Prosecution Insights
Last updated: October 02, 2026
Application No. 18/601,534

ALPHA-AMYLASE VARIANTS

Non-Final OA §102§112§DP
Filed
Mar 11, 2024
Priority
Jun 30, 2011 — EU 11172251.8 +7 more
Examiner
LEE, JAE W
Art Unit
1656
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Novozymes A/S
OA Round
1 (Non-Final)
66%
Grant Probability
Favorable
1-2
OA Rounds
9m
Est. Remaining
99%
With Interview

Examiner Intelligence

Grants 66% — above average
66%
Career Allowance Rate
277 granted / 421 resolved
+5.8% vs TC avg
Strong +39% interview lift
Without
With
+38.6%
Interview Lift
resolved cases with interview
Typical timeline
3y 4m
Avg Prosecution
39 currently pending
Career history
453
Total Applications
across all art units

Statute-Specific Performance

§101
3.8%
-36.2% vs TC avg
§103
33.2%
-6.8% vs TC avg
§102
22.3%
-17.7% vs TC avg
§112
30.9%
-9.1% vs TC avg
Black line = Tech Center average estimate • Based on career data from 421 resolved cases

Office Action

§102 §112 §DP
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 Application status Claims 1-18 and 20-21 are pending in this application. Priority This application is a DIV of 17/378,288 filed on 07/16/2021 (now PAT 12012623), which is a DIV of 16/928,207 filed on 07/14/2020 (now PAT 11091748), which is a DIV of 16/190,580 filed on 11/14/2018 (now PAT 10752889), which is a DIV of 15/218,599 filed on 07/25/2016 (now PAT 10167458), which is a DIV of 14/129,565 filed on 02/04/2014 (now PAT 9434932), which is a 371 of PCT/EP2012/062748 filed on 06/29/2012, which claims benefit of PRO 61/503,768 filed on 07/01/2011. Acknowledgment is made of applicant's claim for foreign priority under 35 U.S.C. 119(a)-(d) to a foreign patent application EP 11172251.8 filed on 06/30/2011. Election Applicant's election with traverse of Group I, Claims 1-16; and species of positions 134 and 476, and SEQ ID NO: 7 in the response filed on 03/16/2026, further comprising species election of D183* in the response filed on 06/23/2026 is acknowledged. Applicants traverse the restriction on the basis that there would not be a serious burden of examination on the examiner. Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. As stated previously, restriction for examination purposes as indicated is proper because all these inventions listed in this action are independent or distinct for the reasons given above and there would be a serious search and examination burden if restriction were not required because one or more of the following reasons apply: (a) the inventions have acquired a separate status in the art in view of their different classification; (b) the inventions have acquired a separate status in the art due to their recognized divergent subject matter; (c) the inventions require a different field of search (for example, searching different classes/subclasses or electronic resources, or employing different search queries); (d) the prior art applicable to one invention would not likely be applicable to another invention; (e) the inventions are likely to raise different non-prior art issues under 35 U.S.C. 101 and/or 35 U.S.C. 112, first paragraph. It is noted by the Examiner that all (a)-(e) applies in the instant case (italicized added emphasis). Furthermore, the Examiner notes that claims 14-16 will be withdrawn from examination on the merits because these claims recite combinations of species, i.e., G182*+D183* or D183*+G184*, which is beyond the scope of single elected species D183* which fall under the further alteration. Claims 3-9, 14-18 and 20-21 are withdrawn from further consideration by the Examiner, 37 CFR 1.142(b) as being drawn to a non-elected invention. For the reasons provided above, this restriction requirement is deemed proper, and therefore, it is made final. Information Disclosure Statement The information disclosure statement (IDS) submitted on 06/20/2025 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Claim Objections Claims 2 and 12 are objected to because of the following informalities: Applicant is advised that should claim 2 be found allowable, claim 12 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof. When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m). Appropriate correction is required. Claim Rejections - 35 U.S.C. § 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. Claims 12-13 are rejected under 35 U.S.C. § 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention. Claim 12 recites “The variant of claim 1, which comprises D134E+G476E” which is unclear and indefinite. The reason is that [1] the variant cannot be