and/or at least two beta-glucanases and a cellulolytic composition is added to whole stillage”. This language is indefinite because it is unclear whether the enzyme blend only requires the cellulolytic composition when the at least two beta-glucanases are present or is the cellulolytic composition present when the at least two hemicellulases and/or at least two beta-glucanases are present in the enzyme blend.
Claims depending from rejected claims have also been rejected because they incorporate
all of the limitations of the claims from which they depend, but fail to resolve the indefiniteness
concerns outlined above.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 31-35, 38-51, and 54-68 are rejected under 35 U.S.C. 103 as being unpatentable over Lee (US20120064213A1, Published 03/15/2012) in view of Milos et al. (US20130330791A1, Published 12/12/20213; cited in the IDS filed 11/06/2023) further in view of Diao et al. (US20170298394A1, Published 10/19/2017) further in view of Peng et al. (US20170335302A1, Published 11/23/2017).
Applicant’s Invention
The applicant’s claims are drawn to a method for producing a feed ingredient from a whole stillage, the method comprising: a) performing a starch-containing grain dry milling process for producing a fermentation product to produce a fermentation product and a whole stillage, wherein step a) comprises: (i) saccharifying the starch-containing grain at a temperature below the initial gelatinization temperature with an alpha-amylase and a glucoamylase; and(ii) fermenting using a fermenting organism to produce the fermentation product, wherein an enzyme blend comprising at least two hemicellulases and/or at least two beta-glucanases and a cellulolytic composition is added to whole stillage, wherein the hemicellulases comprise a GH10 xylanase and a GH62 a-L- arabinofuranosidase, wherein the GH10 xylanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 20 to 397 of SEQ ID NO: 2,wherein the GH62 a-L-arabinofuranosidase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 325 of SEQ ID NO: 11;wherein the beta-glucanases are from a family selected from the group consisting of GH5 15 and GH64,wherein the GH5 15 family beta-glucanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 408 of SEQ ID NO: 15,wherein the GH64 family beta-glucanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 447 or 64 to 447 of SEQ ID NO: 20;wherein the cellulolytic composition comprises:(i) a cellobiohydrolase I having an amino acid sequence comprising at least 85% sequence identity to amino acids 27 to 532 of SEQ ID NO: 21;(ii) a beta-glucosidase having an amino acid sequence comprising at least 85% sequence identity to amino acids 20 to 863 of SEQ ID NO: 23 with the substitutions F100D,S283G, N456E, and F512Y; and(iii) an endoglucanase I having an amino acid sequence comprising at least 85% sequence identity to amino acids 23 to 459 of SEQ ID NO: 44; b) separating the whole stillage into an insoluble solids portion and a thin stillage portion; c) separating the thin stillage portion into at least a first separated water-soluble solids portion, and at least a first separated protein portion; d) optionally separating at least the first separated protein portion into at least a second separated water-soluble solids portion, and at least a second separated protein portion; and e) drying at least the first separated protein portion, and/or optionally at least the second separated protein portion, to define a protein product, wherein the protein product is a feed ingredient comprising at least 40 wt. percent protein on a dry basis.
Determination of the scope and the content of the prior art
(MPEP §2141.01)
Regarding claims 31,41, and 57, Lee teaches a method for producing a high protein corn meal from a whole stillage byproduct includes, in a corn dry-milling process for making ethanol, separating the whole stillage byproduct into an insoluble solids portion and a thin stillage portion. The thin stillage portion is separated into a protein portion and a water soluble solids portion. Then, the protein portion is dewatered and dried to define a high protein corn meal that includes at least 40 wt. % protein on a dry basis (page 1, paragraph [0008]). Lee further teaches the high protein corn meal includes at least 45 wt. % protein on a dry basis. In another embodiment, the high protein corn meal includes at least 50 wt. % protein on a dry basis. In yet another embodiment, the high protein corn meal includes at least 60 wt. % protein on a dry basis. In still another embodiment, the high protein corn meal includes about 56 wt. % protein on a dry basis (paragraph [0078]).
