Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
DETAILED ACTION
Application Status
This application is a CON of US patent application 15/804,507, filed on 03/03/2023.
Claim(s) 1 is currently pending in the instant application.
The claim set filed on 03/03/2023 is acknowledged.
Claim(s) 1 is present for examination.
Priority
Acknowledgement is made of applicants claim for priority of US patent applications 15/804,507, filed on 11/06/2017, now ABN, and 13/993,923, filed on 06/13/2013, now ABN, which was 371 of PCT/EP11/72509, filed on 12/13/2011, and also acknowledgement is made of applicants claim for foreign priority under 35 U.S.C. 119(a)-(d) to a foreign patent application GERMANY 102010063457.3, filed on 12/17/2010 without English translation.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/06/2023 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are considered by the examiner. The signed copy of 1449 is enclosed herewith.
Drawings
There is no drawings submitted with this application.
Claim Rejections - 35 USC § 112(a) (new matter)
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.
Claim 1 is rejected under 35 U.S.C. 112(a), 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(s), at the time the application was filed, had possession of the claimed invention. This is a new matter rejection.
The Broadest Reasonable Interpretation (BRI) of claim 1, which is drawn to a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity, the method comprising: (1) mixing, to formulate the liquid washing or cleaning agent: (a) a protease comprising the amino acid sequence of SEQ ID NO: 2, wherein said amino acid sequence imparts a proteolytic activity to the protease, and wherein the protease imparts a proteolytic activity to the washing or cleaning agent; and (b) a cellulase; and (2) storing the liquid washing or cleaning agent for at least 4 weeks, wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1; wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage for 4 weeks at 30 0C as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1, wherein, at the beginning of such storage, the liquid washing or cleaning agent and the control liquid washing or cleaning agent have the same concentration of protease and the same concentration of cellulase, and wherein the protease and the cellulase are in solution in the liquid washing or cleaning agent.
There is no indication in the specification of the recitation “increased storage stability of cellulolytic activity” in the context of cleaning agent, within the scope of the invention as conceived by Applicants at the time the application was filed. Accordingly, Applicants are required to cancel the new matter in response to this Office Action.
Claim Rejections - 35 USC § 102
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 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 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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
MPEP-2131 Anticipation — Application of 35 U.S.C. 102 [R-08.2017]
A claimed invention may be rejected under 35 U.S.C. 102 when the invention is anticipated (or is "not novel") over a disclosure that is available as prior art. To reject a claim as anticipated by a reference, the disclosure must teach every element required by the claim under its broadest reasonable interpretation. See, e.g., MPEP § 2114, subsections II and IV.
"A claim is anticipated only if each and every element as set forth in the claim is found, either expressly or inherently described, in a single prior art reference." Verdegaal Bros. v. Union Oil Co. of California, 814 F.2d 628, 631, 2 USPQ2d 1051, 1053 (Fed. Cir. 1987). "When a claim covers several structures or compositions, either generically or as alternatives, the claim is deemed anticipated if any of the structures or compositions within the scope of the claim is known in the prior art." Brown v. 3M, 265 F.3d 1349, 1351, 60 USPQ2d 1375, 1376 (Fed. Cir. 2001) Note that, in some circumstances, it is permissible to use multiple references in a 35 U.S.C. 102 rejection. See MPEP § 2131.01.
MPEP-2131.01 Multiple Reference 35 U.S.C. 102 Rejections [R-11.2013]
Normally, only one reference should be used in making a rejection under 35 U.S.C. 102. However, a 35 U.S.C. 102 rejection over multiple references has been held to be proper when the extra references are cited to:
(A) Prove the primary reference contains an "enabled disclosure;"
(B) Explain the meaning of a term used in the primary reference; or
(C) Show that a characteristic not disclosed in the reference is inherent.
Claim 1 is rejected under 35 U.S.C. 102(a)(1/2) based upon a public use or sale or other public availability of the invention as anticipated by Wieland et al. (Storage-stable liquid detergent or cleaning agent containing proteases. WO2011/032988A1, publication 03/24/2011, PCT/EP2010/063556, filed on 09/15/2010, see, IDS, which is also published as US PGPUB 2012/0238005A1, publication 09/20/2012, claim benefit of PCT/EP2010/063556, filed on 09/15/2010).
