DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s amendment of claims 7, in the paper of 3/3/2026, is acknowledged. Applicants' arguments filed on 3/3/2026, have been fully considered and are deemed to be persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn. Claims 1-3, 7-9, 37, 52, 55-59, 62-64, are at issue and are present for examination.
Election/Restrictions
Applicants election without traverse of Group 1, claims 1-4, 7-9, 11, 37, 52-55 and 64, drawn to an enzyme for reducing the amount of acrylamide in a preparation, in the paper of 3/17/2025, is acknowledged. Applicants election without traverse of the following species:
Species Group 1: (a) Position L424 to position A507;
Species Group 2: the combination of (a) Position L424 to position A507; (b) position S33 to position A74;.
Species Group 3: (a-1);
Species Group 4: (a-1) and (b-2);
Species Group 5: (a-1)(b-2) and (c-1);
Species Group 6: E24.
Species Group 7: A74 and G445.
Species Group 8: A74 and G445.
Species Group 9: G445;
Species Group 10: SEQ ID NO:22;
Species Group 11: No election made;
Species Group 12: No election made;
Species Group 13: No election made;
Claims 56-59, 62, 63 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Specification
The disclosure is objected to because of the following informalities: As stated in the previous office action applicants reference to “P487” and “A486” in previous claim 7 was unclear. Applicants specification is objected to on the basis that applicants have corrected the issue in claim 7, however the issue remains in applicants specification (i.e. “P487” and A486”).
Appropriate correction is required.
Claim Rejections - 35 USC § 102
The rejection of claims 1, 2, 7, 8, 9, 11 and 55 under 35 U.S.C. 102(a)(1) as being anticipated by Wasabi et al., JP2006340630A (IDS of 3/17/2025, Google Translation PTO-892) is withdrawn based upon applicants amendment of the claims in the paper of 10/24/2025.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 2, 3, 7, 8, 9 and 55 is/are rejected under 35 U.S.C. 103 as being unpatentable over Watabe et al., JP2006340630A (IDS of 3/17/2025, Google Translation PTO-892).
This rejection was stated in the previous office action as it applied to previous claims 1, 2, 3, 7, 8, 9 and 55. In response to the rejection applicants have amended the claims and traverse the rejection as it applies to the newly amended claims. For applicants convenience the original rejection is repeated herein.
Watabe et al., JP2006340630A teach isolation of an amidase enzyme from Pseudonocardia thermophila comprising the amino acid sequence of SEQ ID NO:10, which has 100% sequence identity to instant SEQ ID NO:2. The amidase enzyme taught by Watabe et al. also has greater than 97% sequence identity to instant SEQ ID NO:22. Watabe et . teach that the amidase has the following characteristics: (a) exhibiting ≥50% of the amidase activities in the absence of the ammonia in a reaction condition of pH 9.0 even in the presence of 0.2 M ammonia; (b) exhibiting higher specific activities on the 2-hydroxy-4-methylthiobutylamide than methionineamide; (c) having an apparent molecular mass of 53 kDa on SDS-PAGE; (d) having 60-70°C optimum temperature of the activities; (e) stable at a temperature of ≤60°C at a nearly neutral pH; and (f) exhibiting high activities in a wide pH range of pH 5.5-10.0. Watabe et al. further teach enzyme variants of the enzyme having the amino acid sequence of SEQ ID NO:10 in which one or several amino acids are deleted, substituted or added in the amino acid sequence of positions 24 to 95 of the amino acid sequence of SEQ ID NO:10.
Watabe et al., JP2006340630A further teach cloning and expression of the nucleic acid encoding the amidase enzyme in E. coli (see claims and supporting text)..
One of skill in the art before the effective filing date would have been motivated to create variant amidases of the amidase enzyme having the amino acid sequence of SEQ ID NO:10, as taught by Watabe et al., as a means of identifying/creating enzymes which have improved amidase properties such as higher ammonia resistance and higher specific activities on 2-hydroxyl-4-methylthiobutylamide. One of skill in the art before the effective filing date would have been motivated to use the nucleic acid encoding the amidase of SEQ ID NO: 10 to substitute each of the amino acid residues of positions 24 to 95 as a means of identifying those variant amidases of SEQ ID NO:10 having improved properties as taught by Watabe et al. One would have been further motivated to substitute multiple amino acids at amino acids positions 24 to 95 as taught by Watabe et al. with amino acids with different reactive side chains such as S33F, S33R, S33H and S33Y as a means of altering the catalytic properties of the amidase. The expectation of success is high given the high level of skill in the art of recombinant protein engineering as exemplified by Watabe et al. and that Watabe et al. teaches all the resources and methods necessary to create such variants amidases of SEQ ID NO:10.
