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
1. Amendment and response filed 7/20/26 to Office Action mailed 4/29/26 is acknowledged.
2. Applicant's amendment and arguments filed 7/20/26 have been fully considered but they are not deemed to be persuasive. The reasons are discussed following the rejection(s).
3. Any objection or rejection of record which is not expressly repeated in this Office Action has been overcome by Applicant’s response and withdrawn.
4. Claims 14-24 are present and under consideration.
5. Claims 14-23 rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for: A method for cleaning a subject, comprising contacting a lipid stain present on the subject to be cleaned with a detergent composition comprising a variant of a parent lipase which variant has lipase activity, has at least 90% but less than 100% sequence identity with SEQ ID NO: 2, and comprises an asparagine (N) at position 33 corresponding to SEQ ID NO: 2, [[and]] comprises substitutions at positions corresponding to T231R+N233R and at least one or more of D96E, D111A, D254S, G163K, P256T, G91T and G38A of SEQ ID NO: 2, and wherein the variant has improved storage stability as compared to an otherwise identical variant that does not comprise said substitutions., does not reasonably provide enablement for: A method for cleaning a subject, comprising contacting a lipid stain present on the subject to be cleaned with a detergent composition comprising a variant of a parent lipase which variant has lipase activity, has at least 60% but less than 100% sequence identity with SEQ ID NO: 2, and comprises substitutions at positions corresponding to T231R+N233R and at least one or more of D96E, D111A, D254S, G163K, P256T, G91T and G38A of SEQ ID NO: 2.
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Claims 14-23 are so broad as to encompass a method for cleaning a subject, comprising contacting a lipid stain present on the subject to be cleaned with a detergent composition comprising a variant of a parent lipase which variant has lipase activity, has at least 60% but less than 100% sequence identity with SEQ ID NO: 2, and comprising substitutions at positions noted above. The scope of the claims is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of variant lipases broadly encompassed by the claims. Since the amino acid sequence of a protein determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. However, in this case the disclosure is limited to variant lipases having a small number of mutations (2-11) of SEQ ID NO: 2.
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass a detergent composition comprising any variant lipase having at least 60-100% identity to SEQ ID NO:2 as noted above because the specification does not establish: (A) regions of the protein structure which may be multiply modified without effecting lipase activity; (B) the general tolerance of lipases to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any lipase residues with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including a method for cleaning a subject, comprising contacting a lipid stain present on the subject to be cleaned with a detergent composition comprising a variant of a parent lipase which variant has lipase activity, has at least 60% but less than 100% sequence identity with SEQ ID NO: 2 and comprising substitutions at positions noted above. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of lipases having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
6. 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.
Claim(s) 14-24 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Svendsen et al. (WO 2008/079685).
Svendsen et al. teach compositions of Humicola lanuginosa lipase variants wherein the lipase variants comprise the substitutions D96E, T231R and N233R (page 3) and have increased stability at pH3 and/or pH6 (page 8). Svendsen et al. teach lipase variants including D27R/N33Q/G91A/D96E/L97Q/D111A/T231R/N233R/P256T (LVA012), N33Q/E87K/D96E/T231R/N233R (LVAR0086), D27S/N33Q/G91A/D96E/L97Q/D111A/S216P/T231R/N233R/P256T (LVA089), D27R/N33Q/G91A/D96E/L97Q/D111A/S216P/L227G/T231R/N233R/P256T (LVA210), D27R/N33Q/G91A/D96E/L97Q/D111A/S216P/T231R/N233R/P256T (LVA211), D27R/N33Q/G91A/D96E/D111A/T231R/N233R/D254G/P256T (LVA238), D27R/N33Q/G91T/D96E/D111A/T231R/N233R/D254S/P256T (LVA480), D27R/N33Q/G38A/G91T/D96E/D111A/G163K/T231R/N233R/D254S/P256T (LVA808), D27R/N33Q/G38A/G91T/D96E/D111A/G163A/T231R/N233R/D254S/P256T (LVA811), D27R/N33Q/G38A/G91T/D96E/L97Q/D111A/T231R/N233R/D254S/P256T (LVA842) as well as others which include the D96E, T231R and N233R substitutions (see Examples). The compositions of Svendsen et al. can include a protease and/or amylase (page 3), a surfactant (page 67) and can be formulated as a gel, a powder, a tablet which can be coated with one or more layers, or a liquid (pages 64-65). While the compositions of Svendsen et al. are disclosed as pharmaceutical compositions while the claims herein recite detergent compositions or laundry, dishwashing, personal care, or hard surface cleaning compositions and a method use, these recitations do not distinguish the compositions of Svendsen et al. from those of the instant claims as they merely recite the intended use of the composition and thus are given no patentable weight. The specification herein does not define a detergent composition (or a laundry, dishwashing, personal care, or hard surface cleaning composition) as including any particular components not present in the compositions of Svendsen et al. As such the compositions of Svendsen et al. anticipate the instant compositions.
