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 3/20/2026, overcomes the rejections of record, however, the new grounds of rejection as set forth below are necessitated by applicants’ amendment and therefore, the following action is Final.
Any objections and/or rejections made in the previous action, and not repeated below, are hereby withdrawn.
Status of the application
3. Claims 1-31 are pending in this office action.
Claim 32 has been cancelled.
Claims 1-31 have been rejected.
Claims 1-31 have been rejected.
Claim Rejections - 35 USC § 103
4. 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.
5. 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. 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 non-obviousness.
7. Claim(s) 1, 8, 17, 25 are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application).
8. Regarding claims 1, 8, 17 and 25,
Haahr et al. also discloses that SEQ ID # 1 and SEQ ID #3( [0565], [0569], [0582], [0585]) match the claimed sequence ID # 74 and SEQ ID # 75 respectively (in PGPUB pages 55 and 56 for applicant’s SEQ ID #74 and #75 respectively).
It is confirmed by ABSS search result (posted 11/18/2025) that the match has 100% identity. For example, Haahr et al. US 2020/0229463 A1 (16/630156) (16/630156 SEQ ID #1 match #74 SEQ ID # 1 matches 100% with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025 , 268 kb “Published Application).
9. Regarding the claim limitation of “ increasing the ratio of kynurenine : tryptophan ratio in an amount of at least 10% compared to the control group without the protease” ad claimed in claims 1,8,17,25, it is to be noted that the disclosed protease has 100% identity with claimed protease of claims 1,8,17, 25 and is used as feed enzymes for claims 1,8,17, 25 as discussed above, therefore, it would have identical claimed property including the increased kynurenine : tryptophan ratio as claimed in claim 1, serotonin: tryptophan ratio as claimed in claim 8, tryptamine: tryptophan ratio as claimed in claim 17, and melatonin: tryptophan ratio as claimed in claim 25.
10. Claims 2- 5 are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application) as applied to claim 1 and further in view of NPL Ohashi et al. (in International Journal of Tryptophan Research 2013:6 (Suppl. 1 ) 9-14).
11. Regarding claim 2, Haahr et al. is silent about the method to measure kynurenine and tryptophan.
NPL Ohashi et al. discloses the method of measuring Kynurenine , tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan and Kynurenine).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Haahr et al. to include the teaching of NPL Ohashi et al. to measure the amount of kynurenine and tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan and Kynurenine) in order to determine their increased ratio which is a parameter to determine the effectiveness for improving the health of the animal in presence of the disclosed feed additive protease compared to non- treated group of individual as claimed in claimed invention.
12. Regarding claim 3, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the “improvement of the health of said group of production animals comprises providing one of more of the following benefits to said group of production animals: improving the welfare of said group of production animals, decreasing systemic inflammation of said group of production animals, decreasing local inflammation of said group of production animals, and reducing the light regimen into the daily circadian rhythm of said group of production animals” as claimed in claim 3.
13. Regarding claim 4, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of “ improvement of welfare comprises reducing social disturbance among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of social disturbance among said group of production animals”.
14. Regarding claims 5, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of the “improvement of welfare [which] comprises reducing feather pecking among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of feather pecking among said group of production animals.
15. Claims 6, 7, 15, 16, 23, 24, 30, 31, are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application) as applied to claims 1, 8, 17, 25 and further in view of Aureli et al. (WO2020/058226).
16. Regarding claims 6, 15, 23, 30, Haahr et al. is silent about the claimed concentration of protease as claimed in claims 6,15,23, 30.
Aureli et al. discloses that the composition or animal feed is dosed so that the polypeptide having protease activity is at a level of 50 to 300 mg per kg ( i.e. 50-300 g/Ton because 1 Ton =100 kg) animal feed, such as 80 to 250 mg, 100 to 200 mg per kg animal feed, or any combination of these intervals (at least in claim 15 of Aureli et al.) which overlaps claimed range protease concentration as claimed in claims 6,15,25,30. It shows prima facie case of obviousness according to MPEP 2144.05. In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990).
