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
Claims 3, 6-13, 20-22, 25-26 and 32-34 are pending.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. §119(e) or under 35 U.S.C. §120, §121, or §365(c) is acknowledged. As previously noted in the Non-Final Office Action mailed on 14 October 2025, this application is a 371 of PCT/EP2021/077792, filed 10/07/2021, and claims foreign priority to EP20200517.9, 10/07/2020.
Applicant has complied with all of the conditions for receiving the benefit of an earlier filing date under 35 U.S.C. §120 or §365(c).
Claims 3, 6-13, 20-22, 25-26 and 32-34 have the effective filing date of 07 October 2020.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 07 February 2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the Examiner.
Specification
The objection to the specification in the Non-Final Office Action mailed on 14 October 2025, as failing to comply with a requirement for patent applications containing sequence disclosures, is maintained because Applicant submitted a proper incorporation by reference paragraph as an amendment to the specification.
Applicant must provide substitute specifications, as marked up and clean copies, as well as a 'no new matter' statement (see below, last paragraph).
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing or incomplete. See item 1) a) or 1) b) above.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
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 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.
Claim Rejections - 35 U.S.C. § 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 of this title, 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.
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 3, 6-13, 20, 25-26 and 32 are rejected under 35 U.S.C. §103 as being unpatentable over Becker et al. (WO 2016/149636 A1) in view of Muzykantov et al. (US 2006/0127386 A1) and Labhasetwar et al. (WO 2014/124142 A2).
"Granule, granulate, co-granule, co-granulate is intended to mean a composition in solid form, such as in layered form or a core comprising the enzymes of the invention and filler allowing for the formation of the solid unit" (originally-filed specification, pg. 4, lines 30-33).
Prior art which describes catalase and/or superoxide dismutase (SOD) in a functional context will be considered as a polypeptide having either catalase activity or SOD activity whether or not the prior art uses the term 'polypeptide'.
Regarding claim 3, pertaining to a granule comprising enzymes,
Becker et al. shows stable, durable granules with active agents, as the described invention (pg. 1, para. [002]). In some embodiments, the active agent is one or more enzymes (pg. 4, cont. para. [0010], entry# 7).
Further regarding claim 3, pertaining to the granule is a coated granule comprising a core and a coating layer surrounding the core,
Becker et al. shows a process for producing a granule which comprises preparing stable granules having a core, at least one active agent, a moisture hydrating layer, and at least one moisture coating (pg. 5, cont. para. [0010], entry# 24). The protective coatings of the described invention generally are applied as one or more layers surrounding the core (pg. 21, para. [0074]).
Claim 3, as amended, recites product-by-process language. MPEP 2113 states: “Even though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). Prior art which shows the process of 'steam pelleting' will be indicated at the discretion of the Examiner.
Becker et al. further shows phytase granules which were prepared according to a formulation having a PVA (polyvinyl alcohol) coating and/or an inorganic salt layer coating (pg. 51, para. [00129]). The residual phytase activity following granulation (compared to the nongranulated enzyme) for each sample is shown in Figure 1. Granules prepared with the additional drying step (i.e., AxtraPHY 383, AxtraPHY 110, and AxtraPHY 112) all retained greater than 70% activity (pg. 53, para. [00132]). Figure 1 is a bar graph showing post-steaming-test residual phytase activity in granules prepared using different processing conditions (pg. 7, para. [0012]; and Fig. 1). It is noted that phytase is an enzyme.
Becker et al. does not show: a polypeptide having superoxide dismutase
activity and a polypeptide having catalase activity [Claim 3]; and the molar ratio of the polypeptide having superoxide dismutase activity to the polypeptide having catalase activity is greater than 5:1 [Claim 3].
Muzykantov et al. shows a method for producing a polymeric nanocarrier-encapsulated protein composition (pg. 1, para. [0009]). Polymeric nanocarrier-encapsulated protein compositions are also encompassed by the described invention (pg. 1, para. [0010] [nexus to Becker et al.- a granule with a protein in a core surrounded by a coating]).
