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
2. Applicants’ arguments and amendments filed on 9/12/2025, have been fully considered. Upon review, examiner noticed that the prior rejection can be made better by considering one new secondary prior art by Yu et al. CN 107927382 A in order to address specifically the claim limitation of “in an amount sufficient” as claimed in the independent claim 34. Therefore, the following action is made non-final.
Any objections and/or rejections made in the previous action, and not repeated below, are hereby withdrawn.
Status of the application
3. Claims 34-53 are pending in this office action.
Claims 34-53 have been rejected.
Obviousness Double Patenting
4. The non-statutory 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 non-statutory obviousness-type 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 USPQe2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQe2d 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); and 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 a non-statutory double patenting ground provided the conflicting application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement.
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. It is to be noted that, in this instance, these two applications filed by the same applicant or assignee. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
In this instance, it is to be noted that this application has independent claim 34 has “catalase and/or superoxide dismutase”. Claims 34-53 of this application is patentably indistinct at least from claims 1, 2 of Application No. 17/441731 (latest submitted amended claims on 10/24/2024 in 17/441731). It is to be noted that claims 41, 48, 49, having the SEQ ID# 31 (SOD) from Aspergillus juponicus of this application is identical to SEQ ID # 44 (SOD) of independent claim 1 in the application No. 17/441731 (in spec in PGPUB OF 17/441731, [0275]). It is to be noted that catalase, superoxide dismutase of claim 34 of this application are broad and can be any catalase and any superoxide dismutase which is/are patentably indistinct at least from claims 1, 2 of Application No. 17/441731.
Claim Rejections - 35 USC § 103
5. 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-AlA) 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 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.
6. Claim 34-38, 50-53 are rejected under 35 U.S.C. 103 as being unpatentable over NPL Pariza (Determining the safely of enzymes used in animal feed. Regulatory Toxicology and Pharmacology 56 (2010) 332-342) in view of NPL Litta et al. (DSM: Vitamin E: more than nature’s most powerful antioxidant 2018) and further in view of Yu et al. CN 107927382 A and as evidenced by NPL Ferreira et al. (Macromol. Biosci. 2003, 3, 179-188).
7. Regarding claim 34-38, 51, 52, 53, NPL Pariza discloses catalase from
Aspergillus niger (EC 1.11.1.6) as an enzyme currently used in animal feeds (in Table 1). One of ordinary skill in the art would have been motivated to perform the method to introduce catalase in feed composition in order to have the reasonable expectation of success to provide multi-beneficial effects when introduced into animal feed composition (page 332, col 2 last paragraph and page 333, col 1 first two paragraphs and Table 1). Therefore, it meets claims 34, 52, 53.
Therefore, the method to introduce catalase in feed composition would have been obvious by the method of applying the composition to an animal feed composition as claimed in claim 51. Therefore, the polypeptide reads on claim 34. It is known that catalase enzyme is a protein and proteins are peptides in nature. Therefore, a catalase polypeptide from A, niger reads on claim 35. It is known that Aspergillus niger is a fungi. Therefore, catalase protein (i.e. polypeptide having specific biological activity as catalase enzyme protein) is from fungal origin. Therefore, it meets claim limitation of claim 37.
NPL Pariza et al. is specifically silent about the claim limitation of “ in an amount sufficient” as claimed in claim 34. It is to be noted that claim 34 is broad.
However, more specifically, Yu et al. discloses that a feed complex enzyme preparation comprising catalase in an amount of 0.5-1.5 x 107 U/kg of the feed complex enzyme (Abstract) can be added in an amount of 0.15-0.4 wt.% of the animal feed (Paragraph above the heading “The beneficial effects of the invention are as follows”) which can enhance animal body immunity, inhibiting intestinal pathogenic bacteria, improving intestinal health level and improving production performance of livestock and poultry First paragraph under “ Inventive Content).
One of ordinary skill in the art may consider the teachings of Yu et al. as an effective amount used for feed additive in order to achieve, with reasonable expectation of success, the preservative property to preserve and protect the other ingredients like lipid, vitamins etc. when introduced into feed composition as claimed in claim 34.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Yu et al. to consider catalase as one additive enzyme in the feed composition having its preservative property and , in combination in feed formulation, it provides an improved production performance of livestock and poultry (at least in First paragraph under “ Inventive Content) in the feed composition.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Yu et al. to consider catalase as one additive enzyme in the feed composition having its preservative property and , in combination in feed formulation, it provides an improved production performance of livestock and poultry (at least in First paragraph under “ Inventive Content) in the feed composition.