Regarding claims 32 and 48, Lee teaches the saccharification and fermentation steps occur simultaneously (page 2, paragraph [0024]).
Regarding claims 33-35 and 49-51, Lee teaches in the fermentation step, a common strain of yeast (Saccharomyces cerevisiae) (i.e., fermenting organism) is added to metabolize the glucose sugars into ethanol (i.e., fermentation product) (page 2, paragraph [0024]).
Regarding claims 42-43 and 58-59, Lee teaches a method and system for producing a high protein corn meal, collectively, from the whole stillage byproduct which produce a high protein corn meal that can be sold, e.g., as pig and chicken feed (i.e., animal feed) (page 2, paragraph [0027]).
Regarding claims 44 and 60, Lee teaches the method of after separating the whole stillage byproduct into an insoluble solids portion and a thin stillage portion and before separating the thin stillage portion into a protein portion and a water soluble solids portion, separating fine fiber from the thin stillage portion (page 11, claim 6).
Regarding claims 45 and 61, Lee teaches the method further including separating soluble solids from the water soluble solids portion to provide a soluble solids portion (page 11, claim 11).
Regarding claims 46 and 62, Lee teaches the method further including separating oil from the water soluble solids portion to provide an oil portion (page 11, claim 13).
Regarding claim 47, Lee teaches in Fig. 1 a typical corn dry milling process beginning with a milling step and then the ground meal is mixed with water to create a slurry, and a commercial enzyme such as alpha-amylase is added. This slurry is then heated in a pressurized jet cooking process to solubilize the starch in the ground meal. This is followed by a liquefaction step 16 at which point additional alpha-amylase may be added. The alpha-amylase hydrolyzes the gelatinized starch into maltodextrins and oligosaccharides to produce a liquefied mash or slurry (page 2, paragraph [0023]). Lee also teaches the liquefaction step is followed by saccharification and fermentation steps, wherein in the saccharification step, the liquefied mash is cooled and a commercial enzyme such as glucoamylase is added and in the fermentation step, a common strain of yeast (Saccharomyces cerevisiae) is added (page 2, paragraph [0024]).
Ascertainment of the Difference Between Scope the Prior Art and the Claims
(MPEP §2141.02)
Lee does not teach wherein (i) saccharifying a starch-containing grain at a temperature below the initial gelatinization temperature with an alpha-amylase and a glucoamylase; and (ii) fermenting using a fermentation organism to produce the fermentation product (instant claim 31); and wherein an enzyme blend comprising at least two hemicellulases and/or at least two beta-glucanases and a cellulolytic composition is added to whole stillage, wherein the hemicellulases comprise a GH10 xylanase and a GH62 a-L- arabinofuranosidase, wherein the GH10 xylanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 20 to 397 of SEQ ID NO: 2, wherein the GH62 a-L-arabinofuranosidase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 325 of SEQ ID NO: 11; wherein the beta-glucanases are from a family selected from the group consisting of GH5 15 and GH64,wherein the GH5 15 family beta-glucanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 408 of SEQ ID NO: 15,wherein the GH64 family beta-glucanase has an amino acid sequence comprising at least 85% sequence identity to amino acids 17 to 447 or 64 to 447 of SEQ ID NO: 20;wherein the cellulolytic composition comprises:(i) a cellobiohydrolase I having an amino acid sequence comprising at least 85% sequence identity to amino acids 27 to 532 of SEQ ID NO: 21;(ii) a beta-glucosidase having an amino acid sequence comprising at least 85% sequence identity to amino acids 20 to 863 of SEQ ID NO: 23 with the substitutions F100D,S283G, N456E, and F512Y; and(iii) an endoglucanase I having an amino acid sequence comprising at least 85% sequence identity to amino acids 23 to 459 of SEQ ID NO: 44 (instant claims 31, 47, and 63-68). Lastly, Lee does not teach wherein: (i) the hemicellulase increases the mass fraction of the high protein feed ingredient compared to the mass of the high protein feed ingredient in the absence of the hemicellulase; and (ii) the beta-glucanase increases the percent protein on a dry basis of the high protein feed ingredient compared to the percent protein on a dry basis of the high protein feed ingredient in the absence of the beta-glucanase (instant claims 38-40 and 54-56). However, these deficiencies are cured by Milos et al, Diao et al, and Peng et al.
