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 .
Status of the Claims
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1-14
Withdrawn claims: 11 and 14
Previously canceled claims: None
Newly canceled claims: None
Amended claims: 4-6, 8, and 12-13
New claims: None
Claims currently under consideration: 1-10 and 12-13
Currently rejected claims: 1-10 and 12-13
Allowed claims: None
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-10 and 12-13 in the reply filed on 5 December 2025 is acknowledged.
Claims 11 and 14 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 5 December 2025.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Specification
The disclosure is objected to because of the following informalities:
On page 3, lines 21 and 24, “Continues to the first aspect” should read, “Continuing from the first aspect” or “Continuing the first aspect”.
On page 4, lines 11 and 30, and throughout the specification, genus and species names should be italicized to conform with taxonomical naming convention.
On page 4, line 32, it appears that “proteases of (i)” should read, “proteases of (a)”.
On page 6, lines 10, 12, and 14, “(a’)” and “(b’)” do not refer to anything. It appears that “(a’)” and “(b’)” should read, “(a)” and “(b)”.
On page 8, line 7, “enzyme” should read, “enzymes”.
Appropriate correction is required.
Claim Objections
Claims 1-3, 9, and 13 are objected to because of the following informalities:
In claim 1, line 2, “i.e., proteases, , wherein” should read, “i.e., proteases, wherein”.
In claim 1, line 5, “maltase and mixture thereof.” should read, “maltase, and a mixture thereof.”
In claim 2, line 2, “consisting of” should read, “consisting of:”.
In claim 2, line 3, “Norcodiopsis” and Nocardiopsis alba” should be italicized to conform with taxonomical naming convention.
Claim 3 should end with a period as each claim should be a single sentence. See MPEP § 608.01(m), which states, “Each claim begins with a capital letter and ends with a period. Periods may not be used elsewhere in the claims except for abbreviations.”
In claim 9b, “xylanase or mixture thereof” should read, “xylanase, or a mixture thereof”.
In claim 13, line 3, “maltase and mixture thereof.” should read, “maltase, and a mixture thereof.”
Appropriate correction is required.
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.
Claims 1-9 and 12-13 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance:
Claim 1 recites the broad recitation, “wherein the protease is a serine protease”, and the claim also recites, “preferably an acid stable serine protease or a S8 protease”, which is the narrower statement of the range/limitation.
Claim 9(a) recites the broad recitation, “the protease is an acid stable protease”, and the claim also recites, “and more preferably a S8 protease”, which is the narrower statement of the range/limitation.
Claim 12 recites the broad recitation, “wherein the proteases are a serine protease”, and the claim also recites, “preferably an acid stable serine protease, and more preferably a S8 protease”, which is the narrower statement of the range/limitation.
The claims are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Applicant can overcome these rejections by identifying the specific elements regarded by the inventors as being the claimed invention. For purposes of examination, the claims are construed as only requiring the broad recitations.
Claim 2 recites the limitation, “the acid-stable protease” in line 5. In light of the interpretation of claim 1 presented hereinabove, there is insufficient antecedent basis for this limitation in the claim. Applicant can overcome this rejection by amending claim 2 to recite, “wherein the serine protease is an acid-stable protease selected from…”. For purposes of examination, the limitation is construed as suggested for amendment.
Claim 2 recites the limitation, “the proteases of (i)” in line 5. There is insufficient antecedent basis for this limitation in the claim. No element (i) was previously recited in claims 1 or 2. It is unclear what constitutes element (i). For purposes of examination, the limitation is construed to be “the proteases of (a)”, referring to claim 2(a).
Claims 3(c) and 3(d) recite the limitation, “a polypeptide comprising the polypeptide of (a’) or (b’)…”. There is insufficient antecedent basis for this limitation in the claim. No elements (a’) or (b’) were previously recited in claims 1 or 3. It is unclear what constitutes elements (a’) and (b’). For purposes of examination, the limitation is construed to be “a polypeptide comprising the polypeptide of (a) or (b)…”, referring to claim 3(a) and 3(b).
Claim 3(d) recites the limitation, “a N-terminal and/or C-terminal extension of up to 10 amino acids, e.g. 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acids”. The phrase “e.g.” renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d). For purposes of examination, the limitation is construed to be “a N-terminal and/or C-terminal extension of up to 10 amino acids”.