NPL Pariza is silent about animal feed containing vitamins.
Litta et al. teach Vitamin E is not synthesized by poultry and pigs and is therefore an essential micronutrient to consider in feed formulation (see first paragraph, Under Summary). As evidenced by the PG Pub of the instant specification, vitamin E is fat soluble ([0472]). It would have been obvious to add a fat-soluble vitamin to an animal feed. One would have been motivated to do so since Pariza discloses an animal feed additive and Litta teaches Vitamin E is an essential micronutrient to consider in feed formulation. One would do so since Litta teaches Vitamin E is not synthesized by poultry and pigs. Therefore, one would add it to feeds for these animals.
One of ordinary skill in the art would have had a reasonable expectation of success to consider the teachings of Litta to include vitamin E in feed formulation because it is vitamin supplement and also it is not synthesized by poultry and pigs (First paragraph of Litta et al.).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Litta et al. to consider vitamin as an animal feed additive and Vitamin E serves as an essential micronutrient to consider in feed formulation. One would do so since Litta teaches Vitamin E is not synthesized by poultry and pigs (First paragraph of Litta et al.). Therefore, one would add it to feeds for these animals.
8. Regarding claim 36, it is known and as Pariza identifies catalase from Aspergillus niger (EC 1.11.1.6) (Table 1) which meets claim 36.
9. Regarding claim 38, NPL Pariza identifies catalase from Aspergillus niger (EC 1.11.1.6) as an enzyme currently used in animal feeds (in Table 1). As evidenced by the PG Pub of the 17/441714 application (retrieved from ABSS Search Report) instant specification at ([0197]) SEG ID NO 7 is the amino acid sequence of a mature polypeptice having catalase activity from Aspergillus niger comprising 730 amino acid residues.
It is to be noted that SEQ ID NO 7 of 17/441714 matches with the current application SEQ ID # 8 (730 aa, A. Niger) [ABSS Search result, SEE 510 Kb, Published Application, posted on 6/4/2025).
Catalase enzyme having SEQ ID NO #7 of 17/441714 is sold under the tradename Catazyme ([0197] of PGPUB of 17/441714) and is also evidenced by NPL Ferreira et al. (see page 1809, left column, first paragraph of Materials and Methods section). Therefore, absent evidence to the contrary, the catazyme from Novo reads on claimed SEQ ID # 8 (SEQ ID #8 has 100% matching SEQ ID # 7 of 17/441714 which is Catazyme [0197] of 17/441714) claim 38.
10. Regarding claim 50, it is to be noted that NPL Pariza Aspergillus niger (EC 1.11.1.6) as an enzyme currently used in animal feeds (in Table 1) which provides multi-beneficial effects when introduced into animal feed composition (page 332, col 2 last paragraph and page 333, col 1 first two paragraphs and Table 1).
One of ordinary skill in the art would have been motivated to perform the method to introduce catalase in feed composition in order to have the reasonable expectation of success to provide multi-beneficial effects when introduced into animal feed composition (page 332, col 2 last paragraph and page 333, col 1 first two paragraphs and Table 1). It is also to be noted that once catalase enzyme is in the feed composition, because the disclosed catalase is identical to claimed catalase of claim 50, therefore, it will have identical claimed property to inhibit (i.e. to protect) degradation of vitamins etc. as claimed in claim 50.
11. Claim 34, 39-40, 42, 43, 44 ,45-47 are rejected under 35 U.S.C. 103 as being unpatentable over NPL Pariza (Determining the safely of enzymes used in animal feed. Regulatory Toxicology and Pharmacology 56 (2010) 332-342) in view of Li et al. (CN 103667222 A) in view of Litta et al. (DSM: Vitamin E: more than nature’s most powerful antioxidant 2018) in view of Kusakabe et al. (JP 57-036984 A ; 1982-02-27) and further in view of Yu et al. CN 107927382 A. and as evidenced by NPL Ferreira et al. (Macromol. Biosci. 2003, 3, 179-188).