In the analogous art of producing a fermentation product and by-products in the fermentative production process, Milos teaches subjecting the fermented mash after the fermentation to an enzyme composition comprising an enzyme or a mixture of enzymes capable of degrading one or more fermented mash components (page 2, paragraph [0038]), wherein the enzyme composition in particular is by using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase (i.e., hemicellulase) (page 3, paragraph [0042]), and wherein stillage is the product which remains after the mash has been converted to sugar, fermented and distilled into ethanol (page 2, paragraph [0040]). Milos also teaches another well-known process, often referred to as a “raw starch hydrolysis” process (RSH process), includes grinding the starch-containing material and then simultaneously saccharifying and fermenting granular starch below the initial gelatinization temperature typically in the presence of an acid fungal alpha-amylase and a glucoamylase (page 4, paragraph [0060]). Milos further teaches fermenting the saccharified material using a suitable fermenting organism (page 3, paragraph [0050]). Milos continues to teach the most widely used process to produce a fermentation product, especially ethanol, is the simultaneous saccharification and fermentation (SSF) process, in which there is no holding stage for the saccharification, meaning that a fermenting organism, such as a yeast, and enzyme(s), including the hemicellulase(s) and/or specific endoglucanase(s), may be added together (page 7, paragraph [0105]). Milos further teaches surprisingly, the degradation of the fermenting microorganisms itself by adding the enzyme composition according to the present disclosure, in particular by using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content in the beer mash which results in an improvement of the nutrition quality like the protein content of the byproducts, as well as reduction of NSPs resulting from the fermentative organism cell wall like the yeast cell wall (page 3, paragraph [0042]).
In the analogous art of improved processes for producing ethanol from cellulosic material and improved fermenting organisms, Diao teaches (a) saccharifying a cellulosic material with a cellulolytic enzyme composition; (b) fermenting the saccharified cellulosic material with a fermenting microorganism to produce ethanol; wherein the fermenting organism is Saccharomyces cerevisiae (paragraph [0006]). Diao further teaches the term “cellulolytic enzyme composition” or “cellulase” means one or more (e.g., several) enzymes that hydrolyze a cellulosic material. Such enzymes include endoglucanase(s), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof (paragraph [0042]). Diao also teaches Hemicellulases are key components in the degradation of plant biomass, wherein examples of hemicellulases include, but are not limited to, arabinofuranosidase, and a xylanase (paragraph [0053]). Diao further teaches that the cellulolytic enzyme composition comprises GH10 xylanase of SEQ ID NO:16 herein (GENSEQP Accession No. BAK46118) (i.e., 100% match of instantly claimed SEQ ID NO:2), the beta-glucosidase variant of SEQ ID NO: 5 herein (GENSEQP Accession No. AZU67153, with one or more, in particular all, of the following substitutions: F100D, S283G, N456E, F512Y (i.e., 99.5% match of instantly claimed SEQ ID NO:23) (paragraph [0167]), EG I (i.e., endoglucanase I) of SEQ ID NO: 21 herein (Swissprot Accession No. P07981) (i.e., 100% match of instantly claimed SEQ ID NO:44) (paragraph [0168]). Diao continues to teach the cellulolytic enzyme composition used in a process of the invention may in one embodiment comprise one or more CBH I (cellobiohydrolase I), wherein in one embodiment the cellulolytic enzyme composition comprises a cellobiohydrolase I (CBH I), such as one derived from a strain of the genus Aspergillus, such as a strain of Aspergillus fumigatus, such as the Cel7A CBH I disclosed SEQ ID NO: 10 herein (i.e., 100% match of instantly claimed SEQ ID NO: 21) (paragraph [0211]).
