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 cancellation of claims 3, 4, amendment of claims 1, 2, 5-16, in the paper of 12/8/2025, is acknowledged. Applicants' arguments filed on 12/8/2025, 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 Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.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, 2, 5-16 and 18 are still at issue and are present for examination.
Election/Restrictions
Applicant's election without traverse of the invention of Group 1, claims 1-14, to a cleaning composition, in the paper of 7/18/2025, is acknowledged.
It is acknowledged that the previous restriction requirement also required a species election from each of 7 different Species election groups. It is further acknowledged that applicants did not elect any species from any of the previous 7 Species groups, however, applicants did amend the claims to address most of the species election requirements.
Claims 15, 16 and 18 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 1, 2, 5, 6, 7, 8, 9, 10, 11-14 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 (claims 2, 5, 6, 7, 8, 9, 10, 11-14 dependent on) is indefinite in the recitation “as evidenced by” as it is unclear how this defines or relates to the claimed improved wash performance. While it is acknowledged that the alpha amylase variant must have an improved wash performance compared to the parent alpha-amylase set forth in SEQ ID NO: 2, it is unclear of applicants intent in “as evidenced by a measure of specific activity of Improvement Factor (IF) >1.0”. Is the “measure of specific activity of Improvement Factor (IF) >1.0” an actual limitation of the claimed alpha amylase variant as to the specific “improved wash performance” or is it just to “evidence” the improved wash performance.
Appropriate correction and/or comment is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim(s) 1, 2, 5, 6, 7, 8, 9, 10, 11-14 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
This rejection was stated in the previous office action as it applied to previous claims 1-14. In response to the rejection applicants have amended the claims and traverse the rejection as it applies to the newly amended claims.
Claim(s) 1, 2, 5, 6, 7, 8, 9, 10, 11-14 are directed to all possible leaning composition comprising: (i) an alpha-amylase variant of a parent alpha-amylase, wherein said variant the variant comprises: (a)_a modification at position 7 selected from G7A, G7S, and G7H, deletions corresponding to R180* and S181*, and optionally a modification at one or more positions corresponding to positions: 1, 2, 3, 26, 31, 37, 40, 41, 54, 56, 60, 63, 72, 73, 93, 94, 98, 103, 104, 105, 106, 109, 110, 111, 113, 114, 116, 117, 118, 123, 126, 128, 131, 132, 134, 135, 136, 137, 138, 140, 142, 144, 146, 151, 152, 155, 159, 160, 165, 167, 169, 172, 173, 174, 176, 177, 178, 182, 183, 185, 188, 189, 193, 194, 196, 202, 203, 205, 224, 225, 242, 243, 244, 252, 256, 258, 259, 260, 261, 266, 276, 279, 280, 283, 286, 302, 303, 315, 320, 321, 322, 323, 346, 354, 359, 360, 361, 362, 365, 371, 383, 390, 394, 395, 405, 409, 414, 420, 422, 427, 455, 457, 458, 470, 472, 473, 474, 475 and 476,
Applicants Response:
Applicants traverse the rejection on the basis that applicants submit that claim 1 recites a particular structure for the claimed variants. Applicants submit that claim 1 recites the variant comprises a modification at position 7 selected from G7A, G7S, and G7H, and deletions corresponding to R180* and S181* relative to the amino acid positions set forth in SEQ ID NO: 1 and that claim 1 further defines the parent alpha-amylase as having the amino acid sequence set forth in SEQ ID NO: 2. Applicants submit that accordingly, claim 1 and its dependents as set forth herein satisfy the requirements of written description.
Applicants submit that it is noted that the specification describes hundreds of representative species of the claimed amylase variants at least in Example 4, Table 2 (page 649-689) of the specification as filed.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered, however, is not found persuasive for the reasons previously stated and for those reasons repeated herein.