Regarding claim 3, pertaining to a polypeptide having superoxide dismutase
activity and a polypeptide having catalase activity,
Muzykantov et al. shows that, in one embodiment, the polymeric nanocarrier-encapsulated protein is an antioxidant enzyme which is capable of reducing oxidative damage by decomposing or degrading reactive oxygen species. Antioxidant enzymes particularly useful include, minimally catalase, and superoxide dismutase (pg. 2, para. [0014]). An experiment was performed to demonstrate that catalase, residing inside the nanocarrier, could degrade H2O2 (pg. 5, para. [0032]). The activity of loaded catalase was determined by the direct monitoring A242 nm absorbance of H2O2 (pg. 8, para. [0046]).
Labhasetwar et al. shows compositions comprising superoxide dismutase (SOD) and catalase encapsulated in one or more nanoparticles, as one aspect of the described invention (pg. 2, para. [0008] [nexus to Becker et al.- a granule with enzymes in a core surrounded by a coating; nexus to Muzykantov et al.- nanocarrier encapsulated SOD and catalase]).
Regarding claim 3, pertaining to the molar ratio of the polypeptide having superoxide dismutase activity to the polypeptide having catalase activity is greater than 5:1, Labhasetwar et al. shows that in one aspect, the SOD and catalase are encapsulated in the same nanoparticle (NP), that is, each of the nanoparticles (NPs) comprise the SOD and the catalase (pg. 2, para. [0008]). In one aspect, each of the one or more nanoparticles comprising SOD is loaded with about 10μg to about 150μg SOD. In other aspects, each of the one or more NPs are loaded with about 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, or 200μg SOD. In another aspect, each of the one or more nanoparticles comprising catalase is loaded with about 10μg to about 150µg catalase. In other aspects, each of the one or more NPs are loaded with about 10, 20, 30, 40, 50, 60, 70, 80, 90,100,110,120,130,140, 150, 160, 170, 180, 190, or 200μg catalase (pg. 11, para. [0041] thru pg. 12, cont. para. [0041]). Each of the nanoparticles can comprise SOD and catalase (each nanoparticle can comprise both SOD and catalase) (pg. 12, para. [0043]). Activity of the catalase was measured using a catalase assay kit (pg. 19, para. [0077]).
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have modified the granule comprising enzymes, wherein the granule is coated and comprises a core and a coating layer surrounding the core, as shown by Becker et al., by incorporating a polypeptide having superoxide dismutase (SOD) activity and a polypeptide having catalase activity [Claim 3], as shown by Muzykantov et al. and Labhasetwar et al., with a reasonable expectation of success, because Muzykantov et al. shows a composition which is akin to the granule shown by Becker et al., in that it is a (nano)particle that contains enzymes (specifically, SOD and catalase) within it (e.g., as a core) which is, in turn, surrounded by a polymeric coating (MPEP 2143 (I)(G)). Becker et al. teaches that the described granule can comprise enzymes (MPEP 2143 (I)(A)).
It would have been further obvious to have formulated each granule to comprise a molar ratio of SOD activity to catalase activity that is greater than 5:1 [Claim 3], with a reasonable expectation of success, because Labhasetwar et al. shows that SOD and catalase can be contained within the described nanoparticles in varying amounts, such that one of ordinary skill in the art could select the amount of each enzyme that would result in a desired ratio of >5:1 (MPEP 2143 (I)(G)), by way of optimizing the granule according to its application.
One of ordinary skill in the art would have been motivated to have made those modifications, because Becker et al. teaches that enzymes are known to improve the digestibility of feed, reduce anti-nutritional factors in feed, and improve animal productivity (pg. 1, para. [003]). A problem exists in the industry to provide protective formulations to make the active agents suitable for storage in unpelleted animal feed mixtures (Becker et al., pg. 1, para. [004]). Muzykantov et al. teaches that there is a need in the art for a delivery system for targeting active therapeutic enzymes and other therapeutic proteins to cells which provides protection of the proteins from subsequent cellular degradation (pg. 1, para. [0008]). In addition, oxidative stress induced by reactive oxygen species (ROS) including H2O2 produced by leukocytes and vascular cells plays a key role in pathogenesis of many disease conditions. Small antioxidants and scavengers can attenuate oxidative stress (Muzykantov et al., pg. 1, para. [0003]-[0004]). That is, combining two antioxidants into one granule would have increased the therapeutic and industrial value of said granule.