In the analogous art of compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity for use in e.g. animal feed, Peng teaches compositions comprising one or more GH10 or GH11 polypeptides having xylanase activity and one or more GH62 polypeptides having arabinofuranosidase activity (paragraph [0009]). Peng further teaches certain arabinofuranosidases from glycoside hydrolase family 62 (herein referred to as GH62) in combination with one or more GH10 or GH11 xylanase are surprisingly good at solubilizing the xylose backbone of sterically hindered arabinoxylan found in plant based material from the sub-family Panicoideae (paragraph [0336]), wherein the composition comprises a GH62 polypeptide having arabinofuranosidase activity having a sequence identity to SEQ ID NO: 27 of at least 99% (i.e., 100% match of instantly claimed SEQ ID NO:11) (paragraph [0398]).
Finding of Prima Facie Obviousness Rationale and Motivation
(MPEP §2142-2143)
It would have been prima facie obvious to one of ordinary skill in the art at the time of filing to have an enzyme blend comprising at least two hemicellulose and/or at least two beta-glucanase in Lee’s method for producing a high protein corn meal from a whole stillage byproduct. Lee teaches a method for producing a high protein corn meal from a whole stillage byproduct. One would have understood in view of Milos that the fermenting organism may be a fungal organism such as yeast, wherein the preferred yeasts according to the disclosure are Saccharomyces species, in particular Saccharomyces cerevisiae (page 3, paragraph [0052]) and that enzyme compositions using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content which results in an improvement of the nutrition quality like the protein content of the byproducts (page 3, paragraph [0042]). One of ordinary skill would have been motivated to have a hemicellulose, a beta-glucanase, or an enzyme blend comprising hemicellulose and/or beta-glucanase in Lee’s method for producing a high protein corn meal from a whole stillage byproduct because Milos teaches that adding the enzymes will result in an increase of the nutrition content which results in an improvement of the nutrition quality like protein content of the byproducts. The artisan of ordinary skill would have reasonable expectation of success because Lee teaches methods for producing a high protein corn meal from whole stillage byproduct (abstract).
With regards to claim 31, wherein step a) is performed and performing step a) comprises: (i) saccharifying a starch-containing grain at a temperature below the initial gelatinization temperature with an alpha-amylase and a glucoamylase, it would have been obvious to one of ordinary skill to perform step a) by saccharifying a starch-containing grain in Lee’s method for producing a high protein corn meal from a whole stillage byproduct because Milos teaches the process of dry-grind wherein the “raw starch hydrolysis” process is a well-known process for dry-grind milling.
With regards to claims 31, 47, and 63-68 wherein the hemicellulases comprise a GH10 xylanase and a GH62 a-L- arabinofuranosidase, wherein the GH10 xylanase has an amino acid sequence comprising at least 85%, 90%, 95%, and 100% sequence identity to amino acids 20 to 397 of SEQ ID NO: 2; wherein the cellulolytic composition comprises:(i) a cellobiohydrolase I having an amino acid sequence comprising at least 85%, 90%, 95%, and 100% sequence identity to amino acids 27 to 532 of SEQ ID NO: 21;(ii) a beta-glucosidase having an amino acid sequence comprising at least 85%, 90%, 95%, and 100% sequence identity to amino acids 20 to 863 of SEQ ID NO: 23 with the substitutions F100D,S283G, N456E, and F512Y; and(iii) an endoglucanase I having an amino acid sequence comprising at least 85%, 90%, 95%, and 100% sequence identity to amino acids 23 to 459 of SEQ ID NO: 44, it