only comprised of two amino acids, and [2] the claim is missing a period after the noted phrase, which makes it unclear whether there is additional claim limitations or not. In the interest of advancing prosecution, claim 12 is interpreted as “The variant of claim 1, wherein the alterations in the variant comprises D134E+G476E.” Claim 13 recites “The variant of claim 1, which consists of D134E+G476E” which is unclear and indefinite. The reason is that [1] the variant cannot only consist of two amino acids. In the interest of advancing prosecution, claim 13 is interpreted as “The variant of claim 1, wherein the alterations in the variant consists of D134E+G476E.” Claim Rejections - 35 USC § 102 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. Claims 1-2 and 10-13 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Jackson et al. (EP2540825-A2 with effective filing date of 06/30/2011, see below sequence search result 1 and result 9 of 20260415_131634_us-18-601-534-7_134e_474e.minpct80.rag available in SCV, which has been copied/pasted below for Applicants’ convenience). The instant claims are drawn to an isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Jackson et al. teach two alpha-amylase mutants, [1] the first one comprising alterations D183*/G184*/D134E/G476E which is 100% identical to Applicants’ SEQ ID NO: 7 (see below sequence search result 1); and [2] second one having the amino acid sequence of 99.9% sequence identity to Applicants’ SEQ ID NO: 7 (see below sequence search result 9). Furthermore, Jackson et al. teach that introducing into a parent alpha-amylase D134E/G476E substitutions improved washing performance at low temperature (see para [0126] and [0137]). Therefore, teaching of Jackson et al. anticipate the claimed invention. RESULT 1 BAJ62664 (NOTE: this sequence has 4 duplicates in the database searched. See complete list at the end of this report) ID BAJ62664 standard; protein; 483 AA. XX AC BAJ62664; XX DT 28-FEB-2013 (first entry) XX DE Bacillus sp. alpha-amylase mutant D183*/G184*/D134E/G476E. XX KW Alpha-amylase; E.C 3.2.1.1; alpha-1,4-glucan-4-glucanohydrolase; mutein; KW surfactant; textile. XX OS Bacillus sp.; 722. OS Synthetic. XX FH Key Location/Qualifiers FT Misc-difference 134 FT /note= "Wild type residue Asp has been replaced by Glu" FT Misc-difference 182..184 FT /note= "Wild type GDGKA has been replaced by Gly-Lys-Ala" FT Misc-difference 474 FT /note= "Wild type residue Gly has been replaced by Glu" XX CC PN EP2540825-A2. XX CC PD 02-JAN-2013. XX CC PF 29-JUN-2012; 2012EP-00174500. XX PR 30-JUN-2011; 2011EP-00172288. XX CC PA (PROC ) PROCTER&GAMBLE CO. XX CC PI Jackson M, Andersen C, Beier L, Friis EP, Toscano MDG; CC PI Bjoernvad M, Rasmussen FW, Christiansen LS, Souter PF, Bewick LS; CC PI Kaasgaard S, Oebro J, Larsen SE, Svendsen A, Johansen AH, Skjoet M; XX DR WPI; 2013-A21617/05. XX CC PT Cleaning composition, useful as liquid laundry detergent composition and CC PT unit dose detergent composition, and for treating textile, comprises CC PT variant of parent alpha-amylase, preferably isolated variant, and CC PT cleaning adjunct. XX CC PS Claim 14; Page; 74pp; English. XX CC The present invention relates to a cleaning composition which comprises a CC variant of a parent alpha-amylase and a cleaning adjunct, preferably in CC an amount from 0.01 to 99.9 wt percent. The invention further provides a CC method of treating a surface, preferably a textile, the method comprises: CC (i) forming an aqueous wash liquor comprising water and the composition; CC (ii) treating the surface with the aqueous wash liquor preferably at a CC temperature of 40 C or less, or more preferably at a temperature of 35 C CC or less, most preferably at a temperature of 30 C or less; and (iii) CC rinsing the surface. The present sequence represents a Bacillus sp. alpha CC -amylase mutant D183*/G184*/D134E/G476E which is used in the cleaning CC composition of the invention. Note: The present sequence is not shown in CC the specification but is derived from the Bacillus sp. alpha-amylase CC sequence given in the sequence listing SEQ ID NO: 1 (see BAJ62622). XX SQ Sequence 483 AA; Query Match 100.0%; Score 2706; Length 483; Best Local Similarity 100.0%; Matches 483; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 Qy 121 EVNPNNRNQEISGEYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 EVNPNNRNQEISGEYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 Qy 181 RGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIK 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 RGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIK 240 Qy 241 YSFTRDWLTHVRNATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASN 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 YSFTRDWLTHVRNATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASN 300 Qy 301 SGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTREQG 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 SGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTREQG 360 Qy 361 YPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTTHP 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 YPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTTHP 420 Qy 421 NSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNEGSVSIW 480 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 421 NSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNEGSVSIW 480 Qy 481 VKR 483 ||| Db 481 VKR 483 RESULT 9 BAJ62688 (NOTE: this sequence has 3 duplicates in the database searched. See complete list at the end of this report) ID BAJ62688 standard; protein; 483 AA. XX AC BAJ62688; XX DT 28-FEB-2013 (first entry) XX DE Bacillus sp. alpha-amylase mutant E260K. XX KW Alpha-amylase; E.C 3.2.1.1; alpha-1,4-glucan-4-glucanohydrolase; mutein; KW surfactant; textile. XX OS Bacillus sp.; 722. OS Synthetic. XX FH Key Location/Qualifiers FT Misc-difference 258 FT /note= "Wild type residue Glu has been replaced by Lys" XX CC PN EP2540825-A2. XX CC PD 02-JAN-2013. XX CC PF 29-JUN-2012; 2012EP-00174500. XX PR 30-JUN-2011; 2011EP-00172288. XX CC PA (PROC ) PROCTER&GAMBLE CO. XX CC PI Jackson M, Andersen C, Beier L, Friis EP, Toscano MDG; CC PI Bjoernvad M, Rasmussen FW, Christiansen LS, Souter PF, Bewick LS; CC PI Kaasgaard S, Oebro J, Larsen SE, Svendsen A, Johansen AH, Skjoet M; XX DR WPI; 2013-A21617/05. XX CC PT Cleaning composition, useful as liquid laundry detergent composition and CC PT unit dose detergent composition, and for treating textile, comprises CC PT variant of parent alpha-amylase, preferably isolated variant, and CC PT cleaning adjunct. XX CC PS Example 1B; Page; 74pp; English. XX CC The present invention relates to a cleaning composition which comprises a CC variant of a parent alpha-amylase and a cleaning adjunct, preferably in CC an amount from 0.01 to 99.9 wt percent. The invention further provides a CC method of treating a surface, preferably a textile, the method comprises: CC (i) forming an aqueous wash liquor comprising water and the composition; CC (ii) treating the surface with the aqueous wash liquor preferably at a CC temperature of 40 C or less, or more preferably at a temperature of 35 C CC or less, most preferably at a temperature of 30 C or less; and (iii) CC rinsing the surface. The present sequence represents a Bacillus sp. alpha CC -amylase mutant E260K which is used in the cleaning composition of the CC invention. Note: The present sequence is not shown in the specification CC but is derived from the Bacillus sp. alpha-amylase sequence given in the CC sequence listing SEQ ID NO: 7 (see BAJ62628). XX SQ Sequence 483 AA; Query Match 99.9%; Score 2704; Length 483; Best Local Similarity 99.8%; Matches 482; Conservative 1; Mismatches 0; Indels 0; Gaps 0; Qy 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 Qy 121 EVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 EVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 Qy 181 RGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIK 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 RGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIK 240 Qy 241 YSFTRDWLTHVRNATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASN 300 |||||||||||||||||:|||||||||||||||||||||||||||||||||||||||||| Db 241 YSFTRDWLTHVRNATGKKMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASN 300 Qy 301 SGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTREQG 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 SGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTREQG 360 Qy 361 YPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTTHP 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 YPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTTHP 420 Qy 421 NSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNGGSVSIW 480 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 421 NSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNGGSVSIW 480 Qy 481 VKR 483 ||| Db 481 VKR 483 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 filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual 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/apply/applying-online/eterminal-disclaimer. Claims 1 and 