12. Regarding claims 34, 39, 40, 42, 44, 45, 46 and 47, it is to be noted that claim 34 “and/or” a polypeptide having superoxide dismutase activity “is considered as “the combination” or as the ‘alternative’ claim limitation which is needed to address dependent claims 39-40, and “and” combinations of two enzymes are claimed for claim 42 and claim 43 which depends on independent claim 34. NPL Pariza identifies catalase from Aspergillus niger (EC 1.11.1.6) as an enzyme currently used in animal feeds (in Table 1) to meet claim 43. The rejection made for independent claim 34 above using Pariza et al. is applicable here also. NPL Pariza et al. discloses a composition that reads on a polypeptide of fungal origin having catalase activity to meet at least claims 42, 43, 44 and 45 which recites “catalase”.
NPL Pariza et al. is silent about (i) claim limitation of claim 45 and (ii) regarding an animal feed comprising superoxide dismutase activity as claimed in claims 34, 39-40, 42-44, 46,47.
With respect to (i), regarding claims 45, and amended claim 46, NPL Pariza identifies catalase from Aspergillus niger (EC 1.11.1.6) as an enzyme currently used in animal feeds (in Table 1). As evidenced by the PGPub of the 17/441714 application (retrieved from ABSS Search Report) instant specification at ([0197]) SEG ID NO 7 is the amino acid sequence of a mature polypeptide having catalase activity from Aspergillus niger comprising 730 amino acid residues. SEQ ID NO 7 of 17/441714 matches with the current application SEQ ID # 8 (730 aa, A. Niger) [ABSS Search result, SEE 510 Kb, Published Application, posted on 6/4/2025).
Catalase enzyme having SEQ ID NO #7 of 17/441714 is sold under the tradename Catazyme ([0197] of PGPUB of 17/441714) and is also evidenced by NPL NPL Ferreira et al... Therefore, absent evidence to the contrary, the catazyme from Novo reads on claimed SEQ ID # 8 (SEQ ID #8 has 100% matching SEQ ID # 7 of 17/441714 which is Catazyme [0197] of 17/441714) claim 45 and amended claim 46.
With respect to (ii), Li discloses a feed compound containing an enzyme prepared from Aspergillus niger (Abstract). Li et al. also discloses superoxide dismutase is used in feed composition ([0031], [0087], [[0124], [0160] claims 1, 2, 10 of Li et al.) in an amount of 5-10 parts of SOD in the enzyme mix composition (0031]) where 5-10% of the enzyme mix composition is used in the feed composition ([0030]).
Kusakabe et al. discloses that superoxide dismutase can be isolated from Trichoderma spp., Aspergillus spp. (i.e. fungal origin) in pure form in order to use it in many products including food composition for its antioxidant property to protect oxidation sensitive component in the food composition (at least on pages 1, 2, under claims 1,2, and Under “Detailed Description). Therefore, it meets claims 34, 39-40, 42-44, 46, 47. Therefore the art teaches a composition that reads on a polypeptide of fungal origin having catalase activity.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Li et al. to add superoxide dismutase to an animal feed (in Li et al. in Abstract) in order to use it in many products including food composition for its antioxidant property to protect oxidation sensitive component in the food composition as disclosed by Kusakabe et al. (at least on pages 1, 2, under claims 1,2, and Under “Detailed Description). One would have had a reasonable expectation of success since Li teaches superoxide dismutase can be added to animal feeds (Abstract) because of its antioxidant property to protect oxidation sensitive component in the food composition as disclosed by Kusakabe et al. (at least on pages 1, 2, under claims 1,2, and Under “Detailed Description).
NPL Pariza et al. is specifically silent about the claim limitation of “ in an amount sufficient” as claimed in claim 34. It is to be noted that claim 34 is broad.
Yu et al. discloses that a feed complex enzyme preparation comprising catalase in an amount of 0.5-1.5 x 107 U/kg of the feed complex enzyme (Abstract) can be added in an amount of 0.15-0.4 wt.% of the animal feed (Paragraph above the heading “The beneficial effects of the invention are as follows”).
