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 .
Final Rejection
Claims 1-3, 5-6, 9, 11-14, 19-20 are pending. Claims 1, 5, 6, 9 and 13 are independent. Claims 4, 7-8, 10, and 15-18 are cancelled.
Support for Applicants amendments to exclude encapsulate is found in [0579]. Support for Applicant’s amendment to “free from bleaches” is found in [0705] of their published specification US 20220112479 A1 copied herein:
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Claim Interpretation
As per Applicant’s remarks 9/10/2025, on page 9, Examiner acknowledges claim language interpretation of “free from bleaches” is defined in Applicant’s specification [0705] is the claimed formulation may comprise bleach in total of 0.01% wt or less of bleaches, inorganic peroxide and chlorine bleaches such as sodium hypochlorite.
Response to Amendment
The rejection of claim 19 under 35 U.S.C.103 as being unpatentable over Duan et al. (WO2012169997A1) in view of Lund et al. “Correlation Between Enzyme Activity and Stability of a Protease, an Alpha-Amylase and a Lipase in a Simplified Liquid Laundry Detergent System”, Determined by Differential Scanning Calorimetry. J Surfact Deterg 15, 9–21 (2012), is withdrawn upon further consideration.
The rejection of claim(s) 1-3, 5-6, 9, 11-14, 20 under 35 U.S.C.103 as being unpatentable over Duan et al. (WO2012169997A1) in view of Lund et al. “Correlation Between Enzyme Activity and Stability of a Protease, an Alpha-Amylase and a Lipase in a Simplified Liquid Laundry Detergent System”, Determined by Differential Scanning Calorimetry. J Surfact Deterg 15, 9–21 (2012), is maintained.
The rejection of claims 1-3, 5-6, 9, 11-14, 19-20 under 35 U.S.C. 103 as being unpatentable over Lee et al. (WO2013158364A1) and Muller et al. (EP 2535401A1) or Antonio De Rose et al. (Catalysts 2017, 7, 91) is maintained.
The provisional rejection of claims 1-3, 5-6, 9, 11-14, 19-20 on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-6, 9, 11-16, 19- 20 of copending Application No. 17/281,496 is maintained.
Response to Arguments
Applicant's arguments filed 9/10/2025 have been fully considered. Applicant’s urge on page 10 of their remarks dated 9/10/2025 that Duan et al. do not teach their solution for cleaning as it is a temporary solution that is subsequently pelletized and the claims as amended exclude encapsulation. Upon careful consideration of Applicants remarks, Duan et al. is pertinent to the claim language for illustrating by example 1 combining triethyl citrate formula I with alpha-amylase and (mixing the same 2 ingredients as claimed) in solvent in their example 1, table 1 on page 5. [0011] further guide one of ordinary skill to the enzyme product being unencapsulated. While the table 1 describes the components in different sections ie core, wetting agent, enteric coating solution, and stomach disintegrative coating solution, it is the Examiner’s position that one of ordinary skill reading Duan et al. understands that this would encompass the claimed mixing because [0031] teaching the protected alpha amylase was mixed with polymers to homogeneity in the example 1. Also one of ordinary skill is guided by [0011] that the unencapsulated alpha amylases can also be used in the exemplified solution even though that embodiment is not exemplified, it is contemplated in [0011]. Duan et al. is prior art under 103 guiding one of ordinary skill to a composition of an aqueous solution of triethyl citrate with alpha-amylase (known cleaning component) as exemplified by Duan et al. making it relevant prior art for one of ordinary skill that the claimed ingredients can be combined and mixed in solution.
Further supporting Examiner’s position above, and leading to Applicant’s next argument urging that Duan et al. teach their solution in Table 1 is short lived and then becomes a pellet. In response to applicant's arguments are not persuasive because the solution described in Table 1 is a solution (wetting agent solution + enteric coating solution +stomach disintegrative solution + water) thus one of ordinary skill reading table 1 can reasonably arrive at the claimed mixing of triethyl citrate formula I with alpha-amylase in solution and furthermore [0031] explicitly teaches that the alpha amylase is mixed to homogeneity with the other ingredients in the solution and [0011] guide one of ordinary skill to use unencapsulated alpha amylase in the similar solution. Duan et al. exemplify further steps to pelletize their composition, however, with respect to the claim language, these subsequent steps of Duan et al. do not teach away from the solution mixture of Table 1 with the unencapsulated alpha amylase enzyme [0011].