The Broadest Reasonable Interpretation (BRI) of claim 1, which is drawn to a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity, the method comprising: (1) mixing, to formulate the liquid washing or cleaning agent: (a) a protease comprising the amino acid sequence of SEQ ID NO: 2, wherein said amino acid sequence imparts a proteolytic activity to the protease, and wherein the protease imparts a proteolytic activity to the washing or cleaning agent; and (b) a cellulase; and (2) storing the liquid washing or cleaning agent for at least 4 weeks, wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1; wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage for 4 weeks at 30 0C as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1, wherein, at the beginning of such storage, the liquid washing or cleaning agent and the control liquid washing or cleaning agent have the same concentration of protease and the same concentration of cellulase, and wherein the protease and the cellulase are in solution in the liquid washing or cleaning agent.
Regarding claim 1, Wieland et al. teach a liquid washing or cleaning agent comprising:
(a1) a protease having an amino acid sequence, and comprises in position 99 in the numbering according to SEQ ID NO. 1 the amino acid glutamic acid (E) or aspartic acid (D), or (a2) a protease having an amino acid sequence which is at least 80% identical to the amino acid sequence stated in SEQ ID NO. 1 and comprises in position 99 in the numbering according to SEQ ID NO. 1 the amino acid asparagine (N) or glutamine (Q), or (a3) a protease having an amino acid sequence, and comprises in position 99 in the numbering according to SEQ ID NO. 1 the amino acid alanine (A) or glycine (G) or serine (S), and (b) a phosphonate, wherein the liquid washing or cleaning agent, the protease further comprises at least one of the following amino acids: (a) threonine in position 3 (3T), (b) isoleucine in position 4 (4I), (c) alanine, threonine or arginine in position 61 (61A, 61T or 61R), (d) aspartic acid or glutamic acid in position 154 (154D or 154E), (e) proline in position 188 (188P), (f) methionine in position 193 (193M), (g) isoleucine in position 199 (199I), (h) aspartic acid, glutamic acid or glycine in position 211 (211D, 211E or 211G), (i) combinations of amino acids (a) to (h), wherein the liquid washing or cleaning agent, further comprises one of the enzymes, a protease, amylase, cellulase, hemicellulase, mannanase, and lipase, or mixture thereof, and further comprising glycerol (see, Table 1) and polyethylene glycol (PEG) (see, para 64), wherein the liquid washing or cleaning agent exhibits enhanced storage stability of cellulolytic activity after storage for 4 weeks at 30 0C (see, abstract, title, para 17, 51, 58, 129, and claims 1-2 and 9).
RESULT 4
US-13-422-260A-5
(NOTE: this sequence has 9 duplicates in the database searched.
See complete list at the end of this report)
Sequence 5, US/13422260A
Publication No. US20120238005A1
GENERAL INFORMATION
APPLICANT: Wieland, Susanne
APPLICANT: Siegert, Petra
APPLICANT: Spitz, Astrid
APPLICANT: Maurer, Karl-Heinz
APPLICANT: O'Connell, Timothy
APPLICANT: Prueser, Inken
APPLICANT: Schiedel, Marc-Steffen
APPLICANT: Eiting, Thomas
APPLICANT: Sendor-Mueller, Dorota
APPLICANT: Bastigkeit, Thomas
APPLICANT: Benda, Konstantin
APPLICANT: Mueller, Sven
TITLE OF INVENTION: Storage-stable liquid detergent or cleaning agents
TITLE OF INVENTION: containing proteases
FILE REFERENCE: H 08707 US
CURRENT APPLICATION NUMBER: US/13/422,260A
CURRENT FILING DATE: 2012-06-04
PRIOR APPLICATION NUMBER: PCT/EP2010/063556
PRIOR FILING DATE: 2010-09-15
PRIOR APPLICATION NUMBER: DE 102009029513
PRIOR FILING DATE: 2009-09-16
NUMBER OF SEQ ID NOS: 8
SEQ ID NO 5
LENGTH: 269
TYPE: PRT
ORGANISM: Bacillus lentus
Query Match 99.7%; Score 1358; Length 269;
Best Local Similarity 99.6%;
Matches 268; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
Qy 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVA 120
||||||||||||||||||||||||||||||||||||||:|||||||||||||||||||||
Db 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGQGAISSIAQGLEWAGNNGMHVA 120
Qy 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
Qy 181 ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
Qy 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269
|||||||||||||||||||||||||||||
Db 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269
It is well known that glycerol and PEG increases cellulase storage stability (see, evidential reference- Yadav et al. Assessing the compatibility of choline-based deep eutectic solvents for the structural stability and activity of cellulase: Enzyme sustain at high temperature. International Journal of Biological Macromolecules (2023), 249, 125988), and thus washing and cleaning agent of Weiland et al. inherently having increased storage stability of cellulase enzyme.