Claim 3(e) recites the limitation, “a fragment of the polypeptide of (a’) or (b’)…”. There is insufficient antecedent basis for this limitation in the claim. No elements (a’) or (b’) were previously recited in claims 1 or 3. It is unclear what constitutes elements (a’) and (b’). For purposes of examination, the limitation is construed to be “a fragment of the polypeptide of (a) or (b)…”, referring to claim 3(a) and 3(b).
Claim 4 recites the limitation, “a N-terminal and/or C-terminal extension of up to 10 amino acids, e.g. 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acids”. The phrase “e.g.” renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d). For purposes of examination, the limitation is construed to be “a N-terminal and/or C-terminal extension of up to 10 amino acids”.
In claims 4 and 5, the phrase “for example” renders the claims indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d). For purposes of examination, claim 4 is construed as, “The method of claim 1, wherein the protease is provided in a dosage of between 1,000 units/kg animal feed and 1,000,000 units/kg animal feed.” Claim 5 is construed as, “The method of claim 1, wherein the carbohydrase is provided in a dosage of between 10 units/kg animal feed and 5,000 units/kg animal feed.”
In claims 6 and 7, the phrase “such as” renders the claims indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d). For purposes of examination, claim 6 is construed as, “The method of claim 1, wherein the animal feed contains carbohydrates selected from the group consisting of arabinoxylan, starch and/or non-starch polysaccharide (NSP).” Claim 7 is construed as, “The method of claim 6, wherein the carbohydrate is in forms of concentrates and/or roughages.”
Claims 2-8 are also rejected due to their dependency from claim 1.
Claim InterpretationIndependent claims 1 and 9 recite, “A method for boosting the activity of a carbohydrase in an animal feed” in the preamble. Independent claim 10 recites, “A method for improving hydrolyzation of a carbohydrate in an animal feed” in the preamble. The preamble limitations are not necessary to breathe life into the claims because the effect recited necessarily flows from performing the positively recited method steps in the claims. Therefore, there is no manipulative difference between adding the claimed serine protease and carbohydrase with the intention of boosting carbohydrase activity or improving hydrolyzation of a carbohydrate in an animal feed, as recited in the instant claims, and prior art disclosing adding serine protease and carbohydrase to animal feed for any other purpose. See MPEP § 2111.02 and Id. (II).
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 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.
Claims 1, 4, 10, and 12-13 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by De Beer et al. (US 2016/0158326 A1, cited on the IDS filed on 17 August 2023).
Regarding claim 1, De Beer teaches a method for increasing the availability of at least one dietary nutrient and/or increasing the metabolizable energy from an animal feed comprising adding to the animal feed a feed supplement comprising a mixture of enzymes having enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (i.e., carbohydrases and proteases) (see claim 33 with reference to claims 17 and 21). De Beer teaches that preferred proteases are acid-stable serine proteases ([0114]).
MPEP 2131.02(III) states, “A reference disclosure can anticipate a claim when the reference describes the limitations but "'d[oes] not expressly spell out' the limitations as arranged or combined as in the claim, if a person of skill in the art, reading the reference, would ‘at once envisage' the claimed arrangement or combination.” Kennametal, Inc. v. Ingersoll Cutting Tool Co., 780 F.3d 1376, 1381, 114 USPQ2d 1250, 1254 (Fed. Cir. 2015) (quoting In re Petering, 301 F.2d 676, 681(CCPA 1962)).” Given De Beer' s teachings that the feed supplement comprises a mixture of enzymes having enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (i.e., carbohydrases and proteases) (see claim 33 with reference to claims 17 and 21), and that preferred proteases are acid-stable serine proteases ([0114]), De Beer clearly envisaged, and a person of skill in the art would at once envisage, the claimed combination of a carbohydrase, selected from the group consisting of glucanase, amylase, xylanase and a mixture thereof, and a serine protease. As such, De Beer teaches adding carbohydrases and an acid stable serine protease to an animal feed.
As discussed above, the effect of boosting the activity of a carbohydrase in an animal feed necessarily flows from performing the positively recited method steps. Therefore, De Beer teaches a method for boosting the activity of a carbohydrase in an animal feed comprising adding to the animal feed one or more proteolytic enzymes, i.e., proteases, wherein the protease is a serine protease, and wherein the carbohydrase is selected from the group consisting of hemicellulase, pectinase, glucanase, amylase, xylanase, maltase, and a mixture thereof.
Claim 1 is therefore anticipated by De Beer.
Regarding claim 4, De Beer teaches that the protease is provided in a dosage of between 1,000 units/kg animal feed and 1,000,000 units/kg animal feed – De Beer teaches, “…the protease is administered in one of the following amounts (dosage ranges): 10,000 units/kg feed, 11,000, 12,000, 13,000, 14,000, 15,000, 16,000, 17,000, 18,000, 19,000, 20,000 units/kg feed.” ([0122]).