On pages 11 of the remarks 9/10/2025, Applicant’s urge Lee et al. teach a triethyl acetyl citrate as a bleach activator thus, urge the composition of Lee necessarily has bleach and the claims have been amended to recite free from bleaches. In response, Applicant’s own remarks filed 9/10/2025 assert that the claim language does not exclude bleach, as made clear on page 9 of the same remarks and [0705] of their specification. Further, Lee et al. [0060] teach bleach active agent as being optional, see [0060] on page 14 teaching the active agent, when present….and listing bleach among those active agents. [0115] teach the TEAC bleach activator as one embodiment. Thus asserting that bleach is necessarily present is not convincing because the “when present” teaching guides one of ordinary skill to understand that bleach is available to be chosen but not obligatory. Further, [0100] teaches that the inclusion of oxido-reductase enzymes catalyze the formation of bleaching agents which is not excluded from the claim language to free of bleaches.
Lee et al. is pertinent to the claimed formulation because [0117] specifically guide one of ordinary skill that the liquid active agents may be solids or liquids. Lee also teach the optional encapsulation of their active ingredients [0060], thus, guiding one of ordinary skill to an option of not encapsulating as claimed. Lee et al. teach liquid [0042] coating compositions [0127] comprising triethyl citrate [0029] in [0137] detergent compositions comprising protease. Further contrary to Applicants arguments see [0028] Lee et al. teaching liquid plasticizers including the claimed triethyl citrate [0029]. Accordingly, the teachings of Lee et al. are pertinent to the claims presented for examination.
On page 10, Applicants request reconsideration of the double patenting rejection in view of the amendments. In response, both sets of claims are amended to exclude bleach and encapsulates and thus, the double patenting rejection is maintained because while the claims of 17/281,496 are not identical to the instant US 17/281,719, both sets of claims encompass the same formula (I) with a hydrolase and protease enzyme and one of ordinary skill is apprised that the claimed alpha amylase and subtilisin type protease are a type of hydrolase. Language to the at least one cleaning component does not distinguish the claims in the instant case with the copending case, because both sets of claims have enzymes which is a known cleaning component.
Thus the claim amendments. are addressed below.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim(s) 1-3, 5-6, 9, 11-14, 20 are rejected under 35 U.S.C.103 as being unpatentable over Duan et al. (WO2012169997A1) in view of Lund et al. “Correlation Between Enzyme Activity and Stability of a Protease, an Alpha-Amylase and a Lipase in a Simplified Liquid Laundry Detergent System”, Determined by Differential Scanning Calorimetry. J Surfact Deterg 15, 9–21 (2012), pdf attached.
Regarding claim 1 component (a) Duan et al. illustrate by example triethyl citrate with claim 1 component (b) alpha-amylase in an aqueous solution (component c) in their example 1, table 1 on page 5. Table 2 and [0031-0034] exemplify both the liquid and solid pellets exemplifying the solid and liquid compositions. The enzyme encompasses limitation to at least one cleaning component.
Claim 1 limitation that the formulation is free from bleaches is met by Duan et al not teaching bleach.
Claim 1 limitation to formulation is not encapsulated is met by [0011] teaching unencapsulated alpha amylase enzymes can be used in the product.
Duan et al. do not specifically teach the claim 1 component (b) specific cell lines selected from alpha-amylases (EC 3.2.1.1) and subtilisin type proteases (EC 3.4.21.62) as required claim 1. Examiner notes when reading the preamble in the context of the entire claim, the recitation to ‘cleaning formulation’ is not limiting because the body of the claim describes a complete invention and the language recited solely in the preamble does not provide any distinct definition of any of the claimed invention’s limitations. Thus, the preamble of the claim(s) is not considered a limitation and is of no significance to claim construction. See Pitney Bowes, Inc. v. Hewlett-Packard Co., 182 F.3d 1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See MPEP § 2111.02.
