DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
Election/Restrictions
Applicant’s election without traverse of Group 1 (claims 117-121 and 128-135), and Species election of the combination of substitutions T022A-E271F regarding the claims in the reply filed on 03/10/2026 is acknowledged.
Claims 122-125, 126-127, and 136 are withdrawn from further consideration pursuant to 37 1.142(b) as being drawn to a nonelected invention, there being no allowable or linking claim. Election was made without traverse in the reply filed 03/10/2026.
For purpose of expedited prosecution, subtilisin comprising T022R and N043R relative to SEQ ID NO:1 is rejoined for prosecution and being examined on the merit.
Claims 117-121 and 128-135 are examined, as encompassing the elected invention.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 117-121 and 128-135, 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 117 and 119 recite “the protease variant” and “the Bacillus lentus subtilisn GG36 protease” however, the claim(s) and its dependency do not previously introduce a “protease variant” or “the Bacillus lentus subtilisn GG36 protease”. Accordingly, it is not clear whether “the protease variant” refers to the previously recited subtilisin variant, to a different protease variant, or a broader genus of proteases. Further, it is not clear which “Bacillus lentus subtilisin GG36 protease” is referenced in the claim(s). The lack of antecedent basis renders the claims indefinite due to the use of the term “the protease variant” and “the Bacillus lentus subtilisn GG36 protease”.
The dependent claims are rejected since they inherit and do not resolve the indefinite issues.
Claim Rejections - 35 USC § 103
The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under pre-AIA 35 U.S.C. 103(a) are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 117-121 and 128-135 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Aaslyng, D et al., (U.S. Patent No: 5665587; 1997-09-09) and further in view of Brode, P.F. et al., (US Patent No: 6599730 B1; 2003-29-07).
Regarding claims 117, 118, and 119, Aaslyng et al. teaches the species T022R-N043R, and N76D (column 52, claim 1), a total net charge relative to the net charge of Bacillus lentus subtilisin serine protease (B. subtilis 309 and 147 are variants of Bacillus lentus deposited with the NCIB and accorded accession numbers NCIB 10147 and NCIB 10309) (Materials and Methods, ‘Bacterial Strains’ paragraph 107). Aaslyng et al., also teaches mutation(s) in an amino acid sequence of subtilisin at positions: 022, 101, 103, 104, 159, 188, 245, 248,and 271 from subtilisin 309 (abstract); where a modified subtilisin comprising, a mutation is an amino acid sequence at a position numbered according to the mature subtilisin BPN’ (column 52, claim 1). Assalyn also teaches a subtilisin comprising E271Q (table XI, Claim 1). Assalyn teaches that one or a combination of mutations can be made on subtilisin (column 12, lines 28-57).
Regarding claim 121, Aaslyng et al., teaches test performance of protease(s) at specified pH, temperature and other test parameters; the subtilisin variant is from subtilisin 309, with an amino acid sequence numbered according to the mature subtilisin BPN’ , and with net charge that is from a subtilisin variant from B.lentus, resulting from the substitutions identified by Aaslyng et al., that are also identified in instant application (paragraph 136- 140 and Table III).
Regarding claims 117-121 Aaslyng et al, does not teach the elected species T022A-E271F, however Aaslyng et al., does teach T022R-N043R also identified by instant application. Further, Aaslyng et al., does not specify SEQ ID NO.1 (claim 117-118) . Also, Aaslyng et al., does not specify parent protease GG36 and its corresponding amino acid sequence(s) which differ from SEQ ID NO. 2, at, at least 80% percent sequence (117,119, 120). Further, Aaslyng et al., does not specify the test characteristics relative to a B. lentus subtilisin GG36 protease (claim 121).
However, Brode et al., teaches subtilisin 309 SEQ ID NO:1 and SEQ ID NO:2 (NO:2 being GG36) from the instant application, with 100% sequence identity for SEQ ID NO:1 and also 100% sequence identity to SEQ ID NO: 2, where amino acid positions are numbered according to SEQ ID NO:1 (sequence of Bacillus amyloliquefaciens subtilisin BPN’) from the instant application (column 2, lines 14-22).