Aureli et al. also discloses that the animal feed composition can be used for turkeys, ducks, piglets etc. (at least on page 6) as claimed in claims 7, 16, 24, 31.
One of ordinary skill in the art would have been motivated to modify Haahr et al. to include the teaching of Aureli et al. to consider the teaching of disclosed range amount of protease in order to provide desired protease treated protein in animal diet for its better digestible form which helps to improve body weight, improving litter quality etc. (at least in claim 15 of Aureli et al.).
It is also to be noted that it is optimizable. One of ordinary skill in the art can optimize the concentration of either of them from within the disclosed range value which will meet the claimed range value in order to have desired benefits. In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990).
Additionally, absent showing of unexpected results, the specific amount of enzyme protease is not considered to confer patentability to the claims. As the age of the animal, health improvement related performances are variables that can be modified, among others, by adjusting the amount of said enzyme protease, the precise amount would have been considered a result effective variable by one having ordinary skill in the art at the time the invention was made. As such, without showing unexpected results, the claimed amount of said enzyme(s) cannot be considered critical. Accordingly, one of ordinary skill in the art at the time the invention was made would have optimized, by routine experimentation, the amount of said enzyme(s) in Aureli et al., to amounts, including that presently claimed, in order to obtain the desired effect e.g. taste, texture etc (5). (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223).
17. Claim 9- 14 are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application) as applied to claim 8 and further in view of Rokutan et al. WO 2017 /047776 A1.
18. Regarding claim 9, Haahr et al. are silent about the method to measure tryptophan and serotonin.
Rokutan et al. discloses the method of measurement of plasma tryptophan and stool serotonin using HPLC method (at least on page 5, under Example 1). It is to be noted that it is within the skill of one of ordinary skill in the art to measure and optimize the measurement of tryptophan in stool also by using the same method used for blood plasma as both are the biological samples.
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Haahr et al. to include the teaching of Rokutan et al. to measure the amount of serotonin and tryptophan in blood (at least page 5, Example 1) in order to determine their increased ratio which is a parameter to determine the effectiveness for improving the health of the animal in presence of the disclosed feed additive protease compared to non- treated group of individual as claimed in claimed invention.
19. Regarding claim 10, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the “improvement of the health of said group of production animals comprises providing one of more of the following benefits to said group of production animals: improving the welfare of said group of production animals, decreasing systemic inflammation of said group of production animals, decreasing local inflammation of said group of production animals, and reducing the light regimen into the daily circadian rhythm of said group of production animals” as claimed in claim 10.
20. Regarding claim 11, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of “ improvement of welfare comprises reducing social disturbance among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of social disturbance among said group of production animals”.
21. Regarding claim 12, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of the “improvement of welfare [which] comprises reducing feather pecking among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of feather pecking among said group of production animals.
22. Regarding claims 13, 14, as discussed above, the disclosed protease has 100% identity with claimed protease and is used as feed enzymes in the animal diet composition. Therefore, it would have identical claimed property including the increased kynurenine : tryptophan ratio which is within the skill of one of ordinary skill in the art who can confirm it by measuring the ratio of kynurenine : tryptophan in the feces or blood by using any standard method. Therefore, this will cause an obvious “improvement of welfare comprising restoration of the natural photoperiod of said group of production animals” as claimed in claim 13 which depends on claim 9 and the effect would have obvious been continued with the natural photoperiod time which can be maintained for “at least 8 hours of darkness’ as claimed in claim 14. The reason is, this is considered as inherent property. In this instance also, when the disclosed additive protease is identical enzyme proteins of claimed protease (e.g. derived from 100% SEQ Identity) in the feed composition, therefore, will have identical claimed property including the claimed property of an “ improvement of welfare comprising restoration of the natural photoperiod of said group of production animals” as claimed in claim 13 and the effect would have obvious been continued with the natural photoperiod time which can be maintained for “at least 8 hours of darkness’ as claimed in claim 14.