As stated above, the rejected claims are directed to all possible cleaning composition comprising: (i) an alpha-amylase variant of a parent alpha-amylase, wherein said variant the variant comprises: (a)_a modification at position 7 selected from G7A, G7S, and G7H, deletions corresponding to R180* and S181*, and optionally a modification at one or more positions corresponding to positions: 1, 2, 3, 26, 31, 37, 40, 41, 54, 56, 60, 63, 72, 73, 93, 94, 98, 103, 104, 105, 106, 109, 110, 111, 113, 114, 116, 117, 118, 123, 126, 128, 131, 132, 134, 135, 136, 137, 138, 140, 142, 144, 146, 151, 152, 155, 159, 160, 165, 167, 169, 172, 173, 174, 176, 177, 178, 182, 183, 185, 188, 189, 193, 194, 196, 202, 203, 205, 224, 225, 242, 243, 244, 252, 256, 258, 259, 260, 261, 266, 276, 279, 280, 283, 286, 302, 303, 315, 320, 321, 322, 323, 346, 354, 359, 360, 361, 362, 365, 371, 383, 390, 394, 395, 405, 409, 414, 420, 422, 427, 455, 457, 458, 470, 472, 473, 474, 475 and 476,
In response to applicants submission that claim 1 recites the variant comprises a modification at position 7 selected from G7A, G7S, and G7H, and deletions corresponding to R180* and S181* relative to the amino acid positions set forth in SEQ ID NO: 1 and that claim 1 further defines the parent alpha-amylase as having the amino acid sequence set forth in SEQ ID NO: 2, this is not found persuasive because while applicants claim may be limited to a few modifications relative to SEQ ID NO:1( G7a, G7S, G7H and deletions corresponding to R180* and S181*, these modifications are not limited with regard to the extreme breadth of the background alpha amylase in which these modifications occur (i.e. any alpha amylase having a mere 60% sequence identity to the amino acid sequence set forth in SEQ ID NO:2.
The submitted species is not sufficiently representative of the extreme breadth of those alpha amylase variants encompassed by applicants claims including any alpha amylase having a mere 60% sequence identity to SEQ ID NO:2 and a G7A modification and deletions corresponding to R180* and S181*, encompassed by these claims. There is no disclosure of any particular structure to function/activity relationship in the disclosed species. The specification also fails to describe sufficient representative species of these amylase variants by any identifying structural characteristics or properties, for which no predictability of structure is apparent.
Given this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 1, 2, 5, 6, 7, 8, 9, 11-14 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Novozymes WO 2018/141707 as evidenced by Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998)..
A similar rejection was stated in the previous office action as it applied to previous claims 1-6, 11, 12-14,. In response applicants have amended the claims and traverse the rejection as it applies to the amended claims. The previous rejection is slightly altered because of applicants amendment is repeated herein.
Novozymes WO 2018/141707 discloses alpha amylase variants with improved wash performance compared to a parent alpha amylase (paragraphs [0008], [0043]; claim 13; sequence 1) and their use in cleaning/detergent compositions. It is noted that the parent enzyme used in Novozymes WO 2018/141707 is the SP722 amylase which also may be used as reference amylase in the present application as SEQ ID NO:3. However it is noted that the way applicants have crafted their claim there is no structural limitations of the referenced “parent alpha-amylase:. Novozymes WO 2018/141707 discloses variants of SEQ ID NO:1 (of Novozymes WO 2018/141707) that comprise a modification G7A of SEQ ID NO:1. It is noted that SEQ ID NO:1 (of Novozymes WO 2018/141707) has greater than 95% sequence identity to instant SEQ ID NO:2 (claims 1-4, 11 and 12). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications and additional positions such as H323N (pg. 25 of Novozymes WO 2018/141707) (claims 5-7). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181 +182 as per WO 96/23873 or 183+184 of SP07 (SEQ ID NO:7 of WO 96/23873) (pg. 1, lines 28-35). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181, 182, 183 and 184 (see claim 21 and supporting text). Novozymes WO 2018/141707 additionally disclose cleaning compositions comprising the above modifications and additional enzymes such as proteases or cellulases in liquid form (claims 13 and 14).
Applicants Response
Applicants traverse this rejection on the basis that applicants submit that Novozymes fails to teach or suggest deletions corresponding to R180* and S181 relative to SEQ ID NO:1.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered, however, is not found persuasive for the reasons previously stated and for those reasons repeated herein.
As stated above, given Novozymes WO 2018/141707 disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181 +182 as per WO 96/23873 or 183+184 of SP07 (SEQ ID NO:7 of WO 96/23873) (pg. 1, lines 28-35). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181, 182, 183 and 184 (see claim 21 and supporting text). The taught deletion of position Gly 182 taught by Novozymes corresponds to S181 of instant SEQ ID NO:1. This is evidenced by Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998) who teach the amino acid sequence alignment of regions including the above Arg-Gly residues between different Bacillus species including BLA (Bacillus licheniformis), BAA (Bacillus amyloliquefaciens), BSA (Bacillus stearothermophilus) and LAMY (Bacillus KSM-1378) (see page 373, Figure 2 and supporting text). This evidences that Arg 181 and Gly182 of Novozymes WO 2018/141707 corresponds to Arg 180 and Gly181 of instant SEQ ID NO:1.
Thus, claim(s) 1, 2, 5, 6, 7, 8, 9, 11-14 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Novozymes WO 2018/141707.
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.
Claim(s) 1, 2, 5, 6, 7, 8, 9, 11-14 is/are rejected under 35 U.S.C. 103 as being unpatentable over Novozymes WO 2018/141707 and Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998).