10-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 11028346 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 1 of ‘346 patent: A detergent composition comprising: (i) at least one alpha amylase variant comprising modifications to amino acid positions corresponding to amino acid positions selected from the group consisting of: H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G 18 4T+N195F+V206L+K391A+P473R+G476K; H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A26 5G+K391A+P473R+G476K; H1*+N54S+V56T+K72 R+G 109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G18 2*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K; H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; and H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K of the amino acid sequence of SEQ ID NO: 1, wherein said alpha-amylase variant shares at least 85%, but less than 100% sequence identity with the amino acid sequence of SEQ ID NO: 1, and wherein said alpha-amylase variant has alpha-amylase activity; and (ii) at least one protease having protease activity, wherein said protease is selected from the group consisting of: (a) a protease having at least 85% sequence identity to the amino acid sequences of SEQ ID NOs: 2, 3, 19, 20, or 23; (b) a protease variant comprising a substitution at one or more amino acid positions corresponding to amino acid positions 171, 173, 175, 179, or 180 of the amino acid sequence of SEQ ID NO: 2, wherein said protease variant has at least 85% but less than 100% sequence identity to the amino acid sequence of SEQ ID NO: 2; (c) a protease variant comprising a modification in one or more amino acid positions corresponding to amino acid positions 32, 33, 48, 49, 50, 51, 52, 53, 54, 58, 59, 60, 61, 62, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 116, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 150, 152, 153, 154, 155, 156, 158, 159, 160, 161, 164, 169, 175, 176, 177, 178, 179, 180, 181, 182, 183, 184, 185, 186, 197, 198, 203, 204, 205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, or 216 of the amino acid sequence of SEQ ID NO: 3, (d) a protease variant comprising a substitution in one or more amino acid positions corresponding to amino acid positions 9, 15, 27, 42, 52, 55, 56, 59, 60, 66, 74, 85, 97, 99, 101, 102, 104, 116, 118, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 198, 199, 200, 203, 206, 210, 211, 212, 216, 230, 232, 239, 242, 250, 253, 255, 256, or 269, of the amino acid sequence of SEQ ID NO: 3, wherein said protease variant has at least 85% sequence identity to the amino acid sequence of SEQ ID NO: 3, and (e) a protease variant comprising a substitution in one or more amino acid positions corresponding to amino acid positions 32, 33, 49, 50, 51, 52, 53, 54, 55, 60, 61, 62, 63, 64, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 118, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 152, 154, 155, 156, 157, 158, 161, 162, 163, 167, 170, 175, 181, 187, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 203, 204, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, or 222 of the amino acid sequence of SEQ ID NO: 23, wherein said protease variant has at least 85% sequence identity to the amino acid sequence of SEQ ID NO: 23. The instant claim 1 and the claims of ‘346 differ in that claims of ‘346 patent recite specific mutant H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G18 2*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K (see boldfaced alterations). However, the instant claim 1 is open to alterations at positions 134 and 476 which overlap in scope with that of ‘346 patent. Also, the variant (SEQ ID NO: 1) of ‘346 patent has 83.5% sequence identity to Applicants’ SEQ ID NO: 1 (see below). For the reasons provided herein, claims 1 and 10-11 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. RESULT 1 Sequence Query Match 83.5%; Score 2270; DB 1; Length 485; Best Local Similarity 80.6%; Matches 391; Conservative 42; Mismatches 52; Indels 0; Gaps 0; Qy 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 ||:|||||:||||||::|||| ||||| ::| ||:| ||||||||||||||||||||||| Db 1 HHDGTNGTIMQYFEWNVPNDGQHWNRLHNNAQNLKNAGITAIWIPPAWKGTSQNDVGYGA 60 Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 |||||||||||||||||||||:::|| || :|| ||:||||||||||||||| || | || Db 61 YDLYDLGEFNQKGTVRTKYGTKAELERAIRSLKANGIQVYGDVVMNHKGGADFTERVQAV 120 Qy 121 EVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 |||| |||||:|| | ||||| |:|||||| :| |||||||||| ||||||| |||||| Db 121 EVNPQNRNQEVSGTYQIEAWTGFNFPGRGNQHSSFKWRWYHFDGTDWDQSRQLANRIYKF 180 Qy 181 RGDGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKH 240 ||||||||||||:||||||||||||||||||||:||| ||| || |||||||||:||||| Db 181 RGDGKAWDWEVDTENGNYDYLMYADVDMDHPEVINELNRWGVWYANTLNLDGFRLDAVKH 240 Qy 241 IKYSFTRDWLTHVRNATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNA 300 ||:|| |||| ||| ||| :|||||:||||||||||||:|||| | |||||||||| | Db 241 IKFSFMRDWLGHVRGQTGKNLFAVAEYWKNDLGALENYLSKTNWTMSAFDVPLHYNLYQA 300 Qy 301 SNSGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTRE 360 ||| ||||| |||||:||:|| ||||||||||:||||:|||||| |||||||| ||||| Db 301 SNSSGNYDMRNLLNGTLVQRHPSHAVTFVDNHDTQPGEALESFVQGWFKPLAYATILTRE 360 Qy 361 QGYPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTT 420 |||| ||||||||||: ||: : :|||:|:||| :||| ||||||| ::|||||||| : Db 361 QGYPQVFYGDYYGIPSDGVPSYRQQIDPLLKARQQYAYGRQHDYFDHWDVIGWTREGNAS 420 Qy 421 HPNSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNGGSVS 480 |||||||||||||||| ||||||: |||:||||:|||: |||||| ||| :| ||||||| Db 421 HPNSGLATIMSDGPGGSKWMYVGRQKAGEVWHDMTGNRSGTVTINQDGWGHFFVNGGSVS 480 Qy 481 IWVKR 485 :|||| Db 481 VWVKR 485 Claims 1 and 10-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 12258542 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 1 of ‘542 patent: A detergent composition comprising: (i) at least one alpha-amylase variant comprising modifications to amino acid positions corresponding to amino acid positions is selected from the group consisting of: H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184 T+N195F+V206L+K391A+P473R+G476K; H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265 G+K391A+P473R+G476K; H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K; H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K; H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K; and H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K, wherein said alpha-amylase variant shares at least 80% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18, and wherein said alpha-amylase variant has alpha-amylase activity; and (ii) at least one protease having protease activity, wherein said protease is selected from the group of: (a) a protease having a sequence identity of at least 85% to the sequences of SEQ ID NOs: 2, 3, 19, 20, or 23; (b) a protease variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO: 2, wherein said protease variant has a sequence identity of at least 85% but less than 100% to SEQ ID NO: 2; (c) a protease variant comprising a substitution or deletion in one or more positions corresponding to positions 32, 33, 48, 49, 50, 51, 52, 53, 54, 58, 59, 60, 61, 62, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 116, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 150, 152, 153, 154, 155, 156, 158, 159, 160, 161, 164, 169, 175, 176, 177, 178, 179, 180, 181, 182, 183, 184, 185, 186, 197, 198, 203, 204, 205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, or 216 as compared to the protease in SEQ ID NO:3, wherein said protease variant has at least 85% sequence identity to SEQ ID NO: 3, (d) a protease variant comprising a substitutions in one or more positions corresponding to positions 9, 15, 27, 42, 52, 55, 56, 59, 60, 66, 74, 85, 97, 99, 101, 102, 104, 116, 118, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 198, 199, 200, 203, 206, 210, 211, 212, 216, 230, 232, 239, 242, 250, 253, 255, 256, or 269, wherein numbering is according to SEQ ID NO: 3, wherein said protease variant has at least 85% sequence identity to SEQ ID NO: 3, and (e) a protease variant comprising a substitution in one or more positions corresponding to positions 32, 33, 49, 50, 51, 52, 53, 54, 55, 60, 61, 62, 63, 64, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 118, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 152, 154, 155, 156, 157, 158, 161, 162, 163, 167, 170, 175, 181, 187, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 203, 204, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, or 222 as compared to the protease shown in SEQ ID NO: 23, wherein said protease variant has at least 85% sequence identity to SEQ ID NO: 23. The instant claim 1 and the claims of ‘542 differ in that claims of ‘542 patent recite specific mutant H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+ G476K (see boldfaced alterations). However, the instant claim 1 is open to any alterations at positions 134 and 476 which overlap in scope with that of ‘542 patent. Also, the variant of ‘542 patent (SEQ ID NO: 1) has 83.5% sequence identity to Applicants’ SEQ ID NO: 1 (see below). For the reasons provided herein, claims 1 and 10-11 