Regarding claim 6, Becker et al. shows that, in one aspect, the enzyme is distributed throughout the core material (pg. 6, cont. para. [0010], entry# 32).
Regarding claims 7 and 8, the durable granules of the described invention include between about 0.0005 to about 20% on a dry weight basis of the enzyme component of the granule (pg. 11, para. [0034]).
Regarding claim 9, the durable granules of the present invention may be sized as desired and are between about 300µm to about 1000µm in diameter (pg. 12, para. [0038]).
Regarding claim 10, suitable fillers useful in the cores include inert materials (pg. 19, para. [0067]).
Regarding claim 11, pertaining to salts, Becker et al. shows that examples of fillers include, but are not limited to, water soluble agents such as, minimally, salts (pg. 20, cont. para. [0067]).
Regarding claim 12, pertaining to (NH4)2SO4, Becker et al. shows that particles composed of inorganic salts and/or sugars and/or small organic molecules may be used as the cores of the described invention. Suitable water soluble ingredients for incorporation into cores include inorganic salts such as, minimally, ammonium sulfate (pg. 19, para. [0064]).
Regarding claim 13, pertaining to microcrystalline wax, Becker et al. shows that simple, compound and derived lipids that may be used in the protective coatings are waxes, for example, minimally, microcrystalline waxes (pg. 22, para. [0081]).
Regarding claim 20, a 'stable' granule refers to a granule in which the activity of the active agent(s) is substantially maintained after inclusion as an ingredient in a formulation subjected to, minimally, steam heated pretreatment processes or steam heated pelleting processes. Stability includes, minimally, thermostability. Thermostability is defined further and, generally, refers to maintenance of activity following exposure to temperatures up to about 85°C to 95°C when the stable, durable granules are an ingredient of pellets, tablets and unpelleted and untableted mixtures (pg. 15, para. [0047]). 'Humid processing air' refers to air used to fluidize, dry, sieve, or otherwise process granules, which air has a high absolute humidity (pg. 18, para. [0059]).
Regarding claims 25, 26 and 32, the use of active agents, such as enzymes, in animal feed is common (pg. 1, para. [003]). The granule for delivering an active agent is an ingredient in a feed base mix or feed premix (pg. 3, para. [0010], entry# 1).
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Claims 21 and 33 are rejected under 35 U.S.C. §103 as being unpatentable over Becker et al. in view of Muzykantov et al., and Labhasetwar et al., as applied to claims 3, 6-13, 20, 25-26 and 32 above, and further in view of Li et al. (WO 2020/200322 A1; Intl. Filing Date: 05 April 2020).
Becker et al. in view of Muzykantov et al. and Labhasetwar et al. do not show: the polypeptide having superoxide dismutase activity is selected from a group which includes SEQ ID NO.: 2 [Claim 21]; and an animal feed composition comprising the granule of claim 21 [Claim 33].
Regarding claims 21 and 33, pertaining to SEQ ID NO.: 2, Li et al. teaches an animal feed additive comprising a polypeptide of fungal origin having catalase activity and optionally a polypeptide having superoxide dismutase activity (pg. 1, lines 27-28). For a solid formulation, the formulation may be for example as a granule (pg. 164, lines 13-14). SEQ ID NO.: 44 is the amino acid sequence of a mature polypeptide having superoxide dismutase (SOD) activity available from Aspergillus japonicus (pg. 26, lines 1-2). SEQ ID NO.: 44 is 100% identical to instant SEQ ID NO.: 2. See sequence alignment in the appendix. It is noted that the instant specification describes the instant SEQ ID NO.: 2 as "the amino acid sequence of a mature polypeptide having superoxide dismutase activity from Aspergillus japonicus comprising 162 amino acid residues" (originally-filed specification, pg. 3, lines 15-16).