Applicants Response
Applicant traverses the rejection on the basis that applicants submit that there is not a reasonable expectation of success to identify the particular improved sequences as currently claimed that show improved stability and activity at such pH values and temperatures present when treating acrylamide containing solutions such as coffee.
Applicant submits that the currently amended claim of the present application identifies several substitutions relative to the wildtype amidase gene, which lead to surprisingly improved enzyme variants. Applicant submits that all of the variants are displayed in the working Examples section (see pages 65-74 of the specification of the present application as originally filed) and their improvement in activity or stability is shown therein.
Applicant submits that the problem with the cited document Watabe is that only the wild-type sequence of a new amidase enzyme from Pseudonocardi thermophila JCM3095 is shown, while substitutions in the range of amino acid 24 to 95 are merely suggested. Applicant submits that Watabe does not make, use, or characterize any other variants of this amidase enzyme from Pseudonocardi thermophila. Applicant submits that thus, Watabe fails to disclose any specific variants, better yet the specific variants cited in the presently pending claim 1 (at least one amino acid substitution at positions S33, D68, A74, G175, S225, L424, G445, A453, and A507).
Applicant submits that most of the mutation positions identified in the present application are outside this suggested area in the enzyme. See, e.g., Table 2 of the present application as originally filed in which three (3) out of nineteen (19) examined substitutions are within this AA 24-AA 95 portion of the amidase enzyme. Applicant submits that moreover, the substitutions identified in the present application and encompassed by the currently pending claims are explicit disclosures of amino acid positions and substitutions thereof, which are neither suggested in Watabe nor has the person skilled in the art the prospect of success only when reviewing the sequence of the wildtype enzyme.
At least insofar as Watabe fails to disclose a specific variant with a specific amino acid substitution selected from positions S33, D68, A74, G175, S225, L424, G445, A453, or A507, Applicant thus asserts the presently pending claims are nonobvious over Watabe.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered however, is found non-persuasive for the reasons previously made of record stated above and for those reasons repeated herein.
In response to applicants submission that there is not a reasonable expectation of success to identify the particular improved sequences as currently claimed that show improved stability and activity at such pH values and temperatures present when treating acrylamide containing solutions such as coffee, this is not found persuasive for the reasons stated previously and repeated above, one of skill in the art before the effective filing date would have been motivated to create variant amidases of the amidase enzyme having the amino acid sequence of SEQ ID NO:10, as taught by Watabe et al., as a means of identifying/creating enzymes which have improved amidase properties such as higher ammonia resistance and higher specific activities on 2-hydroxyl-4-methylthiobutylamide. One of skill in the art before the effective filing date would have been motivated to use the nucleic acid encoding the amidase of SEQ ID NO: 10 to substitute each of the amino acid residues of positions 24 to 95 as a means of identifying those variant amidases of SEQ ID NO:10 having improved properties as taught by Watabe et al. One would have been further motivated to substitute multiple amino acids at amino acids positions 24 to 95 as taught by Watabe et al. with amino acids with different reactive side chains such as S33F, S33R, S33H and S33Y as a means of altering the catalytic properties of the amidase. While it is admitted that Watabe et al. does not disclose specifically disclosed mutations or “improved sequences”, they do make obvious substitutions of positions 24 to 95 of SEQ ID NO:10.
In response to applicants submission that the currently amended claim of the present application identifies several substitutions relative to the wildtype amidase gene, which lead to surprisingly improved enzyme variants, this is not found persuasive as it is not surprising that alterations in the wildtype amidase enzyme would lead to improved enzyme variants.
Applicants suggestion that the “problem” with the cited document Watabe is that only the wild-type sequence of a new amidase enzyme from Pseudonocardi thermophila JCM3095 is shown, while substitutions in the range of amino acid 24 to 95 are merely suggested, is not found persuasive as a “problem”. Further applicants acknowledgement of Watabe et al.’s teaching of the wild-type sequence of a new amidase enzyme from Pseudonocardi thermophila JCM3095 as well as the suggestion of substitutions in the range of amino acid 24 to 95 is appreciated.
In response to applicants submission that Watabe does not make, use, or characterize any other variants of this amidase enzyme from Pseudonocardi thermophila, this is acknowledged, however not relevant to the current rejection based upon obviousness.
In response to applicants submission that most of the mutation positions identified in the present application are outside this suggested area in the enzyme, is acknowledged, and it is noted that those amino acid substitutions outside of the region of position 24 to 95 are not currently a part of this rejection.