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. RESULT 1 AASEQ2_07172026_124733 Query Match 83.5%; Score 2270; DB 1; Length 485; Best Local Similarity 80.6%; Matches 391; Conservative 42; Mismatches 52; Indels 0; Gaps 0; Qy 1 HHNGTNGTMMQYFEWHLPNDGNHWNRLRDDASNLRNRGITAIWIPPAWKGTSQNDVGYGA 60 ||:|||||:||||||::|||| ||||| ::| ||:| ||||||||||||||||||||||| Db 1 HHDGTNGTIMQYFEWNVPNDGQHWNRLHNNAQNLKNAGITAIWIPPAWKGTSQNDVGYGA 60 Qy 61 YDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVVMNHKGGADATENVLAV 120 |||||||||||||||||||||:::|| || :|| ||:||||||||||||||| || | || Db 61 YDLYDLGEFNQKGTVRTKYGTKAELERAIRSLKANGIQVYGDVVMNHKGGADFTERVQAV 120 Qy 121 EVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSDFKWRWYHFDGVDWDQSRQFQNRIYKF 180 |||| |||||:|| | ||||| |:|||||| :| |||||||||| ||||||| |||||| Db 121 EVNPQNRNQEVSGTYQIEAWTGFNFPGRGNQHSSFKWRWYHFDGTDWDQSRQLANRIYKF 180 Qy 181 RGDGKAWDWEVDSENGNYDYLMYADVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKH 240 ||||||||||||:||||||||||||||||||||:||| ||| || |||||||||:||||| Db 181 RGDGKAWDWEVDTENGNYDYLMYADVDMDHPEVINELNRWGVWYANTLNLDGFRLDAVKH 240 Qy 241 IKYSFTRDWLTHVRNATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNA 300 ||:|| |||| ||| ||| :|||||:||||||||||||:|||| | |||||||||| | Db 241 IKFSFMRDWLGHVRGQTGKNLFAVAEYWKNDLGALENYLSKTNWTMSAFDVPLHYNLYQA 300 Qy 301 SNSGGNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYALILTRE 360 ||| ||||| |||||:||:|| ||||||||||:||||:|||||| |||||||| ||||| Db 301 SNSSGNYDMRNLLNGTLVQRHPSHAVTFVDNHDTQPGEALESFVQGWFKPLAYATILTRE 360 Qy 361 QGYPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDYFDHHNIIGWTREGNTT 420 |||| ||||||||||: ||: : :|||:|:||| :||| ||||||| ::|||||||| : Db 361 QGYPQVFYGDYYGIPSDGVPSYRQQIDPLLKARQQYAYGRQHDYFDHWDVIGWTREGNAS 420 Qy 421 HPNSGLATIMSDGPGGEKWMYVGQNKAGQVWHDITGNKPGTVTINADGWANFSVNGGSVS 480 |||||||||||||||| ||||||: |||:||||:|||: |||||| ||| :| ||||||| Db 421 HPNSGLATIMSDGPGGSKWMYVGRQKAGEVWHDMTGNRSGTVTINQDGWGHFFVNGGSVS 480 Qy 481 IWVKR 485 :|||| Db 481 VWVKR 485 Claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 9434932 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: Claim 1. An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claims of ‘932 patent: Claim 1. An isolated variant of a parent alpha-amylase, comprising at least two substitutions at positions corresponding to 140 and 206 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90% sequence identity with the polypeptide of SEQ ID NO: 1, and has alpha-amylase activity, and wherein the substitution at position 206 is V206Y. Claim 5. The variant of claim 1, which further comprises two or more substitutions selected from the group consisting of G304R, W140YF, W189EGT, D134E, E260GHIKNRTY, W284DFR, W439RG, G476EK, G477EKMR. The instant claim 1 and the claims of ‘932 directly overlap in scope, which recite D134E and G476E (see claim 5 of ‘932 patent), and have the ‘open’ language of “comprising” or “comprises”. For the reasons provided herein, claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. Claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-39 of U.S. Patent No. 10167458 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: Claim 1. An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claims of ‘458 patent: Claim 1. An isolated variant of a parent alpha-amylase, comprising at least two substitutions at positions corresponding to positions 206 and 476 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90%, but less than 100% sequence identity with the polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 5. The variant of claim 2, further comprises at least two substitutions at corresponding positions selected from the group consisting of G304R, W140YF, D134E, E260GHIKNRTY, W284DFR, G476EK, and G477EKMR. The instant claim 1 and the claims of ‘458 directly overlap in scope, which recite D134E and G476E (see claim 5 of ‘458 patent), and have the ‘open’ language of “comprising” or “comprises”. For the reasons provided herein, claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. Claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 10752889 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: Claim 1. An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claims of ‘889 patent: Claim 1. An isolated variant of a parent alpha-amylase, comprising at least three substitutions at positions corresponding to positions 134, 206 and 260 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90% but less than 100% sequence identity with the polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 5. The variant of claim 1, which comprises two or more (several) substitutions