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have modified the granule comprising a polypeptide having superoxide dismutase activity and a polypeptide having catalase activity, wherein the granule is coated and comprises a core and a coating layer surrounding the core, as shown by Becker et al. in view of Muzykantov et al., and Labhasetwar et al., as applied to claims 3, 6-13, 20, 25-26 and 32 above, by including a polypeptide with the amino acid sequence of SEQ ID NO.: 2 which has superoxide dismutase activity [Claim 21]; and incorporating the polypeptide into an animal feed composition [Claim 33], as taught by Li et al., with a reasonable expectation of success, because Li et al. teaches a solid animal feed composition comprising polypeptides having catalase and superoxide dismutase (SOD) activity, the solid composition being in the form of a granule, which is the granule shown by Becker et al. in view of Muzykantov et al. (MPEP 2143 (I)(G)).
One of ordinary skill in the art would have been motivated to have made those modifications, because Li et al. shows that the SOD polypeptides of the described invention have advantageously high gastric stability. Moreover, some SODs even have higher activity under gastric stability studies than at the reference pH, indicating that they are more active at low pH. This makes fungal SODs very well suited for use in vivo by means of administration through animal feed (pg. 128, lines 11-12; and lines 24-28). Therefore, including said enzyme polypeptides into a granule and/or an animal feed composition would improve the therapeutic activity of the polypeptides via their improved gastric stability. Li et al. teaches that the described compositions would improve or enhance the immune response and/or reduce inflammation and/or modulate gut flora (pg. 19, lines 14-17).
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Claims 22 and 34 are rejected under 35 U.S.C. §103 as being unpatentable over Becker et al. in view of Muzykantov et al., and Labhasetwar et al., as applied to claims 3, 6-13, 20, 25-26 and 32 above, and further in view of Liu et al. (US 2016/0298154 A1) as evidenced by NCBI global align (SEQ ID NO: 6 vs SEQ ID NO.: 90, Datasheet [online], Downloaded on 02 Sept. 2025, pp. 1-4).
Becker et al. in view of Muzykantov et al., and Labhasetwar et al. do not show: the polypeptide having catalase activity is selected from a group which includes SEQ ID NO: 6 [Claim 22]; and an animal feed composition comprising the granule of claim 22 [Claim 34].
Liu et al. teaches processes for degrading a cellulosic material, comprising: treating the cellulosic material with an enzyme composition in the presence of a combination of an AA9 polypeptide and one or more oxidoreductases selected from the group consisting of a catalase, a laccase, and a peroxidase (pg. 1, para. [0009]). The described invention also relates to enzyme compositions comprising a combination of an AA9 polypeptide and one or more oxidoreductases selected from the group consisting of a catalase, a laccase, and a peroxidase (pg. 1, para. [0015] [nexus to Becker et al. in view of Muzykantov et al- composition comprising catalase]).
Regarding claim 22, pertaining to SEQ ID NO.: 6, Liu et al. teaches examples of useful catalases include, but are not limited to, catalases from, minimally, Thermoascus aurantiacus (WO 2012/130120) (pg. 20, para. [0256]). Thermoascus aurantiacus catalase (SEQ ID NO: 90) was prepared according to WO 2012/130120 (pg. 24, para. [0326]). NCBI global align shows that SEQ ID NO.: 90, as taught by Liu et al., is 100% identical to instant SEQ ID NO.: 6. It is noted that the instant specification describes the instant SEQ ID NO.: 6 as "the amino acid sequence of a mature polypeptide having catalase activity from Thermoascus aurantiacus comprising 740 amino acid residues" (originally-filed specification, pg. 3, lines 23-24).