Claim 4 is therefore anticipated by De Beer.
Regarding claim 10, De Beer teaches a method for increasing the availability of at least one dietary nutrient and/or increasing the metabolizable energy from an animal feed comprising adding to the animal feed a feed supplement comprising a mixture of enzymes having enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (i.e., carbohydrases and proteases) (see claim 33 with reference to claims 17 and 21). As such, De Beer teaches adding carbohydrases and a protease to an animal feed.
As discussed above, the effect improving hydrolyzation of a carbohydrase in an animal feed necessarily flows from performing the positively recited method steps. Therefore, De Beer teaches a method for improving hydrolyzation of a carbohydrate in an animal feed comprising adding to the animal feed one or more proteolytic enzymes, i.e., proteases, and a carbohydrase.
Claim 10 is therefore anticipated by De Beer.
Regarding claim 12, De Beer teaches that the proteases are a serine protease – De Beer teaches that preferred proteases are acid-stable serine proteases ([0114]).
MPEP 2131.02(III) states, “A reference disclosure can anticipate a claim when the reference describes the limitations but "'d[oes] not expressly spell out' the limitations as arranged or combined as in the claim, if a person of skill in the art, reading the reference, would ‘at once envisage' the claimed arrangement or combination.” Kennametal, Inc. v. Ingersoll Cutting Tool Co., 780 F.3d 1376, 1381, 114 USPQ2d 1250, 1254 (Fed. Cir. 2015) (quoting In re Petering, 301 F.2d 676, 681(CCPA 1962)).” Given De Beer' s teachings that the feed supplement comprises a mixture of enzymes having enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (i.e., carbohydrases and proteases) (see claim 33 with reference to claims 17 and 21), and that preferred proteases are acid-stable serine proteases ([0114]), De Beer clearly envisaged, and a person of skill in the art would at once envisage, the claimed combination of a carbohydrase, selected from the group consisting of glucanase, amylase, xylanase and a mixture thereof, and a serine protease. As such, De Beer teaches adding carbohydrases and an acid stable serine protease to an animal feed.
Claim 12 is therefore anticipated by De Beer.
Regarding claim 13, De Beer teaches that the carbohydrase is selected from the group consisting of hemicellulase, pectinase, glucanase, amylase, xylanase, maltase, and a mixture thereof – De Beer teaches that the mixture of enzymes has enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (see claim 33 with reference to claims 17 and 21). It is noted that De Beer further discloses that pectinases may be included in the enzyme mixture ([0090]).
Claim 13 is therefore anticipated by De Beer.
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 2 and 5-9 are rejected under 35 U.S.C. 103 as being unpatentable over De Beer et al. (US 2016/0158326 A1, cited on the IDS filed on 17 August 2023).
Regarding claim 2, De Beer teaches the method of claim 1.
De Beer also teaches that the acid-stable protease is selected from the group consisting of:
a. proteases derived from Nocardiopsis sp. NRRL 18262, and Nocardiopsis alba – ([0118]; see also [0114], “N. prasinia (previously alba)”).
b. proteases of at least 60, 65, 70, 75, 80, 85, 90, or at least 95% amino acid identity to any of the proteases of (a) – ([0118]).
Although De Beer does not provide a specific arrangement of all elements of the claim, the claimed acid-stable serine proteases are disclosed as being suitable for use in the disclosed feed supplement ([0114]). MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”. Therefore, the claimed proteases represent obvious choices for inclusion in the feed supplement of De Beer.
Claim 2 is therefore rendered obvious.
Regarding claim 5, De Beer teaches that the carbohydrase is provided in a dosage of between 10 units/kg animal feed and 5,000 units/kg animal feed – In Table 1, De Beer discloses the composition of feed supplements for corn-soybean meal type of diets ([0064]). The diets comprise Fungal Glucanase 1, Xylanase, and Fungal Glucanase 2 that read on the carbohydrases of claim 1. These enzymes are provided in amounts ranging from 1.25 to 5.0 Units/kg feed of Fungal Glucanase 1, 135 to 674 units/kg feed of Xylanase, and 40 to 200 units/kg feed of Fungal Glucanase 2. Upon summation of these data, De Beer discloses that the carbohydrase is provided in a dosage of between 176.25 to 879 units/kg of feed. The disclosed range lies inside the claimed range.