23. Claims 18- 22 are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application) as applied to claim 17 and further in view of NPL Ohashi et al. (in International Journal of Tryptophan Research 2013:6 (Suppl. 1 ) 9-14) and in view of O'BRIEN et al. CA 3077692 A1.
24. Regarding claim 18, Haahr et al. is silent about the method to measure tryptophan and tryptamine.
NPL Ohashi et al. discloses the method of measuring tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan).
O'BRIEN et al. discloses the method of measuring tryptamine in biological sample e.g. blood, stool etc. (Under “Methods of assaying tryptamine” , pages 29-30).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Haahr et al. to include the teaching of NPL Ohashi et al. to measure the amount of kynurenine and tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan and to include the teaching of to measure the amount of tryptophan as disclosed by NPL Ohashi et al. and tryptamine as disclosed by O'BRIEN et al. O'BRIEN et al. to measure tryptamine in biological sample e.g. blood (Under “Methods of assaying tryptamine”) in order to determine their increased ratio of tryptamine: tryptophan which is a parameter to determine the effectiveness for improving the health of the animal in presence of the disclosed feed additive protease compared to non- treated group of individual as claimed in claimed invention.
25. Regarding claim 19, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the “improvement of the health of said group of production animals comprises providing one of more of the following benefits to said group of production animals: improving the welfare of said group of production animals, decreasing systemic inflammation of said group of production animals, decreasing local inflammation of said group of production animals, and reducing the light regimen into the daily circadian rhythm of said group of production animals” as claimed in claim 19.
26. Regarding claim 20, claim 20 depends on claim 19 and claim 19 ultimately depends on claim 17. As discussed above, the disclosed protease has 100% identity with claimed protease of claim 17 from which claim 20 ultimately depends. Therefore, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the “improvement of the performance of said group of production animals comprises providing one of more of the following benefits to said group of production animals: improving nutrient absorption, reduce gut peristaltic motility, improving vitamin absorption, and improving feed enzymatic processing” as claimed in claim 20.
17. Regarding claim 21, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of “ improvement of welfare comprises reducing social disturbance among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of social disturbance among said group of production animals”.
27. Regarding claim 22, it is to be noted that the disclosed protease has 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of the “improvement of welfare [which] comprises reducing feather pecking among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of feather pecking among said group of production animals.
28. Claim 26-29 are rejected under 35 U.S.C. 103 as being unpatentable over Haahr et al. US 2020/0229463 A1 (16/630156) and as evidenced by ABSS Search Report posted 11/18/2025 (16/630156 SEQ ID #3 match #74 SEQ ID # 1 matches with SEQ ID # 74 protease of current application. SEE ABSS search result posted 11/18/2025, 268 kb “Published Application) as applied to claim 17 and further in view of NPL Ohashi et al. (in International Journal of Tryptophan Research 2013:6 (Suppl. 1 ) 9-14) and in view of Ideas et al. FR 3052063 A1.
29. Regarding claim 26, Haahr et al. is silent about the method to measure tryptophan and tryptamine.
NPL Ohashi et al. discloses the method of measuring Kynurenine , tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan and Kynurenine).
Ideas et al. discloses the method of measuring melatonin in blood (Melatonin in blood , page 4, Under Ex 1 ).
One of ordinary skill in the art before the effective filling date of the claimed invention would have been motivated to modify Haahr et al. to include the teaching of NPL Ohashi et al. to measure the amount of tryptophan in blood sample (at least in page 10, col 2 under “Determination of tryptophan and Kynurenine) and to include the teaching of Ideas et al. to measure the amount of melatonin as disclosed by Ideas et al. in order to determine their increased ratio of melatonin : tryptophan which is a parameter to determine the effectiveness for improving the health of the animal in presence of the disclosed feed additive protease compared to non- treated group of individual as claimed in claimed invention.