While as discussed above the recitations of “detergent composition” in the instant claims are not given patentable weight, if one assumes these recitations imply the presence of one or more components not present in the compositions of Svendsen et al., the following obviousness rejection would still apply.
7. 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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim 14-24 is/are rejected under 35 U.S.C. 103 as being unpatentable over Souter et al. (US 2009/0217464) in view of Svendsen et al. (WO 2008/079685).
Souter et al. teach detergent compositions of Humicola lanuginosa lipase variants wherein the lipase variants comprise the substitutions T231R and N233R [0057] and have increased detergent stability [0004]. The compositions can comprise additional enzymes [0086], a surfactant [0092], can be formulated as laundry detergents or dishwashing detergents [0089] and can be formulated as a gel, a powder, a tablet which, or a liquid [0089] in a method of cleaning a subject. Souter et al. does not disclose compositions of a lipase variant comprising all of D96E, T231R and N233R substitutions.
Svendsen et al. is discussed above and discloses Humicola lanuginosa lipase variants wherein the lipase variants comprise the substitutions D96E, T231R and N233R (page 3).
As Souter et al. teach the use of Humicola lanuginosa lipase variants wherein the lipase variants comprise the substitutions T231R and N233R in detergent compositions and as Svendsen et al. teach additional Humicola lanuginosa lipase variants comprising the T231R and N233R as well as many other additional substitutions in common, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to use the numerous Humicola lanuginosa lipase variants of Svendsen et al. (as noted in paragraph 6) and comprising at least the D96E, T231R and N233R substitutions in the detergent compositions of Souter et al., and use in a method for cleaning a subject, comprising contacting a lipid stain present on the subject to be cleaned with the composition according to claim 1. One skilled in the art would have been motivated in view of the importance of lipases as biocatalysts which have shown to be useful for various applications such as in cleaning methods. Thus, the claimed invention was within the ordinary skill in the art to make and use at the time was made and was as a whole, prima facie obvious.
8. Double patenting rejection
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP §§ 706.02(l)(1) - 706.02(l)(3) for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 14-24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11-15 of US Patent 10,457,920. An obviousness-type double patenting rejection is appropriate where the conflicting claims are not identical, but an examined application claim not is patentably distinct from the reference claim(s) because the examined 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). Although the conflicting claims are not identical, they are not patentably distinct from each other. Claims 1-13 herein and claims 11-15 of US Patent 10,457,920 are both directed to detergent compositions comprising Humicola lanuginosa lipase variants wherein the lipase variants comprise the substitutions T231R and N233R. The claims differ in that claims 14-23 herein recite “a method of cleaning a subject using detergent compositions of any physical form with lipase variants wherein the lipase variants comprise the substitutions G38A, T231R and N233R whereas claims 11-15 of US Patent 10,457,920 recite compositions of a particular physical form i.e., a water-soluble film comprising the lipase variant and encapsulating a surfactant and/or builder, wherein the variants recited encompass those having G38A, T231R and N233R substitutions and variants having the T231R and N233R substitutions in the absence of a G38A substitution. The portion of the specification in US Patent 10,457,920 that supports the recited lipase variants includes – and provides a water-soluble film and a detergent pouch comprising a lipase as disclosed which have improved lipolytic stability and which may be employed in the method of cleaning a subject. The compositions of the invention may be used in laundry and dish wash cleaning compositions and applications, lipase variants that comprise the substitutions G38A, T231R and N233R and the numerous other variants disclosed that would anticipate claims 14-24 herein. Claims 14-24 herein cannot be considered patentably distinct over claims 11-15 of US Patent 10,457,920 when there is a specifically recited embodiment that would anticipate claims 14-24 herein. Alternatively, claims 14-24 herein cannot be considered patentably distinct over claims 11-15 of US Patent 10,457,920 when there is a specifically disclosed embodiment in the copending application that supports claims 11-15 of that patent and falls within the scope of claims 14-23 herein because it would have been obvious to one having ordinary skill in the art to modify the detergent pouch of claims 11-15 of US Patent 10,457,920 by selecting a specifically disclosed embodiment (i.e. a lipase variant comprising the substitutions G38A, T231R and N233R – among others) that supports that claim. One having ordinary skill in the art would have been motivated to do this because that embodiment is disclosed as being a preferred embodiment within claims 11-15 of US Patent 10,457,920.
9. Claims 14-24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 9 of US Patent 11,312,946.
US Patent 11,312,946 claims 9 and claims 1-8 & 10-17 are drawn to as follows:
9. A method for cleaning an object, comprising contacting a lipid stain present on the object to be cleaned with the composition according to claim 1.