Lund et al. Correlation Between Enzyme Activity and Stability of a Protease, an Alpha-Amylase and a Lipase in a Simplified Liquid Laundry Detergent System, Determined by Differential Scanning Calorimetry. J Surfact Deterg 15, 9–21 (2012), pdf attached teaches that the claimed cell lines, namely, a protease (EC 3.4.21.62), an amylase (EC 3.2.1.1) along with a lipase (EC 3.1.1.3) are all commonly used detergent enzymes, chosen for their diversity in thermostability, function and considerations when formulating detergents in general. See the attached pdf page 10, right col. middle of last paragraph.
It would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to modify the alpha-amylase exemplified by Duan et al. with the claimed alpha-amylase (EC 3.2.1.1) Lund et al. teach it is commonly understood in the art that the claimed cell lines are commonly choosen for their diversity in thermostability, function and considerations when formulating detergents in general.
Regarding claim 2 wherein said enzyme preparation comprises component ( a ) in amounts in a range of 0.1 to 30 % by weight, see the table 1 guiding one of ordinary skill to 650 g of alpha amylase in a total composition of 2386 g, thus exemplifying 27% which falls within the claimed range. See table 1 on page 5.
Regarding claim 3, it is the Examiner’s position the claimed property would be met by the alpha amylase of the prior art as the commonly know alpha-amylase (EC 3.2.1.1) would inherently have the property as claimed as it is the same enzymatic cell line as being claimed.
Regarding claims 5-6 and 9 component (a) Duan et al. illustrate by example triethyl citrate with claim 1 component (b) alpha-amylase in an aqueous solution (component c) in their example 1, table 1 on page 5. Table 2 and [0031-0034] exemplify both the liquid and solid pellets exemplifying the solid and liquid compositions. The enzyme encompasses limitation to at least one cleaning component.
Claims 5-6 and 9 limitation that the formulation is free from bleaches is met by Duan et al not teaching bleach.
Claims 5-6 and 9 limitation to formulation is not encapsulated is met by [0011] teaching unencapsulated alpha amylase enzymes can be used in the product.
Claim 11 is taught in [0081] teaching source of amylase (Bacillus amyloliquefaciens vs. Bacillus subtilis) and protease with the alpha amylase is taught in the formulations I, II and II in table 2.
Regarding claim 12, Lund et al. page 12, last paragraph on the left teaches one of ordinary skill to use the prepared formulations (Tables 1, 2) at room temperature. Thus, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to arrive at the claimed temperature range as such is commonly well established in the art using the same enzymes as claimed.
Regarding claim 13, Duan et al. illustrate by example triethyl citrate for formula 1 with alpha-amylase in an aqueous solution in their example 1, table 1 on page 5. Table 2 and [0031-0034] exemplify both the liquid and solid pellets exemplifying the solid and liquid compositions. The liquid compositions of Duan et al. read upon the liquid formulation of claim 13.
Claim 14 is read upon by Lund et al. teaching the formulation is used within 30 days of preparation. See page 12 left column, last sentence.
Claim 20 is met by Lund et al. teaching enzymatic liquid laundry detergents. See title.
Claims 1-3, 5-6, 9, 11-14, 19-20 are rejected under 35 U.S.C. 103 as being unpatentable over Lee et al. (WO2013158364A1) and Muller et al. (EP 2535401A1) or Antonio De Rose et al. (Catalysts 2017, 7, 91).
Lee et al. (WO2013158364A1) teach an enzymatic gel or liquid detergent composition [0013] comprising the component (a) propane-1,2,3-tricarboxylate of formula (I), see Lee et al. teaching triethyl citrate (see page 6, [0029]) which is the same triethyl citrate compound according to claimed formula (I) as noted in Applicant’s specification USPGpub 2021/0395651 A1 page 23, [0382] regarding the synonym nomenclature of compound (a) according to formula (I) of claim 1.
The enzyme component of claim 1 is met by subtilisin proteases (see page 41,[0099-0100]) encompassing the amylases and triacylglycerol lipase (see page 36, [0093]). See also page 36, [0094] for teaching lipases from T. lanuginosa. Examiner notes that while the art may not teach the claimed cell lines by number EC 4.4.21.62, Examiner notes that the instant specification [0117] explains that the claim language to subtilisin-type (EC 4.4.21.62) may be bacterial proteases originating from a microorganism selected from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram - negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma which scope is encompassed by Lee et al. [0099].