30. Regarding claim 27, it is to be noted that the disclosed protease have 100% identity with claimed protease, therefore, it would have identical claimed property including the “improvement of the health of said group of production animals comprises providing one of more of the following benefits to said group of production animals: improving the welfare of said group of production animals, decreasing systemic inflammation of said group of production animals, decreasing local inflammation of said group of production animals, and reducing the light regimen into the daily circadian rhythm of said group of production animals” as claimed in claim 27.
31. Regarding claim 28, it is to be noted that the disclosed protease have 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of “ improvement of welfare comprises reducing social disturbance among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of social disturbance among said group of production animals”.
32. Regarding claim 29, it is to be noted that the disclosed protease have 100% identity with claimed protease, therefore, it would have identical claimed property including the claimed property of the “improvement of welfare [which] comprises reducing feather pecking among said group of production animals”. It is to be noted that it is within the skill of one of ordinary skill in the art to evaluate “reduction of feather pecking among said group of production animals.
Response to arguments
33. Applicant’s arguments and amendments overcome claim objection, and 112 second paragraph rejections of record. Applicant’s arguments and amendment of independent claims 1, 8, 17, 25 overcome the rejections of record made using Aureli et al. as primary prior art.
It is to be noted that Aureli et al. was used as primary prior art to address “protease and muramidase” in the animal diet. As amended claims 1,8,17,25 have been amended to delete ‘muramidase’, therefore, independent claims 1,8,17,25 have been rejected by considering Haahr et al. as primary prior art. We considered Aureli et al. as secondary prior art to address the concentration of protease in combination with result effective variable, as claimed in claims 6,15,23,30 and to meet the specific animal as claimed in claims 7, 16, 24, 31 in order to make final office action. Haahr et al. has 100% sequence identity with the claimed protease of claims 1,8,17,25. As because the new ground of rejection is made based on the amendment of independent claims 1,8,17,25, therefore, the rejection is made as final.
34. Applicants argued on fourth page, first paragraph that “ As illustrated in Example 3 of the present application, protease supplementation increased tryptophan levels in the gut (Fig. 2) and increased the kynurenine :tryptophan ratio, serotonin :tryptophan ratio and melatonin :tryptophan with more than 10%, while decreasing the tryptamine :tryptophan ratio with more than 20% (Table 1). The Examples also show that the concentrations of serum insulin and glucagon increase to a higher level in the protease treated group compared to the control group which suggests that feeding protease to broilers may result in a positive effect of prolonging the daylight period to the broilers (Example 4)”.
In response, it is to be noted that independent claim 1 , 8, 17 and 25 broadly claim “a feed additive comprising a protease”. The combinations of prior arts meet the claim limitation of supplementing protease in the animal diet and discussed in the office action above. Therefore, as the disclosed protease is identical to the claimed protease, therefore, it would have been obvious that the disclosed protease containing animal diet would have the identical claimed property including the property of an increased in the kynurenine :tryptophan ratio, serotonin :tryptophan ratio and melatonin :tryptophan with more than 10%, while decreasing the tryptamine :tryptophan ratio with more than 20% (Table 1).
35. Applicants argued that “Notably, Aureli et al. is absolutely silent concerning:
i. Methods which can regulate tryptophan and/or tryptophan-derived metabolites in the body of a group of production animals kept in a confined space.
While Aureli et al. discusses performance parameters, such as European Production Efficiency Factor (EPEF), Body Weight (BW) and Feed Conversion Ratio (FCR), Aureli et al. does not show any effect on tryptophan and/or tryptophan-derived metabolites. In particular, Aureli et al. does not once mention tryptophan-derived metabolites.
ii. A feed composition comprising a protease without a muramidase.
The observed positive effects on litter quality and/or footpad dermatitis of birds are demonstrated for compositions comprising a muramidase alone or a muramidase in combination with a protease, never for a protease alone. Hence, Aureli et al. does not show any technical effect of a protease alone.
iii. A feed composition comprising a protease sequence identity of at least 70% to any one of SEQ ID NOs 72-76 or being a variant of any one of SEQ ID NOs: 72-76 as defined in the claims”.
