Prosecution Insights
Last updated: April 19, 2026
Application No. 17/786,557

CLEANING COMPOSITIONS COMPRISING DISPERSINS IX

Non-Final OA §103§112
Filed
Jun 17, 2022
Examiner
NOAKES, SUZANNE MARIE
Art Unit
1656
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Henkel AG & Co. KGaA
OA Round
1 (Non-Final)
73%
Grant Probability
Favorable
1-2
OA Rounds
2y 8m
To Grant
91%
With Interview

Examiner Intelligence

Grants 73% — above average
73%
Career Allow Rate
763 granted / 1047 resolved
+12.9% vs TC avg
Strong +18% interview lift
Without
With
+18.4%
Interview Lift
resolved cases with interview
Typical timeline
2y 8m
Avg Prosecution
49 currently pending
Career history
1096
Total Applications
across all art units

Statute-Specific Performance

§101
5.6%
-34.4% vs TC avg
§103
22.8%
-17.2% vs TC avg
§102
24.2%
-15.8% vs TC avg
§112
29.5%
-10.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 1047 resolved cases

Office Action

§103 §112
DETAILED ACTION Notice of 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. Election /Restrictions Applicant's election with traverse of Group I, claims 1-12 and 15-16; and species SEQ ID NO: 24 ( mannanase Species I), SEQ ID NO: 36 ( alpha-amylase Species II), SEQ ID NO: 17 ( dispersin Species III) and (b), a solid laundry detergent (Species IV) in the reply filed on 01 October 2025 is acknowledged. The traversal is on the ground(s) that the combination of O o ehlenschlaeger et al. (US 10626354) and Cuevas et al. (US 2018016 3191) , both cited on previous PTO-892, disclose or suggest the specific mannanase variants of claim 1 . This is not found persuasive because claim 1 does not require mannanase ; rather, the claim requires a dispersin and an variant alpha-amylase or a variant mannanase or both alpha-amylase and mannanase (e.g. “and/or”) . The teachings of O o ehlenschlaeger et al. (US 10626354) and Cuevas et al. (US 20180163191) reach the limitations of the variant alpha-amylase (part III in claim 1) and the dispersin . The requirement is still deemed proper and is therefore made FINAL. Status of Application Claims 1-12 and 14-17 are pending; Claim 14 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected subject matter, there being no allowable generic or linking claim. Additionally, species SEQ ID NO: 39-41 ( mannanase ), SEQ ID NO: 37-38 (alpha-amylase) and SEQ ID NO: 1-16, 18-23 ( dispersin ) are withdrawn, as they are non-elected species. Thus, claims 1-12 and 15-17 are subject to examination on the merits. Priority The instant application is a 371 of PCT/ EP2020 / 084952 filed 07 December 2020 which claims benefit of foreign priority document DE 10 2019 135 361.0 filed 20 December 2019 is acknowledged. Said document has been received. Information Disclosure Statement The information disclosure statements (IDS) submitted on 10/01/2025, 01/13/2025, 10/08/2024, 10/07/2024, 11/08/2022 (x3) and 06/17/2022 have been considered by the examiner. See initialed and signed PTO/SB/08’s. Claim Objections Claim 6 is objected to because of the following informalities: all of the genus names in the claim should be italicized. Appropriate correction is required. Claim Rejections - 35 USC § 112(b) 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 appl icant regards as his invention. Claim s 1-12 and 15-17 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. Claims 1 and 2 both recite in part (I) for claim 1, and in the wherein clause for claim 2, that the mannanase variant comprises “two or more modifications”. In part (I) ( 1 ) /( i ) of these claims, the s e modifications are selected from one or more substitutions and the modification also requires an insertion. Thus, this minimally equals “two or more modifications”. However, in part (I) ( 2 ) /(ii) of both claims, the limitations only require “one or more modifications”, which obvious ly is less than the required “two or more”, thus, rendering the claim indefinite because of the internal inconsistency. To overcome this, it is suggested to change part (I)(2)/(ii) of the claims to recite “two or more substitutions”. Claims 3-12 and 15-17 are included as they do not remedy the noted deficiencies. Claims 1-12 and 15-17 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. It is noted, regarding part (III) of instant claim 1, it recites a substitution at “R375” and optionally at “S360”, however, there is no R/Arg at position 375 of SEQ ID NO: 1 (it is a Thr instead), rather the nearest Arg is at position 377; similarly, position 360 of instant SEQ ID NO: 36 is not “S360” (this position is instead a Tyr in SEQ ID NO: 36), rather the closest Ser is position 362. Thus, given the ambiguity the positions recited do not have antecedent basis in SEQ ID NO: 36. I t is interpreted that these are typographical errors in the claims and