Since the Office does not have the facilities for examining and comparing applicants' cellulase enzyme with the cellulase enzyme of the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed product (i.e., cellulase) and the product of the prior art (i.e., cellulase). See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
Therefore, Wieland et al. anticipate claim 1 of the instant application as written.
Claim Rejections – AIA 35 U.S.C. § 103
The following is a quotation of 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 of this title, 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 negatived by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 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.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
According to MPEP 2143:
“Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield
predictable results;
(B) Simple substitution of one known element for another to obtain predictable
results;
(C) Use of known technique to improve similar devices (methods, or products)
in the same way;
(D) Applying a known technique to a known device (method, or product) ready
for improvement to yield predictable results;
(E) “ Obvious to try ” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in
either the same field or a different one based on design incentives or other market
forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art
reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.”
Claims 1 is rejected under 35 U.S.C. 103(a) before the effective filing date as being unpatentable over Christianson et al. (Improved enzymes and detergents containing them. WO1995/023221A1, 08/31/19954, see IDS) and in view of Gabriel et al. (Stabilization of enzymes in laundry detergents. US 5877141A, publication 03/02/1995).
The Broadest Reasonable Interpretation (BRI) of claim 1, which is drawn to a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity, the method comprising: (1) mixing, to formulate the liquid washing or cleaning agent: (a) a protease comprising the amino acid sequence of SEQ ID NO: 2, wherein said amino acid sequence imparts a proteolytic activity to the protease, and wherein the protease imparts a proteolytic activity to the washing or cleaning agent; and (b) a cellulase; and (2) storing the liquid washing or cleaning agent for at least 4 weeks, wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1; wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage for 4 weeks at 30 0C as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1, wherein, at the beginning of such storage, the liquid washing or cleaning agent and the control liquid washing or cleaning agent have the same concentration of protease and the same concentration of cellulase, and wherein the protease and the cellulase are in solution in the liquid washing or cleaning agent.
Regarding, Claim 1, Christianson et al. teach a mutant subtilisin protease, comprising at least one mutation of its amino acid sequence of SEQ ID NO: 1, which is 99.6% identity to SEQ ID NO: 1 of the instant application, wherein the position for said amino acid replacement of at least one amino acid residue is selected from the group consisting of arginine R) at position 99, serine-154, and leucine-211 is replaced by a glutamic acid (E) or an aspartic acid residue (D), wherein the enzymatic detergent composition, comprising a mutated subtilisin protease, of R99G, R99A, R99S, R99E, L211 D, L211 E, S154D, S154E, and an enzymatic detergent composition comprising said mutant protease having enhanced enzymatic activity and enhanced washing performance, wherein the detergent composition also comprises cellulase enzyme, wherein said detergent composition also comprises 5% propanediol as stabilizing reagent of the enzymes in enzymatic detergent composition, which has the long storage capability in enzymatic detergent composition (see, claims 3, 6-7, 51-52, 74, 75, pg 9, para 3, pg 26, para 2, pg 35, para 1, and Example 11-12).
RESULT: 58
AAR80417
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID AAR80417 standard; protein; 269 AA.
XX
AC AAR80417;
XX
DT 16-OCT-2003 (revised)
DT 11-APR-1996 (first entry)
XX
DE BLAP (R99X).
XX
KW Mutant; alkaline protease; Bacillus lentus DSM 5483; 130; detergent;
KW B. lentus alkaline protease; BLAP; M131; anionic surfactant; builder;
KW substrate binding area; improved wash performance; proteinogenic fibre;
KW wool; blood; egg.
XX
OS Bacillus lentus; DSM 5483.
XX
FH Key Location/Qualifiers
FT Misc-difference 99
FT /label= Gly, Ala, Ser
XX
CC PN WO9523221-A1.
XX
CC PD 31-AUG-1995.
XX
CC PF 23-FEB-1995; 95WO-US001937.
XX
PR 24-FEB-1994; 94US-00201120.
PR 17-JAN-1995; 95US-00373818.
XX
CC PA (COGN-) COGNIS INC.
XX
CC PI Christianson TM, Goddette DW, Kottwitz B, Maurer K, Paech CG;
CC PI Pochandke W, Poethkow J, Schmidt I, Tang MR, Upadek H, Weiss A;
CC PI Wilson CR;
XX
DR WPI; 1995-311532/40.
XX
CC PT Variants of Bacillus lentus alkaline protease (BLAP) - giving improved
CC PT washing performance in detergent compositions.
XX
CC PS Claim 4; Page ?; 97pp; English.