would have been obvious to one of ordinary skill in the art to have SEQ ID NOs: 2, 21, 23, and 44 in Lee’s method for producing a high protein corn meal from a whole stillage byproduct. Milos that the fermenting organism may be a fungal organism such as yeast, wherein the preferred yeasts according to the disclosure are Saccharomyces species, in particular Saccharomyces cerevisiae (page 3, paragraph [0052]) and that enzyme compositions using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content which results in an improvement of the nutrition quality like the protein content of the byproducts (page 3, paragraph [0042]). One would have understood in view of Diao that one can (a) saccharifying a cellulosic material with a cellulolytic enzyme composition; (b) fermenting the saccharified cellulosic material with a fermenting microorganism to produce ethanol (paragraph [0006]). Diao also teaches hemicellulases are key components in the degradation of plant biomass, wherein examples of hemicellulases include, but are not limited to, arabinofuranosidase, and a xylanase (paragraph [0053]). Diao further teaches that the cellulolytic enzyme composition comprises GH10 xylanase of SEQ ID NO:16 herein (GENSEQP Accession No. BAK46118) (i.e., 100% match of instantly claimed SEQ ID NO:2), the beta-glucosidase variant of SEQ ID NO: 5 herein (GENSEQP Accession No. AZU67153, with one or more, in particular all, of the following substitutions: F100D, S283G, N456E, F512Y (i.e., 99.5% match of instantly claimed SEQ ID NO:23) (paragraph [0167]), EG I (i.e., endoglucanase I) of SEQ ID NO: 21 herein (Swissprot Accession No. P07981) (i.e., 100% match of instantly claimed SEQ ID NO:44) (paragraph [0168]). Diao continues to teach the cellulolytic enzyme composition used in a process of the invention may in one embodiment comprise one or more CBH I (cellobiohydrolase I), wherein in one embodiment the cellulolytic enzyme composition comprises a cellobiohydrolase I (CBH I), such as one derived from a strain of the genus Aspergillus, such as a strain of Aspergillus fumigatus, such as the Cel7A CBH I disclosed SEQ ID NO: 10 herein (i.e., 100% match of instantly claimed SEQ ID NO: 21) (paragraph [0211]). It would have been obvious to one of ordinary skill in the art to have SEQ ID NO: 2, 21, 23, and 44 in Lee’s method for producing a high protein corn meal from a whole stillage byproduct because Lee teaches a method for producing a high protein corn meal from a whole stillage byproduct, Milos teaches fermenting organisms using enzyme compositions using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content which results in an improvement of the nutrition quality like the protein content of the byproducts (page 3, paragraph [0042]); and Diao teaches the use of cellulolytic enzyme compositions for fermentation wherein the cellulolytic enzyme compositions can comprise GH10 xylanase of SEQ ID NO:16 herein (GENSEQP Accession No. BAK46118) (i.e., 100% match of instantly claimed SEQ ID NO:2), the beta-glucosidase variant of SEQ ID NO: 5 herein (GENSEQP Accession No. AZU67153, with one or more, in particular all, of the following substitutions: F100D, S283G, N456E, F512Y (i.e., 99.5% match of instantly claimed SEQ ID NO:23) (paragraph [0167]), EG I (i.e., endoglucanase I) of SEQ ID NO: 21 herein (Swissprot Accession No. P07981) (i.e., 100% match of instantly claimed SEQ ID NO:44) (paragraph [0168]), and a cellobiohydrolase I (CBH I), such as one derived from a strain of the genus Aspergillus, such as a strain of Aspergillus fumigatus, such as the Cel7A CBH I disclosed SEQ ID NO: 10 herein (i.e., 100% match of instantly claimed SEQ ID NO: 21) (paragraph [0211]). Therefore, the instantly claimed SEQ ID NOs: 2, 21, 23, and 44 taught by Diao are suitable for the purpose of a cellulolytic enzyme composition for fermentation. SEE MPEP 2144.07.