In response to applicants submission that the substitutions identified in the present application and encompassed by the currently pending claims are explicit disclosures of amino acid positions and substitutions thereof, which are neither suggested in Watabe nor has the person skilled in the art the prospect of success only when reviewing the sequence of the wildtype enzyme, this is not found persuasive for the reasons previously stated and repeated above, one of skill in the art before the effective filing date would have been motivated to create variant amidases of the amidase enzyme having the amino acid sequence of SEQ ID NO:10, as taught by Watabe et al., as a means of identifying/creating enzymes which have improved amidase properties such as higher ammonia resistance and higher specific activities on 2-hydroxyl-4-methylthiobutylamide. One of skill in the art before the effective filing date would have been motivated to use the nucleic acid encoding the amidase of SEQ ID NO: 10 to substitute each of the amino acid residues of positions 24 to 95 as a means of identifying those variant amidases of SEQ ID NO:10 having improved properties as taught by Watabe et al. One would have been further motivated to substitute multiple amino acids at amino acids positions 24 to 95 as taught by Watabe et al. with amino acids with different reactive side chains such as S33F, S33R, S33H and S33Y as a means of altering the catalytic properties of the amidase. The expectation of success is high given the high level of skill in the art of recombinant protein engineering as exemplified by Watabe et al. and that Watabe et al. teaches all the resources and methods necessary to create such variants amidases of SEQ ID NO:10.
Thus, claim 1, 2, 3, 7, 8, 9 and 55 is/are rejected under 35 U.S.C. 103 as being unpatentable over Watabe et al., JP2006340630A (IDS of 3/17/2025, Google Translation PTO-892).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP §§ 706.02(l)(1) - 706.02(l)(3) for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1-3, 7-9, 37, 52, 55 and 64 are provisionally rejected under 35 U.S.C. 101 as claiming the same invention as that of claims 1, 3-10, 18 and 19 of copending Application No. 17/794,333 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because instant claims 1-3, 7-9, 11, 37, 52, 54-55 and 64 drawn to an enzyme for reducing the amount of acrylamide in a preparation, comprising an amino acid sequence having a sequence identity of at least 90% to the total length of an enzyme having a sequence according to SEQ ID NO. 2, wherein the amino acid sequence has, compared to SEQ ID NO. 2, at least one amino acid substitution at a position located in one of the following sequence segments of SEQ ID NO. 2: (a) Position L424 to position A507; (b) position S33 to position A74; or (c) Position G175 to position L229; wherein the amino acid sequence has, compared to SEQ ID NO. 2, at least one of the amino acid substitutions selected from positions S33, D68, A74, G175, S225, L424, G445, A453,and A507, wherein when the amino acid substitution is in position S33, then said amino acid substitution is selected from S33F, S33R, S33H, or S33Y; wherein when the amino acid substitution is in position D68, then said amino acid substitution is D68N; wherein when the amino acid substitution is in position A74, then said amino acid substitution is A74Y; anticipate and are anticipated by claims 1-10, 18 and 19 of copending Application No. 17/794,333 (reference application) drawn to an enzyme for reducing the amount of acrylamide in a preparation comprising an amino acid consensus sequence according to SEQ ID NO. 1, wherein said amino acid sequence is not a sequence according to SEQ ID NO. 2 and wherein said enzyme comprises an amino acid sequence having a sequence identity of at least 95%, 96%, 97%,98% or 99% to the total length of an enzyme having a sequence selected from the group consisting of sequences according to SEQ ID NO. 3 to SEQ ID NO.41, and wherein the amino acid sequence has: at position 33 an arginine or a tyrosine or a histidine or a phenylalanine, and/or at position 41 a tyrosine, and/or at position 68 an asparagine, and/or at position 74 a tyrosine, and/or at position 94 an isoleucine, and/or at position 175 an alanine, and/or at position 201 a phenylalanine, and/or at position 217 an arginine, and/or at position 221 a glycine, and/or at position 225 a threonine, and/or at position 229 a cysteine, and/or at position 317 an isoleucine, and/or at position 328 an arginine, and/or at position 424 a valine, and/or at position 445 an arginine or a serine, and/or at position 448 a histidine, and/or at position 453 an aspartate or a cysteine or an asparagine or a glutamine or a glutamate or a lysine or an arginine or a serine, and/or at position 454 an asparagine, and/or at position 457a glycine, and/or at position 507 a proline..
This is a provisional statutory double patenting rejection since the claims directed to the same invention have not in fact been patented.
Applicants have asked that this rejection be held in abeyance until allowable subject matter is identified.
Remarks
No claim is allowed.
Conclusion
THIS ACTION IS MADE FINAL. 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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RICHARD G HUTSON whose telephone number is (571)272-0930. The examiner can normally be reached 6-3 EST Mon-Fri.
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rgh
5/6/2026
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652
Prosecution Insights