XX
CC The sequences given in AAR80415-22 represent generic mutant alkaline
CC proteases derived from Bacillus lentus DSM 5483. These sequences are
CC based on the sequences given in patent application Serial No. 07/806,691
CC filed May 29, 1991. These B. lentus alkaline proteases (BLAP's) are based
CC on wild type BLAP, and mutants M131 and 130. Mutant M131 contains the
CC mutations S3T, V4I, A188P, V193M, V199I, and mutant M130 contains the
CC same mutations excluding the mutation at position 4. Proteases which
CC conform to these generic sequences may be used in the preparation of an
CC enzymatic detergent. The detergent composition may contain two different
CC BLAP mutants, and also pref. comprises an anionic surfactant and a
CC builder. The altered amino acids are located in the substrate binding
CC area causing an improved wash performance. Detergent compositions
CC containing these enzymes are particularly useful for washing
CC proteinogenic fibres, e.g. wool, without causing harm to the fibres. They
CC are also particularly useful in the effective removal of stains such as
CC blood and egg. (Updated on 16-OCT-2003 to standardise OS field)
XX
SQ Sequence 269 AA;
Query Match 99.6%; Score 1356; Length 269;
Best Local Similarity 99.6%;
Matches 268; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
Qy 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVA 120
|||||||||||||||||||||||||||||||||||||| |||||||||||||||||||||
Db 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGXGAISSIAQGLEWAGNNGMHVA 120
Qy 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
Qy 181 ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
Qy 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269
|||||||||||||||||||||||||||||
Db 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269
Christianson et al. do not teach enhanced storage activity of cellulase enzyme in said enzymatic detergent composition for 4 weeks at 30oC (for claim 1).
However, Gabriel et al. teach stabilization of enzymes including protease, cellulase or lipase in laundry detergents, and further teach that glycolic acids and its salts are effective in stabilizing said enzymes in laundry detergents at 22oC and 37oC for 4 weeks (see, title, abstract, Col 6, para 4, Table 2, and claims 1-2, 4, 6-7).
Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to combine the teachings of Christianson et al. and Gabriel et al. to stabilize storage activity of cellulase enzyme in said enzymatic detergent composition for 4 weeks at 22 or 37oC as taught by Gabriel et al. and it is also obvious to a skilled artisan in the same field to use 30oC for storage of cellulase enzyme for 4 weeks in view of the teachings of Gabriel et al. on the basis of Obvious to try of KSR and modify Christianson et al. to make washing, detergent composition comprising mutant protease and cellulase enzymes with storage capacity for 4 weeks at 30oC in view of the teachings of Christianson et al. and Gabriel et al. to make washing, detergent composition to arrive the claimed invention.
One of ordinary skilled in the would have been motivated to use glycolic acid or its salts for enhanced storage activity of cellulase enzyme in said enzymatic detergent composition for 4 weeks at 30oC, which is commercially, industrially and financially beneficial.
One of ordinarily skilled artisan would have had a reasonable expectation of success because Christianson et al. and Gabriel et al. could successfully produce storage stable enzymatic detergent composition.
Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of claimed invention.
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. See 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); and 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) may be used to overcome an actual or provisional rejection based on a nonstatutory double patenting ground provided the conflicting application or patent is shown to be commonly owned with this application. See 37 CFR 1.130(b).
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
Claim 1 is rejected under the judicially created doctrine of obviousness-type double patenting as being unpatentable over at least claims 1 and 8 of US patent 9163226 B2, patent granted on 01/24/2023, see, PTO892).
Although the conflicting claims are not identical, they are not patentably distinct from each other because claim 1 of the instant application is directed to Claim 1 of the instant application is drawn to a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity, the method comprising: (1) mixing, to formulate the liquid washing or cleaning agent: (a) a protease comprising the amino acid sequence of SEQ ID NO: 2, wherein said amino acid sequence imparts a proteolytic activity to the protease, and wherein the protease imparts a proteolytic activity to the washing or cleaning agent; and (b) a cellulase; and (2) storing the liquid washing or cleaning agent for at least 4 weeks, wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1; wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage for 4 weeks at 30 0C as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1, wherein, at the beginning of such storage, the liquid washing or cleaning agent and the control liquid washing or cleaning agent have the same concentration of protease and the same concentration of cellulase, and wherein the protease and the cellulase are in solution in the liquid washing or cleaning agent.