(iv) As acknowledged on page 6 of the Office Action, Aureli et al. is silent about any specific proteases, and in particular, Aureli et al. is silent concerning a protease of any one of SEQ ID NOs: 72-76 of the present application.
In summary, Aureli et al. teaches the skilled person that a muramidase and a combination of a muramidase and a protease can be used for improving litter quality and/or footpad dermatitis of birds.
(v) Aureli et al. does not teach or even suggest that a combination of a “muramidase and a protease” can be used to regulate the tryptophan-derived metabolites in the gut or blood of a group of production animals, even less specifically for increasing the ratio of kynurenine:tryptophan, increasing the ratio of peripheral serotonin:tryptophan, decreasing the ratio of tryptamine:tryptophan or increasing the ratio of melatonin:tryptophan. Even less, does Aureli et al. teach or even suggest an effect of a protease alone on any of these metabolites or metabolite ratios.
As the skilled person is provided no indication that a protease can be used to regulate the tryptophan-derived metabolites or any of the claimed metabolite ratios, the skilled person is provided no motivation to consult Haarh et al. in the first place.
Even if the skilled person was to consult Haarh et al., Haarh et al. is also silent concerning an effect of a protease on any of the claimed metabolites or metabolite ratios.
In response to (i), it is to be noted that Haarh et al. is used as primary prior art and Aurelli et al. is used as secondary prior art in this office action. Secondary prior art by Aureli et al. is used to address protease enzyme is included in a method of making an animal feed composition. Therefore, even if Aureli et al. does not specifically disclose the “Methods which can regulate tryptophan and/or tryptophan-derived metabolites in the body of a group of production animals kept in a confined space” as alleged by the applicants, it is considered as inherent property. Once the disclosed method comprising protease in the diet composition, therefore, the disclosed protease containing diet composition is identical to the claimed protease containing diet composition as claimed in claims 1, 8,17, 25. Therefore, the disclosed diet composition would have claimed property as claimed in claims 1,8,17,25.
In response to (ii), it is to be noted that Aureli et al. does not have to show any technical effect of a protease alone. Claims 1, 8, 17, 25 are amended to claim “the method comprising a feed additive comprising a protease”. It is to be noted that the claims recite “comprising” open ended transitional phrase in the amended independent claims 1,8,17, 25. Therefore, it does not exclude other additives other than protease in the claims 1, 8, 17 and 25.
In response to (iii), it is agreed that Aureli et al. broadly discloses “protease”. However, Haahr et al. discloses specific protease containing animal diet composition which has 100% identity with the claimed protease sequence of claims 1,8,17,25. As mentioned above, It is to be noted that Aureli et al. was used as primary prior art to address “protease and muramidase” in the animal diet. As amended claims 1,8,17,25 have been amended to delete ‘muramidase’, therefore, we can consider rejecting claims 1,8,17,25 by considering Haahr et al. as primary prior art.
36. Applicant’s other arguments in relation the Aureri et al. have been considered but are moot as Aureri is no longer the primary reference.
The reason is and as mentioned above, Aureri et al. is considered to address claims 6, 15, 23 and 30 because, Aureri et al. broadly discloses that the range amount of protease is applicable broadly to any protease including the protease of Haahr et al. also. Therefore, this disclosed range amount of protease would provide the guideline to one of ordinary skill in the art to consider optimizing the amount of protease which will be effective to have desired effect including an increased ratio of kynurenine: tryptophan etc. in the body of experimental animal fed with the protease supplemented diet compared to control group of animals.
The rejection is made as final.
Conclusion
37. 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 the communication or earlier communications from the examiner should be directed to Bhaskar Mukhopadhyay whose telephone number is (571)-270-1139.
If attempts to reach the examiner by telephone are unsuccessful, examiner’s supervisor Erik Kashnikow, can be reached on 571-270-3475. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/BHASKAR MUKHOPADHYAY/
Examiner, Art Unit 1792
/ERIK KASHNIKOW/Supervisory Patent Examiner, Art Unit 1792
Prosecution Insights