Therefore, it would have been obvious to a person of ordinary skill in the art at the effective date of filing, to have combined the amino acid substitution(s) T022R-N043R, and N76D (as described in instant application) with corresponding numbering to subtilisin BPN’ (SEQ ID NO. 1 of instant application) as described by Aaslyng et al., into the GG36 protease (corresponding to SEQ ID NO. 2 of instant application), as taught by Brode et al. This combination of Aaslyng et al., and Brode et al., would have resulted in a subtilisin protease variant with (1) amino acid sequence combination, T022R-N043R (2) a net charge of the variant corresponding to GG36 with a N76D substitution (3) wherein the numbering of the amino acid position corresponds to SEQ ID NO. 1, and (4) the protease variant having 80% of greater sequence identity to SEQ ID NO. 2 .
Further, both Aaslyng et al., and Brode et al., described subtilisin serine proteases, derived from the same organism(s), with sequence numbering identified to the same subtilisin BPN’ (SEQ ID NO: 1 of instant application), and with amino acid substitutions identified at several of the same positions (022, 101, 103, 104, 159, 188, 245, 248, and 271) from subtilisin 309, and with the same intended use. Lastly, Aaslyng et al., conducts test performance of protease(s) to determine performance efficacy at variable temperatures and pH to determine cleaning efficacy as identified in instant application.
Regarding the elected species, subtilisin comprising T022A-E271F, it would be obvious to modify the subtilisin of Asalyng et al. to comprising a T022A and E271F into the GG36 protease (corresponding to SEQ ID NO. 2 of instant application), as taught by Brode et al. in order to generate (1) an equivalent substitution resulting in T022A-E271F based on the same positions being modified by Aaslyng et al., in which Assalyn describes T022R and E271Q (Claim 1) and Brode et al, further describes in multiple embodiments substitution of amino acids relative to subtilisin 309 wild-type, in which the modification of the amino acid is relative to the desired charge and/or function of the protease – such that, in some preferred embodiments, the variant has decreased absorption and increased hydrolysis of an insoluble substrate, as compared to a wild-type. Accordingly, the combination of Aaslyng et al., and Brode et al., provides a result specific optimization of known proteases, in which for purposes of examples: substitution(s) in neutral amino acids are substituted with negatively and/or a more negatively and/or hydrophilic charged amino acids, or a highly charged amino acid replaced with a more neutral charged amino acid or hydrophobic amino acid, such that the overall net charge of the protease variant provides a net charge with the intended functionality compared with a wild-type protease. Thus, the combination of Aaslyn et al., and Brode et al., would result in the species of T022A-E271F, as the combination and/or described substitutions would be a desired outcome relative to protease function and/or net charge which would result in substitutions to the amino acid(s) at the selected position(s), which are previously taught, resulting in the desired protease activity.
Further these substitutions would be introduced to the subtilisin serine protease, as compared with the positions that are identified with SEQ ID NO. 1 and corresponding to parent protease GG36 (SEQ ID NO:2). Resultingly, the modification would produce changes to the charge of the mutant enzyme in a way to provide a mutant protease having an isoelectric point that is shifted and a decrease in the isoelectric point and hence net charge of a subtilisin type protease, which under washing conditions can result in not only an improved wash performance of the enzyme but also an improved compatibility with lipase and/or other enzymes which improve the efficiency of the protease and its activity at various temperatures to meet said test performance.
A skilled artisan would have reasonably expected success in the combination since both address the same problems and/or improvements to the same subtilisin type serine protease(s), as identified in the instant application. Since the combined prior art prescribes the same solutions as the instant application, the prior art is able to produce the same outcome.
Regarding claim 128, 129, 130, 131, 132,133, 134 and 135, Aaslyng et al., teaches the detergent compositions for textiles, hard surface or other materials to be cleaned (‘Summary of the Invention’, paragraph 131), where the composition is a liquid and contains sodium phosphate (column 51, example 4L), a powder (column 51, example 5L), a granulate (column 51, example 6L), and is able to resist bleaching agents (column 6, lines 36-43). The liquid detergent is provided as a non-phosphate containing composition (column 52, lines 3-14). The example composition(s) can contain a lipase and protease enzyme that is mutant S001 and alternatively S003, S004, and/or C004 (column 51, Example 5L).
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 reconsider at 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
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www.uspto.gov/patents/apply/applying, online/eTerminal-disclaimer.
Claims 117-121 and 128-135 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 11447762B2 (ref. to as ‘762). This is a non-provisional nonstatutory double patenting rejection because the claims of U.S. Patent No. 11447762B2 (ref. to as ‘762) are not patentably distinct from the instant application.