clarification is required . For examination purposes, the positions will be interpreted as R377 and S362. Claim s 4 and 15 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 4 is dependent upon claim 1; wherein claim 1 (iii) recites the parent amylase has R375, and optionally S 360; and at least one mutation at an amino acid residue, or residues, corresponding to an amino acid residue selected from the group consisting of N126, F153, T180, E187, and I203 relative to SEQ ID NO: 36; claim 1 (iv) recites a mutation at an amino acid residue E187 using SEQ ID NO: 36 for numbering; and at least one mutation at an amino acid residue selected from the group consisting of N126, Y150, F153, L171, T180, and 1203 . However, claim 4 is not a “further comprising” claim and recites: “a mutation at at least one residue corresponding to T38 , N126, F153, E187, I203, G476, and G477 ”. However, T38, G476 and G477 are not recited anywhere in claim 1 as residues for mutation in the alpha-amylase and thus, it is considered that claim 4 does not have antecedence for these substitutions . In addition, said additional substitutions could be construed as broader as well. Claim 15 does not remedy the noted deficiency. Claim Rejections - 35 USC § 112(a) 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 1-12 and 15-17 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. The MPEP in section 2163(I) states that the purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made/filed, of the specific subject matter claimed: To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonable conclude the inventor had possession of the claimed invention. See, e.g., Moba , B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar , 935 F.2d at 1563, 19 USPQ2d at 1116. However, a showing of possession alone does not cure the lack of a written description. Enzo Biochem , Inc. v. Gen-Probe, Inc., 323 F.3d 956, 969-70, 63 USPQ2d 1609, 1617 (Fed. Cir. 2002). For example, it is now well accepted that a satisfactory description may be found in originally-filed claims or any other portion of the originally-filed specification. See In re Koller, 613 F.2d 819, 204 USPQ 702 (CCPA 1980); In re Gardner, 475 F.2d 1389, 177 USPQ 396 (CCPA 1973); In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976). However, that does not mean that all originally-filed claims have adequate written support. The specification must still be examined to assess whether an originally-filed claim has adequate support in the written disclosure and/or the drawings. An applicant shows that the inventor was in possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997) " Further, for a broad generic claim, the specification must provide adequate written description to identify the genus of the claim. In Regents of the University of California v. Eli Lilly & Co. the court stated: "A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers , 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe , 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) ("In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus ...") Regents of the University of California v. Eli Lilly & Co. , 43 USPQ2d 1398 (Fed. Circ. 1997). MPEP § 2163 further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the sequence, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence." Furthermore, the courts have also held that p ossession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester , 358 F.3d at 927, 69 USPQ2d at 1895. The instant claims are drawn to a detergent composition comprising a dispersin , any or all dispersin except for claim 8, or those from microbial, bacterial or fungal sources. In addition, the composition also comprises a variant amylase and/or mannanase wherein the variants are unlimited in their starting sequences. They must only have mutations in positions corresponding to SEQ ID NO: 24 (for the mannanase ) or SEQ ID NO: 36 for the alpha-amylase. (It is noted, part (II) and (IV)(ii), (IV)(iii) are withdrawn species). However, this is not limiting the starting/parent sequences to SEQ ID NO: 24 and/or SEQ ID NO:36. The mutation positions need only to correspond to those is the noted sequences. In addition, the claim language for the variant mannanase and variant suggests an unlimited number of substitutions are permitted, there being no upper limit to said number of substitutions by way of numbering or percent identity to a specific sequence. Thus, the claims are drawn to enormous combination of a huge and variable genus of dispersins , in combination with huge and variable genus of alpha-amylase and/or mannanase variants. The specification, however, is limited in the suggested dispersins utilized in said cleaning composition, wherein nearly all examples utilize Terribacillus saccharophilus SEQ ID NO: 17. Further, the alpha-amylases are limited to suggested variants of SEQ ID NO: 36, 37 or 39; and the mannanase are limited to suggested variants of SEQ ID NO: 24, noting that no actual cleaning composition was ever formulated and tested comprising any of the two to three enzyme components, although the variant enzyme components are known separately in the prior art (See Ooehlenschlaeger et al. (US 10626354) and Cuevas et al. (US 20180163191), both cited on previous PTO-892 and again below) . Thus, these limited number of combinations are not representative of the entire claimed genus in terms of structure and function, with regard to (a) the diverse and unlimited dispersin , alpha-amylase and mannanase sequences; and (b) the unlimited number of substitutions, insertions, deletions, mutations also encompassed by the variant mannanase and alpha-amylases. Claim Rejections - 35 USC § 103 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 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, 4-12 and 15-17 are rejected under 35 U.S.C. 103 as being unpatentable over Ooehlenschlaeger et al. ( WO 2017186943 – cited on previous PTO-892 ) in view of Cuevas et al. (US 20180163191 – cited previous PTO-892 ). Regarding claims 1, 5-6, 8-9, 11, 16, Ooehlenschlaeger et al. teach a number of polypeptides having hexosaminidase activity and methods of using said polypeptides. Ooehlenschlaeger et al. teach one such polypeptide comprising the amino acid sequence of SEQ ID NO:10 from Terribacillus saccharophilus and its use in compositions for cleaning purposes comprising additional enzymes and cleaning components. The hexosaminidase of SEQ ID NO:10 taught by Ooehlenschlaeger et al. has 100% sequence identity to the dispersin of instant SEQ ID NO:17 (See supplemental content, 20250729_121218_us-17-786-557-17.ra i file for SEQ ID NO: 17, Result #1). Ooehlenschlaeger et al. teach cleaning compositions comprising said dispersin of SEQ ID NO:10 and an amylase or amylase variant ( See col. 28, line 66 to Col. 30, line 57 ). Regarding claim 7 , said hexosaminidase is also known as a dispersin and catalyzes the hydrolysis of β-1,6-glycosidic linkages of N-acetyl-glucosamine polymers (See Col. 3, lines 60-64 ). Regarding claim s 10 and 17 , the dispersin / hexosaminidase detergent composition comprises a concentration of at least 0.0 1 ppm , wherein the composition further comprises both non-ionic and anionic surfactants (See Col. 18, lines 60 to Col. 19, line 18 ) ; in addition, it is noted the concentration in the examples is 0.2ppm (See Exampl es 5-10 , Table 7) . Regarding claim 12 , the composition is a solid detergent composition ; and said detergent composition comprises at least said dispersin , a builder and at bleach component and can comprise additional enzymes such as proteases or peroxidases (See Col. 21, lines 6-19 ; Col. 30, line 58 to Col. 31, line 12; Col. 33, lines 58-63; Col. 50, line 38 to Col. 51, line 54 ) . Ooehlenschlaeger et al., however, do not teach the specific alpha-amylase variant such as that from Cytophaga sp. of SEQ ID NO: 36 , nor the specific concentration utilized of said amylase (instant claim 10) . Cuevas et al. teach a number of alpha amylase variants with improved properties and detergent compositions comprising said alpha amylase. Cuevas et al. specifically teach: a recombinant variant of a parent α-amylase comprising: a mutation at an amino acid residue corresponding to R377, and optionally S362; and at least one mutation, and optionally at least two mutations, at an amino acid residue, or residues, corresponding to an amino acid residue selected from the group consisting of N126, F153, T180, E187, and I203; wherein the variant α-amylase or the parent α-amylase has at least 60%, optionally 70%, optionally 80%, optionally 85%, optionally 90%, or optionally 95%, amino acid sequence identity relative to SEQ ID NO: 1, which is used for numbering; and wherein the variant has increased low pH stability and/or starch liquefaction activity, compared to the parent α-amylase or a reference α-amylase differing from the variant α-amylase only by the absence of the mutations (claim 1 , paragraph 0209 ) . Specific mutations are further taught in R377Y, and optionally S362A; and at least one mutation, and optionally at least two mutations, at an amino acid residue, or residues, corresponding to an amino acid residue selected from the group consisting of T38N, N126Y, F153W, T180H, T180D, E187P, I203Y , T129 , using SEQ ID NO: 1 for numbering (claim s1-8, 12-18 ; paragraphs 0211-0226 ). Said variant alpha-amylase further comprises deletions corresponding to R178, G179, T180 and G181; or mutations at G476, G477 (paragraph 0220) . It is noted, said SEQ ID NO: 1 is from Cytophaga and has 100% sequence identity