The claims 1 and 8 of the US patent 9163226 B2 disclose a liquid washing or cleaning agent comprising: a protease having an amino acid sequence which is at least 80% (under BRI at least 80% could be interpreted as about 100%) identical to the amino acid sequence stated in SEQ ID NO. 1 and comprises amino acid arginine (R), wherein the washing or cleaning agent has improved cleaning performance, wherein the at least one further enzyme is a protease, amylase, cellulase or mixture thereof, wherein the storage stability is the inherent property of the liquid washing or cleaning agent of the reference patent. (See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594).
The above indicated claim(s) of the reference patent while not totally identical to the instant claims, are indeed a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity. Claim 1 of the instant application listed above cannot be considered patentably distinct over claim 1 of the reference patent, when there are specifically recited embodiments that would either anticipate to claim 1 of the instant application or alternatively render them obvious. Alternatively, claim 1 cannot be considered patentably distinct over claims 1 and 8 of the reference patent, when there is specifically disclosed embodiment in the reference copending application falls within the scope of claim 1 of the instant application, i.e. there is substantially overlapping scope between the claimed invention and the teachings of the reference.
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 the claim 1 of the reference patent.
Claim 1 is rejected under the judicially created doctrine of obviousness-type double patenting as being unpatentable over at least claims 1, 5, and 7 of US patent 12415973 B2, patent granted on 09/06/2025, see, PTO892).
Although the conflicting claims are not identical, they are not patentably distinct from each other because claim 1 of the instant application is directed to Claim 1 of the instant application is drawn to a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity, the method comprising: (1) mixing, to formulate the liquid washing or cleaning agent: (a) a protease comprising the amino acid sequence of SEQ ID NO: 2, wherein said amino acid sequence imparts a proteolytic activity to the protease, and wherein the protease imparts a proteolytic activity to the washing or cleaning agent; and (b) a cellulase; and (2) storing the liquid washing or cleaning agent for at least 4 weeks, wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1; wherein the liquid washing or cleaning agent exhibits increased storage stability of cellulolytic activity after storage for 4 weeks at 30 0C as compared to a control liquid washing or cleaning agent that is the same liquid washing or cleaning agent but comprises a protease that differs from the protease of (1)(a) solely by having a protease comprising the amino acid arginine (R) at location 99 in the count according to SEQ ID NO: 1, wherein, at the beginning of such storage, the liquid washing or cleaning agent and the control liquid washing or cleaning agent have the same concentration of protease and the same concentration of cellulase, and wherein the protease and the cellulase are in solution in the liquid washing or cleaning agent.
The claims 1, 5 and 7 of the US patent 12415973 B2 disclose a textile washing agent, comprising a) at least one protease, wherein the protease has proteolytic activity and comprises an amino acid sequence which has at least 80% sequence identity with the amino acid sequence as set forth in SEQ ID NO: 1 over its entire length and, in each case based on the numbering according to SEQ ID NO: 1, has (i) amino acid substitutions 99E and 154D, (ii) optionally comprising at least one additional amino acid substitution at the position corresponding to positions 3, 4 or 199, and (iii) optionally comprising at least one additional amino acid substitution at the position corresponding to position 74, 136, 143, 161, 163, 171, 200, 203, 209, 212 or 256; and b) at least one washing agent ingredient, wherein the textile washing agent has a pH ranging from approximately 9 to approximately 12, measured at 20° C. in 1 wt. % solution in deionized water, wherein the textile detergent further comprising at least one additional enzyme amylases, cellulases, lipase, and combinations thereof, wherein the detergent ingredient is surfactants, builders, complexing agents, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents, peroxygen compounds, bleach activators or bleach catalysts, water-miscible organic solvents, enzyme stabilizers, sequestering agents, electrolytes, pH regulators, optical brighteners, graying inhibitors, dye transfer inhibitors, foam regulators, dyes, fragrances, and combinations thereof.
The above indicated claim(s) of the reference patent while not totally identical to the instant claims, are indeed a method of formulating a liquid washing or cleaning agent for storage stability of cellulolytic activity. Claim 1 of the instant application listed above cannot be considered patentably distinct over claim 1 of the reference patent, when there are specifically recited embodiments that would either anticipate to claim 1 of the instant application or alternatively render them obvious. Alternatively, claim 1 cannot be considered patentably distinct over claims 1, 5 and 7 of the reference patent, when there is specifically disclosed embodiment in the reference copending application falls within the scope of claim 1 of the instant application, i.e. there is substantially overlapping scope between the claimed invention and the teachings of the reference.
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 the claim 1 of the reference patent.
Conclusion
Status of the claims:
Claim 1 is rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F from 9:00 AM-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Iqbal H. Chowdhury, Primary Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656