With regards to claims 31, 47, and 63-68 wherein the GH62 a-L-arabinofuranosidase has an amino acid sequence comprising at least 85%, 90%, 95%, and 100% sequence identity to amino acids 17 to 325 of SEQ ID NO: 11, it would have been obvious to one of ordinary skill in the art to have SEQ ID NOs: 2, 21, 23, and 44 in Lee’s method for producing a high protein corn meal from a whole stillage byproduct. Diao teaches that the cellulolytic enzyme composition comprises GH10 xylanase of SEQ ID NO:16 herein (GENSEQP Accession No. BAK46118) (i.e., 100% match of instantly claimed SEQ ID NO:2), the beta-glucosidase variant of SEQ ID NO: 5 herein (GENSEQP Accession No. AZU67153, with one or more, in particular all, of the following substitutions: F100D, S283G, N456E, F512Y (i.e., 99.5% match of instantly claimed SEQ ID NO:23) (paragraph [0167]), EG I (i.e., endoglucanase I) of SEQ ID NO: 21 herein (Swissprot Accession No. P07981) (i.e., 100% match of instantly claimed SEQ ID NO:44) (paragraph [0168]). The artisan of ordinary skill would have been motivated to do so because Peng teaches compositions comprising one or more GH10 or GH11 polypeptides having xylanase activity and one or more GH62 polypeptides having arabinofuranosidase activity (paragraph [0009]), wherein certain arabinofuranosidases from glycoside hydrolase family 62 (herein referred to as GH62) in combination with one or more GH10 or GH11 xylanase are surprisingly good at solubilizing the xylose backbone of sterically hindered arabinoxylan found in plant based material from the sub-family Panicoideae (paragraph [0336]), wherein the composition comprises a GH62 polypeptide having arabinofuranosidase activity having a sequence identity to SEQ ID NO: 27 of at least 99% (i.e., 100% match of instantly claimed SEQ ID NO:11) (paragraph [0398]). The skilled artisan would have had a reasonable expectation of success because Diao teaches the use of GH10 xylanase in an cellulolytic enzyme composition and Peng teaches that the addition of GH62 to GH10 enhances and gives a synergistic effect in its ability to solubilize more xylose (paragraph [0009]).
Claims 38-40 and 54-56 requires the limitation wherein (i) the hemicellulase increase the mass fraction of the high protein feed ingredient compared to the mass of the high protein feed ingredient in the absence of the hemicellulase; and (ii) the beta-glucanase increases the percent protein on a dry basis of the high protein feed ingredient compared to the percent protein on a dry basis of the high protein ingredient in the absence of the beta-glucanase. Milos teaches hemicellulase and beta-glucanase as enzymes used in the method of producing high protein feed ingredient, and that the degradation of the fermenting microorganisms itself by adding the enzyme composition according to the present disclosure, in particular by using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content in the beer mash which results in an improvement of the nutrition quality like the protein content of the byproducts, as well as reduction of NSPs resulting from the fermentative organism cell wall like the yeast cell wall (page 3, paragraph [0042]), but do not explicitly disclose that the hemicellulase increases the mass fraction of the high protein feed ingredient, or the beta-glucanase increase the percent protein on a dry basis of the high protein feed ingredient as claimed. However, such property must necessarily be present. Where, as here, the claimed and prior art products are identical or substantially identical, or are produced by identical or substantially identical processes, the PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of the claimed product. See In re Ludtke, 441 F.2d 660, 169 USPQ 563 (CCPA 1971). Whether the rejection is based on "inherency" under 35 USC 102, on "prima facie obviousness" under 35 USC 103, jointly or alternatively, the burden of proof is the same, and its fairness is evidenced by the PTO's inability to manufacture products or to obtain and compare prior art products. In re Best, Bolton, and Shaw, 195 USPQ 430, 433 (CCPA 1977) citing In re Brown, 59 CCPA 1036, 459 F.2d 531, 173 USPQ 685 (1972).
Claims 36-37 and 52-53 are rejected under 35 U.S.C. 103 as being unpatentable over Lee (US20120064213A1, Published 03/15/2012) in view of Milos et al. (US20130330791A1, Published 12/12/20213; cited in the IDS filed 11/06/2023) further in view of Diao et al. (US20170298394A1, Published 10/19/2017) further in view of Peng et al. (US20170335302A1, Published 11/23/2017) further in view of Argyros et al. (WO2018167669A1, Published 09/20/2018).
Applicant’s Invention
Lee, Milos, Diao, and Peng render obvious all the limitations of instant claim 31. Applicants claims 36-37 and 52-53 further adds the limitation wherein the fermenting organism is a recombinant yeast host cell comprising a heterologous polynucleotide encoding the hemicellulose(s) and/or beta-glucanase(s); and wherein the recombinant host cell further comprises a heterologous polynucleotide encoding a glucoamylase, an alpha-amylase, and/or protease.