A similar rejection was stated in the previous office action as it applied to previous claims 7, 8 and 9. In response applicants have amended the claims and traverse the rejection as it applies to the amended claims, similar to previous claims 7, 8 and 9. The previous rejection is slightly altered because of applicants amendment is repeated herein.
Novozymes WO 2018/141707 discloses alpha amylase variants with improved wash performance compared to a parent alpha amylase (paragraphs [0008], [0043]; claim 13; sequence 1) and their use in cleaning/detergent compositions. It is noted that the parent enzyme used in Novozymes WO 2018/141707 is the SP722 amylase which also may be used as reference amylase in the present application as SEQ ID NO:3. However it is noted that the way applicants have crafted their claim there is no structural limitations of the referenced “parent alpha-amylase”. Novozymes WO 2018/141707 discloses variants of SEQ ID NO:1 (of Novozymes WO 2018/141707) that comprise a modification G7A of SEQ ID NO:1. It is noted that SEQ ID NO:1 (of Novozymes WO 2018/141707) has greater than 95% sequence identity to instant SEQ ID NO:2 (claims 1-4, 11 and 12). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications and additional positions such as H323N and the deletion of position H1 (pg. 25 of Novozymes WO 2018/141707 and Table 10 and supporting text) (claims 5-7). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181 +182 as per WO 96/23873 or 183+184 of SP07 (SEQ ID NO:7 of WO 96/23873) (pg. 1, lines 28-35). Novozymes WO 2018/141707 further disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181, 182, 183 and 184 (see claim 21 and supporting text). Novozymes WO 2018/141707 additionally disclose cleaning compositions comprising the above modifications and additional enzymes such as proteases or cellulases in liquid form (claims 13 and 14).
Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998) disclose that the deletion of an arginine181-glycine182 residues improves the thermostability of a Bacillus a-amylase (EC 3.2.1.1) and this is caused by enhanced calcium binding. Igarashi et al. disclose that the deletion of the arginine181-glycine182 residues also increased pH stability and resistance to sodium dodecyl sulfate and chelating agents such as EDTA. Igarashi et al. further teach the amino acid sequence alignment of regions including the above Arg-Gly residues between different Bacillus species including BLA (Bacillus licheniformis), BAA (Bacillus amyloliquefaciens), BSA (Bacillus stearothermophilus) and LAMY (Bacillus KSM-1378) (see page 373, Figure 2 and supporting text).
One of ordinary skill in the art before the effective filing date would have been motivated to make the same deletions taught by Igarashi et al. in the alpha-amylase taught by Novozymes WO 2018/141707 as a means of increasing the thermostability and ph stability for use in cleaning compositions. The obvious deletions taught by Igarahi et al. include those listed in Figure 2 as corresponding to the arginine181-glycine182 of the LAMY alpha amylase as taught by Igarahi et al. These corresponding deletions are R181 and S182 of the alpha amylase taught by Novozymes WO 2018/141707. One would have been further motivated to additionally delete positions 182 and 183 as thought by Novozymes WO 2018/141707. The motivation for such is that such an increase in the thermostability and ph stability would lead to a longer lasting better cleaning composition. The expectation of success is high based upon the high level of skill in the art with regard to recombinant protein engineering as exemplified by Igarashi et al. and Novozymes WO 2018/141707.
Applicants Response
Applicants traverse the rejection on the basis that applicants have amended the claims and applicants submit that neither Novozymes nor Igarashi, alone or in combination, teaches all elements of independent claim 1. Applicants submit that the references at least fail to teach or suggest an alpha-amylase variant comprising deletions corresponding to R180* and S181*, relative to the positions of the amino acid sequence set forth in SEQ ID NO: 1.
Applicants submit that while Novozymes may disclose the deletion of amino acids 181+182 or amino acids 183+184, relative to the amino acid positions of Novozymes SEQ ID NO: 1, the reference fails to disclose deletions corresponding to R180* and S181* as claimed herein. Applicants submit that rather, Novozymes teaches an arginine (R) residue at position 181 and a glycine (G) residue at position 182, relative to Novozymes SEQ ID NO: 1. Applicants submit that Novozymes teaches an aspartic acid (D) residue at position 183 and a further glycine (G) residue at position 184.
Applicants submit that Novozymes is silent with respect to any modification or deletion whatsoever at position 180 and teaches different residues as being present at positions 180 and 181 (phenylalanine (F) instead of the claimed arginine (R) at position 180; and arginine (R) instead of the claimed serine (S) at position 181. Applicants submit that Igarashi fails to cure the deficiencies of Novozymes.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered, however, is not found persuasive for the reasons previously stated and for those reasons repeated herein.