selected from the group consisting of G304R, W140YF, W189EGT, D134E, E260GHIKNRTY, W284DFR, W439RG, G476EK, G477EKMR. The instant claim 1 and the claims of ‘889 directly overlap in scope, which recite D134E and G476E (see claim 5 of ‘889 patent), and have the ‘open’ language of “comprising” or “comprises”. For the reasons provided herein, claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. Claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 11091748 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: Claim 1. An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claims of ‘748 patent: Claim 1. An isolated variant of a parent alpha-amylase, comprising at least two substitutions V206Y and G304R corresponding to positions 206 and 304 of the polypeptide of SEQ ID NO: 1, respectively, wherein the variant has at least 80% but less than 100% sequence identity with the polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 5. The variant according to claim 1, which comprises three or more substitutions, wherein the additional substitutions are selected from the group consisting of W140YF, W189EGT, D134E, E260GHIKNRTY, W284DFR, W439RG, G476EK and G477EKMR. The instant claim 1 and the claims of ‘748 directly overlap in scope, which recite D134E and G476E (see claim 5 of ‘748 patent), and have the ‘open’ language of “comprising” or “comprises”. For the reasons provided herein, claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. Claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-19 of U.S. Patent No. 12012623 since the claims, if allowed, would improperly extend the "right to exclude" already granted in the patent. The subject matter claimed in the instant application is fully disclosed in the patent and is covered by the patent since the patent and the application are claiming common subject matter, as follows: Claim 1 of the instant application: Claim 1. An isolated variant of a parent alpha-amylase, comprising an alteration at positions corresponding to positions 134 and 476 of the mature polypeptide of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claims of ‘623 patent: Claim 1. An isolated variant of a parent alpha-amylase, comprising at least two substitutions at positions corresponding to positions 140 and 260 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 80% but less than 100% sequence identity with the polypeptide of any of SEQ ID NOs 1, 2, 3, 4, 5, 6, 7, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Claim 5. The variant of claim 1, which further comprises at least two substitutions at corresponding positions selected from the group consisting of G304R, W189EGT, D134E, W284DFR, W439RG, G476EK, and G477EKMR. The instant claim 1 and the claims of ‘623 directly overlap in scope, which recite D134E and G476E (see claim 5 of ‘623 patent), and have the ‘open’ language of “comprising” or “comprises”. For the reasons provided herein, claims 1-2 and 10-13 are rejected on the ground of nonstatutory double patenting to prevent the unjustified or improper timewise extension of said patent. Conclusion Claims 1-2 and 10-13 are rejected for the reasons as stated above. Applicants must respond to the objections/rejections in this Office action to be fully responsive in prosecution. The instant Office action is non-final. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAE W LEE whose telephone number is (571)272-9949. The examiner can normally be reached on M-F between 9:00-6:00. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached on (571)272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /JAE W LEE/ Examiner, Art Unit 1656 /MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656
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Prosecution Timeline

Mar 11, 2024
Application Filed
Aug 11, 2026
Non-Final Rejection mailed — §102, §112, §DP (current)

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Patent 12734213
ANTIVIRAL COMPOSITIONS AND METHODS
3y 10m to grant Granted Sep 15, 2026
Patent 12735715
NOVEL PROMOTER AND USE THEREOF
2y 10m to grant Granted Sep 15, 2026
Patent 12735725
ALTERING TISSUE TROPISM OF ADENO-ASSOCIATED VIRUSES
2y 5m to grant Granted Sep 15, 2026
Patent 12703866
ENGINEERED MICROORGANISMS
3y 2m to grant Granted Aug 11, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
66%
Grant Probability
99%
With Interview (+38.6%)
3y 4m (~9m remaining)
Median Time to Grant
Low
PTA Risk
Based on 421 resolved cases by this examiner. Grant probability derived from career allowance rate.

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