However, more specifically, Yu et al. discloses that a feed complex enzyme preparation comprising catalase in an amount of 0.5-1.5 x 107 U/kg of the feed complex enzyme (Abstract) can be added in an amount of 0.15-0.4 wt.% of the animal feed (Paragraph above the heading “The beneficial effects of the invention are as follows”) which can enhance animal body immunity, inhibiting intestinal pathogenic bacteria, improving intestinal health level and improving production performance of livestock and poultry First paragraph under “ Inventive Content).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Yu et al. to consider catalase as one additive enzyme in the feed composition having its preservative property and , in combination in feed formulation, it provides an improved production performance of livestock and poultry (at least in First paragraph under “ Inventive Content) in the feed composition.
Li et al. discloses SOD can be used in an amount of 5-10 parts of SOD in the enzyme mix composition (0031]) where 5-10% of the enzyme mix composition is used in the feed composition ([0030]) and SOD serves as an important antioxidant property in the composition (at least under Background of the invention, first paragraph) and it provides beneficial effects when used in an animal feed or animal feed additive, alone or in combination with a catalase, to improve animal performance and/or health (Paragraph above “Summary of the Invention).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Li et al. to include SOD in the feed composition because SOD serves as an important antioxidant property in the composition (at least under Background of the invention, first paragraph) and it provides beneficial effects when used in an animal feed or animal feed additive, alone or in combination with a catalase, to improve animal performance and/or health (Paragraph above “Summary of the Invention).
It is also to be noted that the disclosed catalase and/or SOD are/is identical to the claimed catalase and therefore, it will have identical property including the property to preserve and protect the other ingredients like lipid, vitamins etc. when introduced into feed composition as claimed in claim 34. it is inherent property of catalase.
NPL Pariza et al. is silent about animal feed containing vitamins.
Litta et al. teach Vitamin E is not synthesized by poultry and pigs and is therefore an essential micronutrient to consider in feed formulation (see first paragraph, Under Summary). As evidenced by the PG Pub of the instant specification, vitamin E is fat soluble ([0472]). It would have been obvious to add a fat-soluble vitamin to an animal feed. One would have been motivated to do so since Pariza discloses an animal feed additive and Litta teaches Vitamin E is an essential micronutrient to consider in feed formulation. One would do so since Litta teaches Vitamin E is not synthesized by poultry and pigs. Therefore, one would add it to feeds for these animals.
One of ordinary skill in the art would have had a reasonable expectation of success to consider the teachings of Litta to include vitamin E in feed formulation because it is vitamin supplement and also it is not synthesized by poultry and pigs (First paragraph of Litta et al.).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify NPL Pariza et al. to include the teaching of Litta et al. to consider vitamin as an animal feed additive and Vitamin E serves as an essential micronutrient to consider in feed formulation. One would do so since Litta teaches Vitamin E is not synthesized by poultry and pigs (First paragraph of Litta et al.). Therefore, one would add it to feeds for these animals.
13. Claims 41, 48 and 49 are rejected under 35 U.S.C. 103 as being unpatentable over NPL Pariza et al. in view of Li et al. (CN 103667222 A) in view of Litta et al. (DSM: Vitamin E: 2018) in view of Kusakabe et al. (JP 57-036984 A ; 1982-02-27) and further in view of Yu et al. as applied to claims 39 and 42, and in view of NPL SOD Seq (2015) (Retrieved from ncbi website)(https://www.ncbi.nlm.nih.gov/protein/ETS03846.1) and as evidenced by NPL SEQ ID No. 29 alignment search. SEE Search Result posted 6/04/2025 , under “Uniport for SEQ ID# 29 , 223 Kb , Result 1: Koike H., et al. "Comparative genomics analysis of Trichoderma reesei strains."; RL Ind. Biotechnol. 9:352-367(2013) This sequence was deposited on 23 Mar, 2015 and in NCBI website ] and further in view of Liu et al. ( CN 106267173 A).
14. Regarding claims 41, 48 and 49, NPL Pariza et al. in view of Li et al. and Kusakabe et al. disclose that the SOD enzyme isolated from many organisms including Trichoderma spp. having antioxidant property protects oxidation sensitive component in the food composition (at least on pages 1, 2, under claims 1, 2, and Under “Detailed
Description of Kusakabe et al.) and can be used in feed composition (in Li et al., Abstract).