Regarding claim 1 optional component (c), Lee et al. teach on page 48, [0128] the inclusion of a non-aqueous solvent.
Regarding the claim 1 limitation to free of bleach is met by Lee et al. [0060] guiding that the bleach active agent when present, provides functionality in an amount of at least about 1%. The “when present” language with reference to a bleach active agent in [0060] guides one of ordinary skill to an embodiment where bleach is optional.
Regarding clam 1 limitation to the formulation not encapsulated, is also met by at least the abstract teaching “Optionally, the active agent may be encapsulated. Further see [0013] teaching the liquid composition is in a water-soluble packet. It is the Examiner’s position that the liquid formulation meets the clamed composition and the water soluble packet is the dosing of the formulation.
Lee et al. do not explicitly exclude bleach and encapsulate as required by the claim 1. However, it would have been obvious to one of ordinary skill to arrive at the claimed composition free of bleach and encapsulate as required by claim 1 because Lee et al. guide one of ordinary skill to optional inclusion of bleach and teach the dosing of the claimed formulation in a water soluble packet. See [0060] and [0013].
Regarding claim 2 wherein said enzyme preparation comprises 0.1 to 30% of the propane-1,2,3-tricarboxylate by weight relative to a total weight of the enzyme preparation is taught on page 45, [0117] teaching the active agent such as the claimed enzyme [0061] can be gel or liquid as required by claim 5 and teach the amount in more than 1% to 99%. And the triethyl citrate (page 6-7, [0029] is taught in amounts of about 25-50 phr. It is the Examiner’s position that the units taught by the prior art encompass the percentage in claim 2.
Regarding claim 3 limitation to the enzyme being stabilized, see page 3, [0014] specifically addresses the combination of the power lubricant and the active agents makes up the enzyme packet and the combination of the powder lubricant described in [0059] of page 14, namely, (corn starch, potato starch, or hydroxyl ethyl starch), silicas, siloxanes, calcium carbonate, magnesium carbonate, clay, talc, silicic acid, kaolin, gypsum, zeolites, cylclodextrins, calcium stearate, zinc stearate, alumina, magnesium stearate, alumina, zinc oxide in an amount of at least about 1 wt%, or in a range of about 1 wt% to about 99 wt%) combined with an active agent encompassing the claimed component a and b in the paragraphs above, demonstrates advantageous stability if one or more of the active agents is known to be unstable in the presence of another active agent or in the presence of a component of the composition enclosed within the packet.
Regarding claim 9 and 13 method step of admixing the ingredients described herein with water to create an aqueous mixture is taught on pages 7-8, in [0032].
Regarding claim 12 fatty stains on textile, one of ordinary skill would reasonably expect oily fats from food stains and Lee specifically motivate one of ordinary skill to include the prior art mixture composition in laundry detergents. See page 51, [0137] teaching that the water-soluble packet may comprise a laundry detergent composition and a first enzyme that is unstable in the presence of a protease, and the active agent may comprise a protease enzyme. The packet, when placed in a washing machine would dissolve, releasing the detergent composition and the first enzyme. When the washing water pH is adjusted to appropriate levels the microcapsule would release the protease, thereby allowing a full dose of a first enzyme and a protease to reach a stained substrate. In an alternative embodiment, a protease may be enclosed within the packet and the active agent may comprise a second enzyme encapsulated in a microcapsule, wherein the protease would be released first and upon reaching the appropriate pH, the second enzyme would be released.
Regarding the cleaning temperature of claim 12, see page 4-5, [0022] teaching that the water-soluble film packets of the prior art have faster solubility at temperatures below about 20 °C and page 50, [0135] teaches an embodiment where the microcapsules will release the active agent upon melting, for example, Lee guide one of ordinary skill that the fabric softener would be delivered to a laundry substrate via a water-soluble packet comprising a detergent enclosed within the packet. During the wash cycle, the microcapsules would disperse onto the laundry substrate, however the fabric softener would not be released until the substrate was heated to a temperature not encountered in the clothes washer (e.g. greater than 40 °C or greater than 50 °C, or greater than 55 °C, or greater than 60 °C) but only encountered in the dryer. See [0022 and 0135] encompassing the claimed ranges in claim 12.