1. A detergent composition comprising a variant of a parent lipase, wherein the variant has lipase activity, has at least 90% but less than 100% sequence identity with SEQ ID NO: 2, has an asparagine (N) corresponding to position 33 of SEQ ID NO: 2, and comprises amino acid substitutions at positions corresponding to G38A+T231R+N233R of SEQ ID NO: 2, wherein the variant has improved storage stability as compared to an otherwise identical variant that has a glycine(G) at position 38.
2. The composition of claim 1 further comprising substitutions at the position corresponding to D27R of SEQ ID NO: 2.
3. The composition of claim 1, further comprising one or more enzymes selected from: hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, chlorophyllases, amylases, or mixtures thereof.
4. The composition of claim 3, wherein the storage stability is in the presence of protease and surfactants, and wherein the storage stability is increased as compared to the storage stability of the parent lipase in the presence of the same protease and surfactants.
5. The composition of claim 1, further comprising at least one surfactant, at least one surfactant system, at least one soap, or any mixtures thereof.
6. The composition of claim 1, wherein the composition is a laundry cleaning composition, a dishwashing cleaning composition, a hard-surface cleaning composition or a personal care cleaning composition.
7. The composition of claim 1, wherein the composition is formulated as a regular, compact or concentrated liquid; a gel; a paste; a soap bar; a regular or a compacted powder; a granulated solid; a homogenous or a multilayer tablet with two or more layers (same or different phases); a pouch having one or more compartments; a single or a multi-compartment unit dose form; or any combination thereof.
8. A method of producing the composition according to claim 1, comprising combining a variant of a parent lipase and a surfactant, wherein said variant has lipase activity, has at least 90% but less than 100% sequence identity with SEQ ID NO: 2, comprises amino acid substitutions at positions corresponding to G38A+T231R+N233R of SEQ ID NO: 2, and comprises an asparagine (N) at position 33.
9. A method for cleaning an object, comprising contacting a lipid stain present on the object to be cleaned with the composition according to claim 1.
10. A variant of a parent lipase, wherein the variant has lipase activity, has at least 90% but less than 100% sequence identity with SEQ ID NO: 2, has an asparaqine (N) corresponding to position 33 of SEQ ID NO: 2, and comprises amino acid substitutions at positions corresponding to G38A+T231R+N233R, wherein the variant has improved storage stability as compared to an otherwise identical variant that has a glycine (G) at position 38.
11. The variant of claim 10, wherein said variant has increased storage stability in the presence of surfactant and protease, and wherein the storage stability is increased as compared to the storage stability of the parent lipase in the presence of the same detergent components.
12. The composition of claim 1, wherein said variant has at least 95% but less than 100% sequence identity with SEQ ID NO: 2.
13. The variant of claim 10, wherein said variant has at least 95% but less than 100% sequence identity with SEQ ID NO: 2.
14. The composition of claim 1, wherein the variant in comparison with the parent lipase has increased storage stability in the presence of detergents D001 or D002.
15. The composition of claim 1, wherein the variant has a storage stability half-life improvement factor above 2.0 as compared to an otherwise identical variant that has a G at position 38.
16. The composition of claim 1, wherein the variant has a storage stability half-life improvement factor above 1.5 as compared to an otherwise identical variant that has a G at position 38.
17. The variant of claim 10, wherein the variant is selected from the following: a)-D27R G38A G91T D96E D111A G163K T231R N233R D254S P256T; b) D27R G38A G91T D96E D111A G163K T231R N233R D254S; c) D27R G38A G91T D96E G163K T231R N233R D254S P256T; d) D27R G38A D96E D111A G163K T231R N233R D254S P256T; e) D27R G38A D96E G163K T231R N233R D254S P256T; f) D27R G38A D96E D111A G163K T231R N233R D254S P256T; g) D27R G38A D96E D111A G163K E210Q T231R N233R D254S P256T; or h) G38A D96E D111A T231R N233R.
Applicants’ SEQ ID NO: 2 naturally has an asparagine (N) corresponding to position 33. The patent anticipates the claims as teaching all the variant combinations and method of use in cleaning [A method for cleaning an object, comprising contacting a lipid stain present on the object to be cleaned with the composition according to claim 1. ].
10. Applicants’ arguments filed 7/20/26 for each of the rejections – recite “To advance prosecution, claims have been amended. Support for the claim amendments can be found in the specification as filed on page 9, lines 8-15, etc. Applicants respectfully request reconsideration and withdrawal of the rejection.” No clear explanation is advanced.
Response: Applicants’ arguments are considered but not found to be persuasive for reasons of record. Also the inclusion of variant “asparagine (N) at position 33 corresponding to SEQ ID NO: 2” is of no consequence since position 33 corresponding SEQ ID NO: 2 is already asparagine (N).
11. No claim is allowed.
12. 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 extension fee 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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/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940
Prosecution Insights