Although De Beer does not provide a specific arrangement of all elements of the claim, (i.e., De Beer is not explicit that the protease from Bacillus licheniformis is a serine protease) the disclosed range of carbohydrases represents an obvious choice for the amount of carbohydrase to include in the feed supplement of De Beer.
Claim 5 is therefore rendered obvious.
Regarding claim 6, De Beer teaches that the animal feed contains carbohydrates selected from the group consisting of arabinoxylan, starch and/or non-starch polysaccharide (NSP) – De Beer discloses that corn-soybean meal feed contains roughly 10-15% or more NSPs ([0039]), and that, in one embodiment, the animal diet is a corn-soybean meal feed ([0053]). De Beer teaches, “[t]he types and amount of NSPs change from starter diet to finisher diet. For example, in one type of corn-soybean meal, corn content increase results in a 22% increase of arabinoxylans and starch content in the finisher diet” ([0008]). Thus, De Beer teaches that corn comprises arabinoxylans and starch. The disclosed corn-soybean meal feed therefore also comprises arabinoxylan and starch.
Although De Beer does not provide a specific arrangement of all elements of the claim, the claimed carbohydrates are disclosed as being suitable for use as part of the animal feed to which the feed supplement is added. MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”. Therefore, the claimed carbohydrates represent obvious choices for inclusion in the animal feed of De Beer.
Claim 6 is therefore rendered obvious.
Regarding claim 7, De Beer teaches that the carbohydrate is in forms of concentrates and/or roughages – “The animal diet can be an animal feed which includes sources of protein and carbohydrates. Examples of sources of protein and carbohydrates include corn, soya, wheat, barley, and rye. Corn-soybean, wheat-soybean, and wheat-corn-soybean, sorghum-soybean, and corn-sorghum-soybean represent other non-limiting examples of suitable animal feeds according to the present invention.” ([0051]). As provided by the instant specification, concentrates include “sorghum, seeds and grains (either whole or prepared by crushing, milling, etc. from e.g. corn, oats, rye, barley, wheat)” (p. 2, lines 26-31).
Although De Beer does not provide a specific arrangement of all elements of the claim, the claimed carbohydrates are disclosed as being suitable for use as part of the animal feed to which the feed supplement is added. MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”. Therefore, the claimed carbohydrates represent obvious choices for inclusion in the animal feed of De Beer.
Claim 7 is therefore rendered obvious.
Regarding claim 8, De Beer teaches that the animal feed is an animal diet based on soy-bean meal, corn and/or wheat – “In some embodiments, the diets are a wheat diet. In certain embodiments, the diets are a corn-soybean meal diet.” ([0016]).
Although De Beer does not provide a specific arrangement of all elements of the claim, the claimed carbohydrates are disclosed as being suitable for use as part of the animal feed to which the feed supplement is added. MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”. Therefore, the claimed carbohydrates represent obvious choices for inclusion in the animal feed of De Beer.
Claim 8 is therefore rendered obvious.
Regarding claim 9, De Beer teaches a method for increasing the availability of at least one dietary nutrient and/or increasing the metabolizable energy from an animal feed comprising adding to the animal feed a feed supplement comprising a mixture of enzymes having enzyme activities selected from the group including glucanase, xylanase, cellulase, protease, and phytase activities, and at least one further enzyme selected from the group consisting of amylases, arabinases, galactosidase, and debranching enzymes (i.e., carbohydrases and proteases) (see claim 33 with reference to claims 17 and 21). De Beer further discloses that pectinases may be included in the enzyme mixture ([0090]). De Beer teaches that preferred proteases are acid-stable serine proteases ([0114]). As such, De Beer teaches adding carbohydrases and an acid stable serine protease to an animal feed.
As discussed above, the effect of boosting the activity of a carbohydrase in an animal feed necessarily flows from performing the positively recited method steps. Therefore, De Beer teaches a method for boosting the activity of a carbohydrase in an animal feed comprising adding to the animal feed one or more proteolytic enzymes, i.e., proteases, wherein:
a) the protease is a serine protease ([0114]) in a dosage of between 10,000 units/kg feed and 30,000 units/kg feed – “…the protease is administered in one of the following amounts (dosage ranges): 10,000 units/kg feed, 11,000, 12,000, 13,000, 14,000, 15,000, 16,000, 17,000, 18,000, 19,000, 20,000 units/kg feed.” ([0122]).
b) the carbohydrase is pectinase, amylase, xylanase, or a mixture thereof – as described above (see claim 33 with reference to claims 17 and 21; see also [0090]).
c) the animal feed is an animal diet based on soybean meal, corn and/or wheat – “In some embodiments, the diets are a wheat diet. In certain embodiments, the diets are a corn-soybean meal diet.” ([0016]).
Although De Beer does not provide a specific arrangement of all elements of the claim, the claimed serine protease and soybean meal, corn and/or wheat are disclosed as being suitable for use as part of the feed supplement and the feed to which the supplement is added. MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”. Therefore, the claimed serine protease and soybean meal, corn and/or wheat represent obvious choices for inclusion in the animal feed of De Beer.
It is noted that “d)” is optional, and therefore not required. It is further noted that the effect of increasing the carbohydrase activity by 5% or more is the result of performing the method steps. De Beer discloses the claimed steps and elements to produce the animal feed. When the method steps recited in the prior art reference are substantially identical to those of the claims, claimed properties of the resulting composition are presumed to be present in the composition of the prior art. The burden of proof shifts to the applicant to provide objective evidence (i.e., test data) to the contrary. See In re Best, 562, F.2d 1252, 1254, 195 USPQ 403, 433 (CCPA 1977). MPEP § 2112.02(I).
Claim 9 is therefore rendered obvious.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over De Beer et al. (US 2016/0158326 A1, cited on the IDS filed on 17 August 2023) as applied to claim 1 above, and further in view of Haahr et al. (US 2020/0229463 A1, cited on the IDS filed on 17 August 2023, matching WO 2019/043191 A1 published on 7 March 2019).
Regarding claim 3, De Beer teaches the method of claim 1.
De Beer does not discuss that the protease is defined by polypeptides having S8 protease activity selected from the list consisting of:
a. a polypeptide having a sequence identity of at least 70% to any one of SEQ ID NOs 3-6;
b. a variant of any one of SEQ ID NOs: 3-6, wherein the variant has protease activity and comprises one or more substitutions, and/or one or more deletions, and/or one or more insertions or any combination thereof in positions 1-50;
c. a polypeptide comprising the polypeptide of (a) or (b) and a N-terminal and/or C- terminal His-tag and/or HQ-tag;
d. a polypeptide comprising the polypeptide of (a) or (b) and a N-terminal and/or C- terminal extension of up to 10 amino acids; and
e. a fragment of the polypeptide of (a) or (b) having protease activity and having at least 90% of the length of the mature polypeptide.
However, Haahr teaches that when a protein source such as soybean meal is included in the feed of mono-gastric animals such as pigs and poultry, a significant proportion of the soybean meal is not digested efficiently, and by improving the digestibility of protein, the animal can uptake more of the protein thereby improving performance, such as increased body weight gain ([0004]). Haahr teaches that proteases which are highly acid stable are especially desirable in improving the digestibility of protein ([0005]). Haahr teaches a method for improving the nutritional value of animal feed (i.e., improving the availability of nutrients in the feed) ([0438]), comprising adding an animal feed additive to the feed ([0439]). The animal feed additive comprises an S8 protease ([0007]) and one or more additional enzymes selected from a group comprising carbohydrases including amylase, alpha-amylase, beta-amylase, beta-glucanase, xylanase, and other carbohydrases ([0132]; [0502]).
Haahr provides polypeptide SEQ ID NOs: 1-9. SEQ ID NO: 1 of Haahr has 95.3% identity with SEQ ID NO: 3 of the instant application (see alignment below). SEQ ID NO: 4 of Haahr is the conserved motif TGXK[V/T][I/V]X[N/S]MSLG ([0033]). This corresponds to SEQ ID NO: 6 of the instant application, which is the motif TGXKV[I/V]XXMSLG.
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As related to the elements of the instant claim 3, where SEQ ID NO: 1 of Haahr has 95.3% identity with SEQ ID NO: 3 of the instant application, and SEQ ID NO: 4 of Haahr matches SEQ ID NO: 6 of the instant application, Haahr teaches that protease is defined by polypeptides having S8 protease activity selected from the list consisting of:
a. a polypeptide having a sequence identity of at least 70% to any one of SEQ ID NOs 3-6 – see Haahr [0008] and [0011].
b. a variant of any one of SEQ ID NOs: 3-6, wherein the variant has protease activity and comprises one or more substitutions, and/or one or more deletions, and/or one or more insertions or any combination thereof in positions 1-50 – see Haahr [0017].
c. a polypeptide comprising the polypeptide of (a) or (b) and a N-terminal and/or C- terminal His-tag and/or HQ-tag – see Haahr [0025].
d. a polypeptide comprising the polypeptide of (a) or (b) and a N-terminal and/or C- terminal extension of up to 10 amino acids – see Haahr [0026].
e. a fragment of the polypeptide of (a) or (b) having protease activity and having at least 90% of the length of the mature polypeptide – see Haahr [0027].