See also [0131] guiding one of ordinary skill to bleaches and bleach components being optional embodiments.
Regarding claims 5-6, 9, 13 Lee et al. claim 5 on page 58 teaches one of ordinary skill to mix the triacylglycerol lipase enzyme (see page 36, [0093]) with a bleach activator triethyl citrate (see page 6, [0029]) in a watersoluble enzyme packet preparation mixture for laundry detergents, bleach and laundry additives, fabric care, dishwashing, hard surface cleaning, beauty care, skin care, other personal care, and foodstuffs. See abstract and claim 5 and [0093] and [0115]. Lee et al. is silent to the enhanced storage stability of the detergent with the enzyme prep as required by claims 13-14 and the complexing agent of claim 19.
In the analogous detergent art wherein bleach components are optional embodiments [see Muller et al. (EP 2535401A1) 0037-0039], guiding one of ordinary skill to a detergent comprising triacylglycerol lipase [0013] that is stored for 19 weeks and has enhanced stability and effectiveness (see fig 3-4) at room temperature. See [0066-0067]. Also, [0002] teaches the efficacy of the stored detergent under washing conditions of less than 60OC in general. And while the higher temperature in [0002] relates to washing fibers at higher temperature and not to storing the detergent at a higher temperature, it is the Examiner’s position that one of ordinary skill would reasonably expect the triacylglycerol lipase of Lee et al. to have the claimed stability as recited in claims 13-14 and as taught by Muller et al. since one of ordinary skill understands that in the hot summers, room temperatures can get up to 37oC. Mueller et al. [0043] teach the complexing agents of claim 19.
In the alternative Antonio De Rose et al. (Catalysts 2017, 7, 91) depict in figure 7 that lipases are commonly known to be stable over 20 days at 37oC. See page 7, figure 7 of the attached pdf also depicting compositions that are bleach-free.
Lee et al., Muller et al. and Antonio De Rose et al. are considered to be analogous to the claimed invention because they are in the same field of cleaning compositions comprising the same triethyl citrate, alpha amylase, and complexing agents where bleach and encapsulation is optional.
Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to arrive at the claimed enhanced storage stability of the detergent with the enzyme prep as required by claims 5, 13-14 because Lee et al. suggest a detergent comprising a propane-1,2,3-tricarboxylate encompassing formula (I) with a triacylglycerol lipase for use in skin care, hard surface and laundry textile cleaning in general (see page 54, [0157]) and Muller et al. guide one of ordinary skill to a detergent comprising triacylglycerol lipase [0013] that is stored for 19 weeks and has enhanced stability and effectiveness (see fig 3-4) at room temperature in general. One of ordinary skill would be motivated to expect the similar triacylglycerol lipase stability as exemplified by Muller et al. at room temperature since one of ordinary skill understands in the summer, room temperatures can get upto 37oC and reading the teachings of Muller would expect similar stability since [0002] suggests effective use with the stored detergents results in effective cleaning in general and furthermore, Antonio De Rose et al. depict in figure 7 that lipases are commonly known to be stable and effective over 20 days at 37oC. See page 7, figure 7 of the attached Catalysts pdf. One of ordinary skill would be motivated to combine the teachings of Lee with Muller, Catalysts since all are in the analogous art of cleaning with enzymatic detergents with optional bleaches.
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 1-3, 5-6, 9, 11-14, 19-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 9-16, 19-20 of copending Application No. 17/281,496.
Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-3, 5-6, 9, 11-16, 19- 20 of copending Application No. 17/281,496 encompass the instant material limitations of the same formula (I) with a hydrolase and protease enzyme and one of ordinary skill is apprised that the claimed alpha amylase and subtilisin type protease are a type of hydrolase. Language to the at least one cleaning component does not distinguish the claims in the instant case with the copending case, because both sets of claims have enzymes which is a known cleaning component. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/PREETI KUMAR/Examiner, Art Unit 1761
/ANGELA C BROWN-PETTIGREW/Supervisory Patent Examiner, Art Unit 1761