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have modified the granule comprising a polypeptide having superoxide dismutase activity and a polypeptide having catalase activity, wherein the granule is coated and comprises a core and a coating layer surrounding the core, as shown by Becker et al. in view of Muzykantov et al., and Labhasetwar et al., as applied to claims 3, 6-15, 20, 25 and 26 above, by including any polypeptide having catalase activity including a catalase with the amino acid sequence of SEQ ID NO.: 6 [Claim 22], with a reasonable expectation of success, because Liu et al. as evidenced by NCBI global align shows a polypeptide having catalase activity which is the polypeptide shown by Muzykantov et al., and Labhasetwar et al. (MPEP 2143 (I)(G)).
One of ordinary skill in the art would have been motivated to have made that modification, because Liu et al. teaches that there is a need in the art to improve the performance of cellulose-hydrolyzing enzyme systems (pg. 1, para. [0006]). The described invention provides processes for increasing hydrolysis of cellulosic materials with enzyme compositions (pg. 1, para. [0008]). Therefore, one of ordinary skill in the art of producing animal feed compositions would have been motivated to have added enzymes (such as catalase and SOD) to said compositions that would help to hydrolyze cellulosic material which is the mainstay of, for example, bovine diets. The addition would improve digestion of animal feed, thereby improving the health benefits of the animal feed, e.g., by alleviating gastric distress and improving absorption of feed components.
Regarding claim 34, Becker et al. teaches the use of active agents, such as enzymes, in animal feed is common (pg. 1, para. [003]). The granule for delivering an active agent is an ingredient in a feed base mix or feed premix (pg. 3, para. [0010], entry# 1).
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Response to Arguments
Applicant’s arguments, pp. 7-11, filed on 08 January 2026, with respect to the prior art references cited in the 35 U.S.C. §103 rejections, have been fully considered but they are either not persuasive or are moot because the arguments do not apply to the references as they are applied in the context of the current rejection, or as new grounds necessitated by Applicant’s amendment, in which claim 3 was amended, and new claims 32-34 were added.
1. Applicant remarks (pg. 8) that Applicant respectfully submits the outstanding rejections are improper because they are founded upon non-analogous art. Muzykantov and Labhasetwar are non-analogous art- they are not from the same field of endeavor as the presently claimed invention and they are not reasonably pertinent to the problems faced by the inventors of the presently claimed invention. Whereas the pending claims are directed to granules for use in animal feed and are intended to address problems associated with the thermostability of superoxide dismutases and catalases exposed to the harsh conditions of steam pelleting at 90° C, both Muzykantov and Labhasetwar are directed to nanoparticles for delivering therapeutic enzymes to human patients and are intended to address problems associated with cellular degradation of those therapeutic enzymes. One seeking to produce thermostable granules for use in animal feed would not have looked to Muzykantov and Labhasetwar for guidance because they are not even remotely related to animal feed and because they are not at all concerned with thermostability.
However, in response to Applicant, the primary reference of Becker et al. shows the production of granules to be used as an animal feed composition, but does not show the specific enzymes of catalase and superoxide dismutase (SOD). However, Becker et al. teaches that the use of active agents, such as enzymes, in animal feed is common. Enzymes are known to improve digestibility of feed, reduce anti-nutritional factors in feed, and improve animal productivity (pg. 1, para. [003]). Becker et al. further teaches that enzymes are important feed ingredients and must be able to withstand increasingly higher processing temperatures used in pelleting processes, while continuing to deliver in vivo efficacy (pg. 2, para. [006]); and a second aspect of the present invention provides stable, durable granules with enzymes that withstand steam-heated feed pretreatment and pelleting process temperatures and compression forces while maintaining dissolution profiles that release the enzyme to provide in vivo bioavailability efficacy (pg. 7, para. [0016]).