NPL SOD sequence discloses that claimed SOD SEQ ID # 29 as claimed in claims 41, 48, 49 match 100% with superoxide dismutase (Cu, Zn SOD) of Trichoderma reesei [307 aa; Submitted Gen Bank: ETs00459.1, 23 Mar-2015) (SEE NPL SOD Seq (2015) filed on 6/13/2025 as NPL Reference. This one has 100% match with NPL SEQ ID No. 29 alignment search as found under Search Result posted 6/04/2025 , under “Uniport for SEQ ID# 29 , 223 Kb , Result 1Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.; RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013)].
It is to be noted that
(a) NPL SOD sequence discloses Cu, Zn SOD Sequence from Trichoderma reesii which matches 100% with claimed SEQ ID #29.
However, NPL SOD sequence is silent about isolation of Cu, Zn SOD from Trichoderma spp.
(b) Kusakabe et al. discloses the method of isolation of SOD from bacterial origin including Trichoderma spp. (at least on pages 1, 2, under claims 1,2, and Under “Detailed Description of Kusakabe et al.).
(c ) Liu et al. discloses the motivation to select specific Cu, Zn SOD enzyme preparation in particle form suitable to be used in food composition ( page 2, paragraph 2 ) which has anti-oxidant effect in vivo ( Page 1, Abstract, Under Technology field) , good thermal stability and storage stability (page 2 paragraph 5 under “Invention contents) and it prevents various diseases and/or subhealth state caused by oxidative stress ( Page 3, paragraph 5).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to consider to modify NPL Pariza et al. in view of Li et al. with the teaching of NPL SOD Enzyme Cu, Zn to select SOD Sequence from Trichoderma reesii which is Cu, Zn SOD and method of making protein from that disclosed sequence to make isolated SOD (Cu,Zn) enzyme using the isolation method from bacterial origin including Trichoderma spp. as disclosed by Kausakabe et al. (at least on pages 1, 2, under claims 1,2, and Under “Detailed Description of Kusakabe et al.) because the specific Cu, Zn SOD enzyme has anti-oxidant effect in vivo, good thermal stability and storage stability and it prevents various diseases and/or subhealth state caused by oxidative stress as disclosed by Liu et al. (Page 1, Abstract, Under Technology field, page 2 paragraph 5 under “Invention contents and Page 3, paragraph 5). In addition, it is an additional advantage that Cu, Zn SOD activity is maintained in presence of Cu, Zn which is normally present or as mineral supplement in an animal diet.
Response to Arguments
15. Applicants’ arguments have been considered. Accordingly, as mentioned above, examiner used one new secondary prior art by Yu et al. CN 107927382 A in order to address specifically the claim limitation of “in an amount sufficient” for catalase and Li et al. discloses the amount of SOD. In addition, Liu et al. is used as another secondary prior art to address and to strengthen motivation to select specific SOD enzyme containing Trichoderma reesi from (Cu, Zn SOD) as disclosed by NPL SOD SEQ from the broadly disclosed SOD enzymes and sources as disclosed by Kusakabe et al. The other arguments are addressed below.
16. Applicants argued that ODP rejection is not proper.
In response to these arguments the examiner notes that section 804 of the MPEP explicitly states that obvious non-statutory double patenting rejections are proper and lays out the procedures for these rejections, procedures which were followed herein.
` Arguments made for NPL Pariza et al.:
17. Applicants argued that
(i) “Pariza is a scientific review article that teaches that "[f]eed enzymes, including catalase, are typically added to animal feed to increase nutrient bioavailability by acting on fed components prior to or after consumption, i.e., within the gastrointestinal tract.
(ii) Pariza nor Ferreira neither teaches nor suggests catalase may somehow be used as a preservative to inhibit degradation of one or more vitamins, one or more proteins, one or more fats and/or one or more lipids.
(iii) It is clearly not sufficient for the Office to merely point to a composition comprising a catalase. Given the disclosures of the cited references, it is not at all surprising that the Office has not cited and neither Pariza nor Ferreira even hint at the possibility that such compositions may comprise catalase in an amount sufficient to inhibit degradation of vitamins, proteins, fats or lipids.