Determination of the scope and the content of the prior art
(MPEP §2141.01)
Regarding claims 36-37 and 52-53, Lee teaches in the fermentation step, a common strain of yeast (Saccharomyces cerevisiae) is added to metabolized the glucose sugars into ethanol and CO2 (page 2, paragraph [0024]). Milos teaches the fermenting organism may be a fungal organism such as yeast, wherein the preferred yeasts according to the disclosure are Saccharomyces species, in particular Saccharomyces cerevisiae (page 3, paragraph [0052]).
Ascertainment of the Difference Between Scope the Prior Art and the Claims
(MPEP §2141.02)
Lee, Milos, Diao, and Peng do not teach wherein the fermenting organism is a recombinant yeast host cell comprising a heterologous polynucleotide encoding the hemicellulase(s) and/or beta-glucanase(s), glucoamylase, an alpha-amylase, and/or protease. However, these deficiencies are cured by Argyros et al.
In the analogous art of enzyme activity in the production of food and/or feed, Argyros teaches the recombinant host cell is a yeast and suitable yeast host cells can be from the genus Saccharomyces (page 11, lines 16-18]). Argyros further teaches the recombinant yeast host cells of the present disclosure include an heterologous nucleic acid molecule (i.e., polynucleotide) intended to allow the expression of (e.g., encode) one or more heterologous feed enzymes, wherein the heterologous enzyme can be β-glucanase, xylanase (i.e., hemicellulase), mannanase (i.e., hemicellulase), amylase, and/or protease (page 11, lines 35-37; page 12, lines 15-18).
Finding of Prima Facie Obviousness Rationale and Motivation
(MPEP §2142-2143)
It would have been prima facie obvious to one of ordinary skill in the art at the time of filing to have the fermenting organism be a recombinant yeast host cell comprising a heterologous polynucleotide encoding the hemicellulose, beta-glucanase, glucoamylase, an alpha-amylase, and/or protease in Milos’ method of using enzymes for improving the quality of by-products in the fermentative production process. Milos teaches the fermenting organism may be a fungal organism such as yeast, wherein the preferred yeasts according to the disclosure are Saccharomyces species, in particular Saccharomyces cerevisiae (page 3, paragraph [0052]) and that enzyme compositions using the beta 1,3 glucanase and/or the beta 1,6 glucanase, particularly in combination with a xylanase and/or a mannanase, results in an increase of the nutrition content which results in an improvement of the nutrition quality like the protein content of the byproducts (page 3, paragraph [0042]). One would have understood in view of Argyros that the recombinant host cell is a yeast and suitable yeast host cells can be from the genus Saccharomyces (page 11, lines 16-18]), wherein the recombinant yeast host cells of the present disclosure include an heterologous nucleic acid molecule (i.e., polynucleotide) intended to allow the expression of (e.g., encode) one or more heterologous feed enzymes, wherein the heterologous enzyme can be β-glucanase, xylanase (i.e., hemicellulase), mannanase (i.e., hemicellulase), amylase, and/or protease (page 11, lines 35-37; page 12, lines 15-18). One of ordinary skill would have been motivated to have the fermenting organism as a recombinant yeast host cell comprising a heterologous polynucleotide encoding hemicellulose, beta-glucanase, glucoamylase, an alpha-amylase, and/or protease because they provide a lower cost source of enzyme activity than the purified products that are traditionally used and can also be used in other baked products, fermented foods, non-fermented foods and animal feed (page 9, lines 17-19 and 23-25). The skilled artisan would have had a reasonable expectation of success because Milos teaches that the enzyme compositions used in the methods are capable to degrade the cell wall components of the fermenting organisms (page 3, paragraph [0043]).
Response to Arguments
Applicant’s arguments with respect to 35 U.S.C. 103 obviousness rejection filed 09/08/2025 have been considered but are moot because the arguments are not applicable to any of the rationale underlying the obviousness conclusion. The new grounds of rejection necessitated by amendment have addressed the arguments.
Conclusion
No claims are allowed.
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AFUA BAMFOAA BOATENGExaminer, Art Unit 1617
/ALI SOROUSH/Supervisory Patent Examiner, Art Unit 1614