to instant SEQ ID NO: 36 – See Supplemental Content, 20250729_123315_us-17-786-557-36.rapbm file, Duplicates for Result #1. Cuevas et al. further teach the concentration of said alpha-amylase in the detergent composition is 0.02 to 0.5 ppm (See paragraph 0457, 0460-0461). It is noted, regarding part (III) of instant claim 1, it recites a substitution at “R375” and optionally at “S360”, however, there is no R/Arg at position 375 of SEQ ID NO: 1 (it is a Thr instead), rather the nearest Arg is at position 377; similarly, position 360 of instant SEQ ID NO: 36 is not “S360” (this position is instead a Tyr in SEQ ID NO: 36), rather the closest Ser is position 362. Thus, given the ambiguity ( See the 112(b) indefiniteness rejection above ), it is interpreted that these are typographical errors in the claims and that the alpha-amylase of Cuevas et al. and the variants they are claiming are one and the same for the instant claim 1(III). It is noted, instant SEQ ID NO: 36 and SEQ ID NO: 1 of Cuevas et al. have 100% sequence identity to one another – See Supplemental Content, 20250729_123315_us-17-786-557-36.rapbm file, Duplicates for Result #1). Therefore, o ne of skill in the art before the effective filing date of the claimed invention would have been motivated to substitute the alpha amylase variant s of SEQ ID NO:1 as taught by Cuevas et al. and having a mutation at an amino acid residue corresponding to R377, and optionally S362; and at least one mutation, and optionally at least two mutations, at an amino acid residue, or residues, corresponding to an amino acid residue selected from the group consisting of T38N, N126Y, F153W, T180H, T180D, E187P, I203Y , T129 and/or deletions R178, G179, T180 and G181 as taught by Cuevas et al. in the disper s in comprising detergent composition taught by Ooehlenschlaeger et al. because said amylases have improved cleaning properties of increased low pH stability and/or starch liquefaction activity. The motivation for the use of the alpha amylase variant taught by Cuevas et al., in the dispersin cleaning compositions taught by Ooehlenschlaeger et al. comes from utilizing better alpha-amylases with improved cleaning properties. In addition, Cuevas et al. teaches their use in similar cleaning compositions. The expectation of success is high based upon the high level of skill in the art of enzymes and their uses in cleaning compositions as exemplified by each of Ooehlenschlaeger et al. and Cuevas et al. In addition, additional motivation and expectation of success comes from combining two known equivalents, utilized for the same purpose, in order to form a third combined composition: “It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art.” In re Kerkhoven , 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980) . (Claims to a process of preparing a spray-dried detergent by mixing together two conventional spray-dried detergents were held to be prima facie obvious). Claim(s) 2 and 3 are rejected under 35 U.S.C. 103 as being unpatentable over Ooehlenschlaeger et al. (WO 2017186943 – cited on previous PTO-892) in view of Cuevas et al. (US 20180163191 – cited previous PTO-892) as applied to claims 1, 4-12 and 15-17 above, and further in view of Hoekstra et al. (WO 2018085524 – cited on IDS of 06/17/2022 ) . The combined teachings of Ooehlenschlaeger et al. and Cuevas et al. are described above. Ooehlenschlaeger et al. further teach the detergent composition comprising the dispersin comprising SEQ ID NO: 10 further may comprise additional enzymes, notably an alpha-amylase and a mannanase , among other additional enzymes (See Col. 6, lines 23-48; Col. 26, lines 10-14). Ooehlenschlaeger et al. teach wash temperatures of preferably 15 to 30 o C (See Col. 54, line 57 to Col 55, line 38). Cuevas et al. further teach the alpha-amylase comprising detergent with a wash temperature of 16 o C (see paragraph 0457). However, neither Ooehlenschlaeger et al. nor Cuevas et al., alone or combined, teach a specific mannanase for use in the detergent composition. Hoekstra et al. teach a laundry detergent composition comprising one or more low temperature enzymes, wherein said enzymes are designed to provide “excellent cleaning under more environmentally friendly conditions”, and also, “provides excellent cleaning at lower temperatures and/or in shorter wash times that conventional laundry detergents. The lower wash temperature and/or shorter wash cycle conserves energy and/or water without sacrificing detergent performance. ” – See Abstract. Specifically, the laundry detergent comprises at least 0.5 or 1ppm of one or more active low temperature mannanase ; and at least 2 or 4 ppm of one or more active low temperature amylase, and/or (ii) at least 5 or 10 ppm of one or more active low temperature protease – See claim 1. It is noted, “low temperature” is to mean 16 to 20 o C (See paragraphs 0017 and 0018). The low temperature mannanase is taught as a variant of SEQ ID NO: 1, wherein said variant has one or more substitutions at positions i ) 10, 19 , 30, 38, 59, 60, 62, 63, 66, 67, 68, 70, 71, 74, 75, 78, 79, 80, 85, 97, 103, 129, 131, 135, 136, 143, 167, 168, 184, 213, 214, 225, 228, 235, 242, 244, 258, 259, 261, and 283 ; or (ii) 19, 38, 67, 85, 97, 129, 143, 168, 184, 225, 228, 235, 244, 258, and 261 (bold are overlapping substitutions; See claim 2). Regarding claims 2 and 3, specific substitutions are taught as two, three, four, five, six, seven or more variations selected from: ( i ) N/ T10Q/T , P19E/ V, A/S30T , T38E /I/L/M/Q/R/V, G/S59D/G/K/N/Q/T, L/Q60F/M/V, E/T62E/I/Q/V, K63R , I/L66C/T/V, D/H/ N67 A/ D /E/G/P/Q/S/V, A/T68L/M/R/S/W, K/R70R/V, E/N71D/H, E/N/S74E/C/Q/V, L/V75I, D/Q78A/D/L/M, N79E/F/W, H/K80Q/T, P/V85L, A/ N /S97E/L/P/Q, V103I , F/ Y129M , S/T131P, D/S135A/C/Q, A136E, D/K/Q143Q/R, F /Y 167 L/S/W/ Y , P168A/E/G/L/M/S/T, L/ Q184 D/F/H/ L /M/P, D/N213E, K/Q214C/Q, G /H 225 A/ C /P/W, T228A /G/H/I/K/S/ V /Y, A/D/ Y235 G/I/ L /Q/S/V, E/Q242S/E, K/ R/Y 244 A/C/G/ L /M/P/S, P/ S /T 258 A/ D /E/G/M/N/P/T, E/G/S259A/E/R/S/W, D/E/ N261 I/M/P/Q/ R /S/T/V/W/Y, and D/G283G/H/T; or (ii) P19E /V, T38E /I/L/M/Q/R/V, D/H/ N67 A/ D /E/G/P/Q/S/V, P/V85L, A/ N/ S 97 E/L/P/Q, F/ Y129M , D/K/Q143Q/R, P168A/E/G/L/M/S/T, L/ Q184 D/F/H/ L /M/P, G /H 225 A/ C /P/W, T228 A/G/H/I/K/S/ V /Y, A/D/ Y235 G/I/ L /Q/S/V, K /R/Y 244 A/C/G/ L /M/P/S, P/ S /T 258 A/ D /E/G/M/N/P/T, and D/E/ N261 I/M/P/Q/ R /S/T/V/W/Y of SEQ ID NO: 1 – See claim 4. In addition, instant SEQ ID NO: 24 has 100% sequence identity to SEQ ID NO: 1 of Hoekstra et al. – See Supplemental Content, 20250729_121218_us-17-786-557-24.rag , Duplicates of Result #1. Therefore it would have been obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to add the variant mannanase as taught by Hoekstra et al. to the combined laundry composition of Ooehlenschlaeger et al. and Cuevas et al. because Ooehlenschlaeger et al. suggests adding both amylases and mannanases to the dispersin laundry detergent and because Hoekstra et al. teach laundry detergents comprising variant mannanase and amylases provide “excellent cleaning under more environmentally friendly conditions”, and also, “provides excellent cleaning at lower temperatures and/or in shorter wash times that conventional laundry detergents. The lower wash temperature and/or shorter wash cycle conserves energy and/or water without sacrificing detergent performance. ” – See Abstract. This would be motivation in and of itself for one skilled in the art of laundry detergent composition creations. One skilled in the art would have a reasonable expectation of success in adding an the variant mannanase as taught by Hoekstra et al. to the combined dispersin and alpha-amylase laundry detergent of Ooehlenschlaeger et al. and Cuevas et al. because they are all utilized for the same purpose. In addition, as with above, additional motivation and expectation of success comes from the combining of two (or more) known equivalents, utilized for the same purpose, in order to form a third combined composition: “It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art.” In re Kerkhoven , 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980) . (Claims to a process of preparing a spray-dried detergent by mixing together two conventional spray-dried detergents were held to be prima facie obvious). Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT SUZANNE M NOAKES whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-2924 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F (7-4) . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Manjunath Rao can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 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 published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /SUZANNE M NOAKES/ Primary Examiner, Art Unit 1656 16 December 2025
Read full office action

Prosecution Timeline

Jun 17, 2022
Application Filed
Dec 16, 2025
Non-Final Rejection — §103, §112 (current)

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NOVEL ACETOHYDROXY ACID SYNTHASE VARIANT AND MICROORGANISM INCLUDING THE SAME
2y 5m to grant Granted Mar 31, 2026
Patent 12584156
Method for Producing Protein
2y 5m to grant Granted Mar 24, 2026
Patent 12584121
ENZYMATIC PRODUCTION OF HEXOSES
2y 5m to grant Granted Mar 24, 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
73%
Grant Probability
91%
With Interview (+18.4%)
2y 8m
Median Time to Grant
Low
PTA Risk
Based on 1047 resolved cases by this examiner. Grant probability derived from career allow rate.

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