As stated above, given the teaching of Novozymes WO 2018/141707 and Igarahi et al., one of ordinary skill in the art before the effective filing date would have been motivated to make the same deletions taught by Igarashi et al. in the alpha-amylase taught by Novozymes WO 2018/141707 as a means of increasing the thermostability and ph stability for use in cleaning compositions. The obvious deletions taught by Igarahi et al. include those listed in Figure 2 as corresponding to the arginine181-glycine182 of the LAMY alpha amylase as taught by Igarahi et al. These corresponding deletions are R181 and S182 of the alpha amylase taught by Novozymes WO 2018/141707. One would have been further motivated to additionally delete positions 182 and 183 as thought by Novozymes WO 2018/141707. The motivation for such is that such an increase in the thermostability and ph stability would lead to a longer lasting better cleaning composition. The expectation of success is high based upon the high level of skill in the art with regard to recombinant protein engineering as exemplified by Igarashi et al. and Novozymes WO 2018/141707.
In response to applicants submission that the references fail to teach or suggest an alpha-amylase variant comprising deletions corresponding to R180* and S181*, relative to the positions of the amino acid sequence set forth in SEQ ID NO: 1, this is not found persuasive on the basis that as stated previously and above, Novozymes WO 2018/141707 disclose the above variant alpha amylases comprising additional modifications including deleting amino acids 181 +182 as per WO 96/23873 or 183+184 of SP07 (SEQ ID NO:7 of WO 96/23873) (pg. 1, lines 28-35). Further as stated above, Igarashi et al. disclose that the deletion of the arginine181-glycine182 residues also increased pH stability and resistance to sodium dodecyl sulfate and chelating agents such as EDTA. Igarashi et al. further teach the amino acid sequence alignment of regions including the above Arg-Gly residues between different Bacillus species including BLA (Bacillus licheniformis), BAA (Bacillus amyloliquefaciens), BSA (Bacillus stearothermophilus) and LAMY (Bacillus KSM-1378) (see page 373, Figure 2 and supporting text). Igarashi et al. further teach that while positions 181 and 182 are arginine and glycine, these same identified residues may occur at slightly different positions in other Bacillus alpha amylases. Further Igarashi et al. that the second amino acid of interest may not always be a glycine such as in the case of the BLA alpha amylase (See alignment of Figure 2 of Igarashi et al. and supporting text). An alignment SEQ ID NO:1 of Novozymes with those alpha amylases of figure 2 in . Igarashi et al. show that the G181 of SEQ ID NO:1 of Novozymes corresponds to S181 of instant SEQ ID NO:1.
In response to applicants additional submission that Novozymes teaches an aspartic acid (D) residue at position 183 and a further glycine (G) residue at position 184, these are the same as those positions found in instant SEQ ID NO:1, further supporting the identification of the region of interest as identified by Igarashi et al. in the alignment in Figure 2 of Igarashi et al.
Thus claim(s) 1, 2, 5, 6, 7, 8, 9, 11-14 is/are rejected under 35 U.S.C. 103 as being unpatentable over Novozymes WO 2018/141707 and Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The 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, 2, 5, 6, 7, 8, 9, 10, 11-14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 16-29 of copending Application No. 17/781,512 in view Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998). Although the claims at issue are not identical, they are not patentably distinct from each other because 16-29 of copending Application No. 17/781,512, drawn to an alpha-amylase variant of a parent alpha-amylase, wherein said variant comprises a modification at one or more position corresponding to positions: 118 using SEQ ID NO: 1 for numbering, and wherein the said variant has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100% sequence identity to the SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 or 14 and wherein said variant has an improved performance, such as an improved wash performance for a measure of specific activity of Improvement Factor (IF) >1.0, when compared to said parent polypeptide, preferably SEQ ID NO: 2 or 3, in view of Igarashi et al. (Biochemical and Biophysical Research Communications, Vol 248, pp 372-377, 1998) for the reasons discussed above anticipate/make obvious instant claims 1-14 drawn to a cleaning composition comprising: (i) an alpha-amylase variant of a parent alpha-amylase, wherein said variant comprises a modification at position 7, and wherein the said variant has at least 60% but less than 100% sequence identity to the SEQ ID NO: 2 and wherein said variant has an improved performance, optionally an improved wash performance, for a measure of specific activity of Improvement Factor (IF) >1.0, when compared to said parent alpha-amylase; and (ii) a cleaning adjunct.
This is a provisional nonstatutory double patenting rejection.
Applicants submit that the claims as set for the herein are distinguishable from those of the 512 application such that the rejection is overcome. This is not found persuasive for the reasons stated previously and repeated above;
Remarks
No claim is allowed.
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 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 on 6-3 EST Mon-Fri.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached on (571) 272-0956. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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rgh
1/28/2026
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652