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to substitute the serine protease of De Beer with the S8 protease of Haar by simple substitution of one known element for another to obtain predictable results. First, De Beer teaches a method for increasing the availability of at least one dietary nutrient and/or increasing the metabolizable energy from an animal feed comprising adding to the animal feed a feed supplement comprising a mixture of carbohydrases and an acid stable protease (see claim 33 with reference to claims 17 and 21, and [0114]). Haahr teaches a method for improving the nutritional value of animal feed (i.e., improving the availability of nutrients in the feed) ([0438]), comprising adding an animal feed additive to the feed ([0439]). The animal feed additive comprises an S8 protease ([0007]) and one or more additional enzymes, including carbohydrases ([0132]; [0502]). Since both De Beer and Haahr teach similar methods using similar enzymes, one of ordinary skill in the art could have substituted one protease for the other and would have expected an increase in availability of nutrients in the feed. See MPEP § 2143(I)(B).
Claim 3 is therefore rendered obvious.
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.
Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claim 5 of U.S. Patent No. 9,279,114.
Although the claims at issue are not identical, they are not patentably distinct from each other because claim 5 of the ‘114 patent teaches a method for improving the nutritional value of an animal feed, comprising adding at least one protease to the feed wherein the protease has a sequence identity of at least 90% to the sequence of amino acids 1-192 of SEQ ID NO: 2, that has protease activity, the method further comprising adding amylase, beta-glucanase, and/or xylanase to the feed. Residues 1-192 of SEQ ID NO: 8 of the ‘114 patent share 84% identity with SEQ ID NO: 1 of the instant claim 2. See alignment below:
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Independent claim 1 recites, “A method for boosting the activity of a carbohydrase in an animal feed” in the preamble. Independent claim 10 recites, “A method for improving hydrolyzation of a carbohydrate in an animal feed” in the preamble. The preamble limitations are not necessary to breathe life into the claims because the effect recited necessarily flows from performing the positively recited method steps in the claims. Therefore, there is no manipulative difference between adding the claimed serine protease and carbohydrase with the intention of boosting carbohydrase activity or improving hydrolyzation of a carbohydrate in an animal feed, as recited in the instant claims, and prior art disclosing adding serine protease and carbohydrase to animal feed for any other purpose. See MPEP § 2111.02 and Id. (II).
Therefore, the limitations of claim 5 of the ‘114 patent read on instant claims 1-2, 10, and 12-13.
Claims 1-2, 10, and 12-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 6 of U.S. Patent No. 9,279,115.
Although the claims at issue are not identical, they are not patentably distinct from each other because claim 6 of the ‘115 patent teaches a method for improving the nutritional value of an animal feed, comprising adding at least one protease to the feed wherein the protease has a sequence identity of at least 90% to the sequence of amino acids 1-192 of SEQ ID NO: 2, that has protease activity, the method further comprising adding amylase, beta-glucanase, and/or xylanase to the feed. SEQ ID NO: 2 of the ‘115 patent shares 69% identity with SEQ ID NO: 1 of the instant claim 2. See alignment below:
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Independent claim 1 recites, “A method for boosting the activity of a carbohydrase in an animal feed” in the preamble. Independent claim 10 recites, “A method for improving hydrolyzation of a carbohydrate in an animal feed” in the preamble. The preamble limitations are not necessary to breathe life into the claims because the effect recited necessarily flows from performing the positively recited method steps in the claims. Therefore, there is no manipulative difference between adding the claimed serine protease and carbohydrase with the intention of boosting carbohydrase activity or improving hydrolyzation of a carbohydrate in an animal feed, as recited in the instant claims, and prior art disclosing adding serine protease and carbohydrase to animal feed for any other purpose. See MPEP § 2111.02 and Id. (II).
Therefore, the limitations of claim 6 of the ‘115 patent read on instant claims 1-2, 10, and 12-13.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to James Shellhammer whose telephone number is (703) 756-5525. The examiner can normally be reached Monday - Thursday 7:30 am - 5:00 pm ET.
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/JAMES P. SHELLHAMMER/Examiner, Art Unit 1793
/EMILY M LE/Supervisory Patent Examiner, Art Unit 1793