(iv) The outstanding rejection of claim 38 should also be withdrawn because the Office has not presented any credible evidence that it would have been obvious to utilize a peptide having catalase activity and at least 80% identity to any one of the recited sequences. The Office assumes, without any evidence or reasonable explanation, that the catalase solution described in Ferreira has 100% sequence identity with the presently recited SEQ ID NO: 8. More specifically, the Office simply assumes that all products sold under the tradename CATAZYME must contain the exact same catalase.
(v) The Office cannot support a rejection under 35 U.S.C. 103 with naked assumptions nor can it shift the burden of proof to Applicant. In the absence of any evidence tending to show the catalase solution described in Ferreira has at least 80% identity to any one of the recited sequences, the Office should withdraw the outstanding rejection of claim 38.
(vi) The outstanding rejection of claim 50 is premised upon an equally faulty assumption: that any composition comprising a catalase necessarily comprises an amount sufficient to inhibit degradation of one or more vitamins, one or more proteins, one or more fats and/or one or more lipids. The Office has not provided any evidence or articulated rationale that might reasonably be interpreted as supporting that assumption. Indeed, the Office has not provided any evidence or explanation at all. Again, the Office offers only a naked assumption. The outstanding rejection of claim 50 should therefore be withdrawn.
In response, as mentioned, examiner used one new secondary prior art by Yu et al. CN 107927382 A in order to address specifically the claim limitation of “in an amount sufficient” as claimed in the independent claim 34.
In response, it is to be noted that and as agreed by the applicants that NPL Pariza et al. suggests the addition of catalase enzyme to animal feed to increase nutrient bioavailability by acting on fed components prior to or after consumption, i.e., within the gastrointestinal tract. It is also to be noted that and as mentioned in the last office action that this catalase which is present in Catazyme (as evidenced by NPL Ferriera et al. [0197] as also evidenced by applicant’s specification [0197] in PGPUB) has 100% matching with the current application Seq ID #8 and discussed in detail in the rejection of claim 38 above and in the last office action. Even if it can be interpreted that catazyme may comprise catalase at least as an enzyme in Catazyme composition because of few formulations of catazyme made by the company, however, the presence of catalase in the catazyme composition is identical to the claimed catalase and having having identical property to the claimed catalase because of 100% sequence matching as discussed under item #9 in this office action above.
It is also to be noted that the composition claims comprising ingredients to make the final composition as final product. Therefore, what the end use is for, or what each individual component is used for is just considered as intended use.
Applicant’s attention is drawn to MPEP 2111.02 which states that intended use statements must be evaluated to determine whether the intended use results in a structural difference between the claimed invention and the prior art. Only if such structural difference exists, does the recitation serve to limit the claim. If the prior art structure is capable of performing the intended use, and then it meets the claim.
Regarding the argument made in (iv) above, it is also to be noted that and as discussed in the office action above that the catazyme from Novo as evidenced by NPL Ferreira et al. (see page 1809, left column, first paragraph of Materials and Methods section) and also as evidenced by applicant’s specification reads on claimed SEQ ID # 8 (SEQ ID #8 has 100% matching SEQ ID # 7 of 17/441714 which is, therefore, specific catalase containing Catazyme [0197] of 17/441714) claim 38. It can be interpreted that the disclosed Catazyme ( [0197] of 17/441714) has at least catalase enzyme which is derived from SEQ ID # 7 of 17/441714 and matches 100% with claimed SEQ ID # 8 (SEQ ID #8 has 100% matching SEQ ID # 7 of 17/441714 as claimed in claim 38. Even if independent claim 34 is broad and does not specify Catazyme, however, we may address that the disclosed catazyme from Novo taught by NPL Ferreira et al. can be identical to claimed catalase of claim 34 can read on catazyme as is evidenced by applicant’s specification and as also claimed in claim 38.
Therefore, the office is not making a rejection under 35 U.S.C. 103 with naked assumptions only as alleged in (v) above.
Regarding the allegations made for the rejection of claim 50 as alleged above in (vi) above, it is to be noted that the response is same as responded for (i)-(iii) above.
18. Applicants argued under section I that Litta teaches vitamin E as a powerful antioxidant and promising feed additive. Litta neither teaches nor suggests adding a catalase or a superoxide dismutase to animal feed, let alone adding one in an amount sufficient to inhibit degradation of one or more vitamins, one or more proteins, one or more fats and/or one or more lipids”.