That is, Becker et al. shows that enzymes are an important component of granules as or in animal feed compositions, and addresses the requirement of the enzymes to be thermostable, including during the steam-heating pelleting process. Becker et al. does not show the specific enzymes of catalase and SOD, but does show the specific enzyme phytase. Therefore, because Muzykantov et al. and Labhasetwar et al. show compositions comprising enzymes, these secondary references are analogous art. In addition, Muzykantov et al. teaches that administration of antioxidant enzymes has been shown to protect against oxidative stress in animals (pg. 11, para. [0068]), and also shows that the polymeric nanocarrier compositions can be administered to any animal, desirably to mammals, and more desirably to humans. (pg. 12, cont. para. [0072]). Labhasetwar et al. also shows an animal model for using SOD-loaded nanoparticles (pg. 20, para. [0086]). That is, both Muzykantov et al. and Labhasetwar et al. show that animals can be administered catalase and SOD, which analogous to the use of the animal compositions comprising enzymes shown by Becker et al.
2. Applicant remarks (pg. 10, para. 1-4) that neither Muzykantov nor Labhasetwar mentions thermostability. The only thing Muzykantov and Labhasetwar have in common with the pending claims is use of a polypeptide having superoxide dismutase activity and a polypeptide having catalase activity. Muzykantov and Labhasetwar provide no relevant teaching regarding the stabilization of enzymes exposed to the harsh conditions of steam pelleting at 90°C.
However, in response to Applicant, the instantly-claimed subject matter is directed to a granule, not a method for making the granule. Therefore, as noted above, the new limitations added to instant claim 3 are considered product-by-process language and are not considered to contribute to the determination of patentability: "If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985) (MPEP 2113). Certainly, it would have been obvious to have included catalase and SOD in the granules or animal feed compositions shown by Becker et al., which, in turn, teaches the inclusion of enzymes in said granules or animal feed compositions, and which addresses the need for thermostability of said granules during the steam-heating pelleting process.
3. Applicant remarks (pg. 10, last para. thru pg. 11) that, even if one of ordinary skill in the art had consulted both Muzykantov and Labhasetwar, he/she would not have been motivated to include a polypeptide having superoxide dismutase activity and a polypeptide having catalase activity in the granules of Becker because neither Muzykantov nor Labhasetwar provides any indication that superoxide dismutases and catalases can themselves "withstand steam-heated feed pretreatment and pelleting process temperatures and compression forces" or that inclusion in Becker's granules would somehow provide the necessary thermostability. Muzykantov nor Labhasetwar says anything at all about thermostability under such conditions.
However, in response to Applicant, this argument has been addressed above. In addition, it is not clear that the enzymes in the granules "provide the necessary thermostability" as much as the enzymes are required to be thermostable because of the processes that the granule compositions go through in order to be pelleted or otherwise processed. Again, such thermostability has been addressed by Becker et al. and, therefore, it would have been obvious to one of ordinary skill in the art to have understood that the granules and animal feed compositions shown by Becker et al. which included enzymes other than phytase (such as catalase and SOD) would also have been inherently thermostable.
4. Applicant remarks (pg. 11) that the Office has not presented any evidence or articulated rationale to show that the molar ratio of superoxidase dismutase to catalase was recognized in the art as a result-effective variable-not with respect to Muzykantov's and Labhasetwar's stated goals of treating human disease and certainly not with respect to thermal stability at 90°C.
However, in response to Applicant, MPEP 2144.05 (II)(B) states, in part: "..., after KSR, the presence of a known result-effective variable would be one, but not the only, motivation for a person of ordinary skill in the art to experiment to reach another workable product or process." See also MPEP 2141. Labhasetwar et al. shows that the described catalase and SOD nanoparticles may comprise catalase and SOD in varying amounts relative to each other, and said amounts include a ratio of superoxide dismutase to catalase activity that is greater than 5:1 (see 103 rejection above). Although Labhasetwar et al. does not show a molar ratio but weight (µg) amounts, it would have been obvious to have converted a weight ratio to a molar ratio with the reasonably predictable expectation that a molar (gr/mole) ratio could have been implemented to reflect a >5:1 ratio of SOD to catalase.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SHARON M PAPCIAK whose telephone number is (571)272-6235. The examiner can normally be reached M-F 8:30am-5:00pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Louise Humphrey can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/SMP/Examiner, Art Unit 1657