Regarding claims 117,118, and 119 of the instant application: claims 1-3 of ‘762 recite: the subtilisin with proteolytic activity and comprising a combination of amino acid substitution(s) with the combination of T022A-E271F, wherein the total net charge of the variants is within the value(s) identified in the claim(s) as compared with B. lentus subtilisin GG36 protease SEQ ID NO:2) and in which the of amino acid numbering is according to SEQ ID. NO. 1, wherein SEQ ID NO.1 of instant application and.
Regarding claim 120 of the instant application: claim 4 of ‘762 recites that the subtilisin variant has 80% or more sequence identity to SEQ ID. NO. 2, and includes one or more of the substitutions as identified in claim 117 of the instant application.
Regarding claim 121 of the instant application: claim 5 of ‘762 recites test performance indices, since the composition of the instant application and ‘762 of the patented claims are the same, the performance indices of instant application would naturally have the same characteristic of ‘762 .
Regarding claims 128-135 of the instant application, dependent to claim 117:
claims 6-13 of ‘762 recites the same language to the instant application and are dependent to claims 1-3 of ‘762. Claim 117 of the instant application in view of claims 1-3 of ‘762 identifies the same limitations and therefore renders obvious the same dependent limitations as recited in claims 128-135. The table summarizes the claims which recite the same language in instant application and ‘762.
18/482,990-Instant Application
Patent No: 11447762 B2
128. (New) A composition comprising at least one subtilisin variant of Claim 117, wherein said composition is a fabric and home care product.
6. A composition comprising at least one subtilisin variant of claim 1, wherein said composition is a fabric and home care product.
129. (New) The composition of Claim 128, wherein said composition is a cleaning composition.
7. The composition of claim 6, wherein said composition is a cleaning composition.
130. (New) The composition of Claim 128, wherein said cleaning composition is a granular, powder, solid, bar, liquid, tablet, gel, or paste composition.
8. The composition of claim 6, wherein said cleaning composition is a granular, powder, solid, bar, liquid, tablet, gel, or paste composition.
131. (New) The composition of Claim 128, further comprising at least one bleaching agent.
9. The composition of claim 6, further comprising at least one bleaching agent.
132. (New) The composition of Claim 128, wherein said cleaning composition is phosphate- free.
10. The composition of claim 6, wherein said cleaning composition is phosphate-free.
133. (New) The composition of Claim 128, wherein said cleaning composition contains phosphate.
11. The composition of claim 6, wherein said cleaning composition contains phosphate.
134. (New) The composition of Claim 128, further comprising at least one additional enzyme.
12. The composition of claim 6, further comprising at least one additional enzyme.
135. (New) The composition of Claim 134, wherein said at least one additional enzyme is selected from hemicellulases, cellulases, peroxidases, proteases, metalloproteases, xylanases, lipases, phospholipases, esterases, perhydrolases, cutinases, pectinases, pectate lyases, mannanases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, arabinosidases, hyaluronidases, chondroitinases, laccases, and amylases, or any combination thereof.
13. The composition of claim 12, wherein said at least one additional enzyme is selected from hemicellulases, cellulases, peroxidases, proteases, metalloproteases, xylanases, lipases, phospholipases, esterases, perhydrolases, cutinases, pectinases, pectate lyases, mannanases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, and amylases, and any combination thereof.
Although the claims at issue are not identical, they are not patentably distinct from each other because the instant application and patent ’762 (disclose subtilisin variants in a mature form having proteolytic activity with the combination of T022A-E271F in which the variant is a variant of parent protease Bacillus lentus subtilisin GG36 SEQ ID NO: 2 and are numbered according to the numbering of amino acid positions in the sequence of Bacillus amyloliquefaciens subtilisin BPN’ (SEQ ID NO: 1) and the variants has amino acid sequence identity to its full length to SEQ ID NO:2 – where both the instant application and ‘762 share the same SEQ ID NO: 1 and SEQ ID NO: 2.
Conclusion
No claims are deemed patentable.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ENUSHA KARUNASENA whose telephone number is (571)272-3972. The examiner can normally be reached Monday-Friday 7:30am-5pm.
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/ENUSHA KARUNASENA/Examiner, Art Unit 1653
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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