In response, yes. Litta et al. is not used to add a catalase or a superoxide dismutase to animal feed. Litta et al. is used as secondary prior art to teach the addition of vitamin E as micronutrient supplement in the feed composition of poultry and pigs because they cannot synthesize vitamin E. Therefore, modified Pariza/Ferrira as modified by Litta et al. with the supplementation of vitamin E to the animal feed as micronutrient supplement in the feed composition of poultry and pigs because they cannot synthesize vitamin E meet the claimed invention.
However, note that while Litta et al. do not disclose all the features of the present claimed invention, Litta et al. is used as teaching reference, and therefore, it is not necessary for this secondary reference to contain all the features of the presently claimed invention, In re Nievelt, 482 F.2d 965, 179 USPQ 224, 226 (CCPA 1973), In re Keller 624 F.2d 413, 208 USPQ 871, 881 (CCPA 1981). Rather this reference teaches a certain concept, namely Vitamin E as micronutrient supplement in feed composition, and in combination with the primary reference, discloses the presently claimed invention.
Arguments made for Kusakabe:
19. Applicants argued under section II and III that
(i) “Kusakabe is a patent application describing microorganisms used in the production of superoxide dismutases. Kusakabe does not teach or suggest a composition comprising an enzymatic preservative comprising a polypeptide having catalase activity and/or a polypeptide having superoxide dismutase activity in an amount sufficient to inhibit degradation of one or more vitamins, one or more proteins, one or more fats and/or one or more lipids present in a feed or feed additive composition.
(ii) Because Kusakabe does not endorse the idea of using a superoxide dismutase for suppressing oxidation of food, it does not even qualify as analogous art and should not have been cited against the pending claims.
In response to applicant's arguments (i) and (ii) above, that Kusakabe is non- analogous art, it has been held that a prior art reference must either be in the field of the inventor’s endeavor or, if not, then be reasonably pertinent to the particular problem with which the inventor was concerned, in order to be relied upon as a basis for rejection of the claimed invention. See In re Oetiker, 977 F.2d 1443, 24 USPQ2d 1443 (Fed. Cir. 1992). In this case, is to be noted that Kusakabe does endorse the idea
of using a superoxide dismutase (SOD) for suppressing oxidation of food (at least in Kusakabe et al. , page 2, second paragraph) as discussed on page 10, last Office Action. However, examiner used Kusakabe in addition to Li who discloses SOD in animal feed composition as discussed above.
20. Applicants also argued that "Two separate tests define the scope of analogous prior art: (1) whether the art is from the same field of endeavor, regardless of the problem addressed and, (2) if the reference is not within the field of the inventor's endeavor, whether the reference still is reasonably pertinent to the particular problem with which the inventor is involved."21 Kusakabe is non-analogous art because it fails to satisfy either prong of that analysis”.
In response , as discussed above, Kusakabe does endorse the idea of using a superoxide dismutase for suppressing oxidation of food (at least in Kusakabe et al. , page 2, second paragraph). Therefore, Kusakabe is an analogous art. Therefore, it meets two pronged analysis to qualify to be an analogous art.
Also, according to MPEP 2143.01, “Obviousness can be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so. In re Kahn, 441 F.3d 977, 986, 78 USPQ2d 1329, 1335 (Fed. Cir. 2006) (discussing rationale underlying the motivation-suggestion-teaching test as a guard against using hindsight in an obviousness analysis)”.
21. Applicants also argued that “Furthermore, even if one of ordinary skill in art had decided to attempt such use, there is no rational basis for believing he/she would have selected the polypeptide of ETS03846 from amongst the countless superoxide dismutase in the GenBank library. The proposed selection of ETS03846 is a clear, unambiguous example of impermissible hindsight bias”.
In response, if we consider responses made above, it is to be noted that examiner has concluded with the motivation to consider Trichoderma reesei Cu,Zn SOD , and it has 100% match with one of the claimed SOD SEQ ID as claimed in the claimed invention and discussed in detail in the office action above. Therefore, it is not unambiguous example of impermissible hindsight bias.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
The rejection is made as non-final.
Conclusion
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/BHASKAR MUKHOPADHYAY/
Examiner, Art Unit 1792