DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-8, 11-15, and 17-21 are pending in the application. In the interest of clarity, it is noted that even though the “8” in claim 8 has strikethrough, claim 8 is considered to be pending because the status identifier for claim 8 is “Currently amended” and not “Cancelled.”
Restriction/Election
Applicant’s election without traverse of:
the invention of Group I, claims 1-8, 11-14, and 17-21,
species A1) protease comprises threonine or serine at position 3 (3T or 3S) for species election A,
species B2) protease comprises amino acid substitutions S3T, V4I, and V205I for species election B, and
species C10) protease comprises amino acid sequence of SEQ ID NO: 4 for species election C
in the reply filed January 20, 2026 is acknowledged.
Claim 15 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Claims 1-8, 11-14, and 17-21 are being examined on the merits with claims 3, 5, and 7 being examined only to the extent the claims read on the elected subject matter set forth above.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international application PCT/EP2021/075665, filed September 17, 2021, which claims foreign priority under 35 U.S.C. 119(a)-(d) to European application nos. 20197482.1 and 20201088.0, filed September 22, 2020 and October 9, 2020, respectively. A certified copy of each of the foreign priority documents has been filed in this application on March 21, 2023.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on March 21, 2023 and January 20, 2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDSs have been considered by the examiner.
Specification/Informalities
The specification is objected to for containing sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.821(a)(1) and (a)(2), yet failing to comply with the requirements of 37 CFR 1.821 through 1.825; applicants’ attention is directed to the final rulemaking notice published at 55 FR 18230 (May 1, 1990), and 1114 OG 29 (May 15, 1990). See specification at p. 15, lines 20-21. To be in compliance, applicants should identify nucleotide sequences of at least 10 nucleotides and amino acid sequences of at least 4 amino acids in the specification by a proper sequence identifier, i.e., “SEQ ID NO:” (see MPEP 2422.01). If these sequences have not been listed in the computer readable form and paper copy of the sequence listing, applicant must provide an initial computer readable form (CRF) copy of the “Sequence Listing”, an initial paper copy of the “Sequence Listing”, as well as an amendment directing its entry into the specification, and a statement that the content of the paper and CRF copies are the same and, where applicable, include no new matter as required by 37 C.F.R. 1.821(e) or 1.821(f) or 1.821(g) or 1.821(b) or 1.825(d).
Claim Objections
Claim 1 is objected to in the recitation of “80% identical” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “80% sequence identity.”
Claims 13 and 14 are objected to in the recitation of “Detergent composition” and in the interest of improving claim form and grammar, it is suggested that the noted phrase be amended to recite “A detergent composition” in claim 13 and “The detergent composition” in claim 14.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 2, 4, 5, 7, and 19-21 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claims 2 and 5 are confusing in the recitation of “which comprises compared to SEQ ID NO: 1 the amino acid substitution R101E or R101D according to the numbering of SEQ ID NO: 2” in claim 2 and the recitation of “wherein the protease comprises compared to SEQ ID NO: 1 the amino acid substitution R101E or R101D…according to the numbering of SEQ ID NO: 2” in claim 5 because SEQ ID NO: 2 has serine and not arginine at position 101. It is suggested that applicant amend the claim(s) appropriately to correct the inconsistency.
Claim 4 is confusing in the recitation of “wherein the protease comprises compared to SEQ ID NO: 1 the amino acid substitution R101E or R101D and the amino acid substitutions S3T, V4I, and V205I according to the numbering of SEQ ID NO: 2” because SEQ ID NO: 2 has serine and not arginine at position 101 and has isoleucine and not valine at position 205. It is suggested that applicant amend the claim(s) appropriately to correct the inconsistency.
Claim 7 is inconsistent with claim 1 for reasons that follow. Claim 1 recites “wherein the amino acid sequence of the protease comprises compared to SEQ ID NO: 1 at least two additional negative charges in the loop region of residues 98 to 104 according to the numbering of SEQ ID NO: 2” with amino acids 98 to 104 of SEQ ID NO: 2 corresponding to amino acids 96 to 102 of SEQ ID NO: 1 (see boxed amino acid sequence of the sequence alignment between SEQ ID NO: 1 and SEQ ID NO: 2 of Appendix A). Claim 7, which depends from claim 1, is confusing for reciting the protease comprises the amino acid sequence of SEQ ID NO: 4 (i.e., part c) of claim 7) because SEQ ID NO: 4 has only one additional negative charge as compared to the sequence of amino acids 96 to 102 of SEQ ID NO: 1 (see boxed amino acid sequence of the sequence alignment between SEQ ID NO: 1 and SEQ ID NO: 4 of Appendix A). As such, claim 7 is inconsistent with claim 1 and it is suggested that applicant amend the claim(s) appropriately to correct the inconsistency.
Claim 19 is indefinite in the recitation of “wherein the additional mutation at position 217 according to the numbering of SEQ ID NO: 2 is L217Q…” because SEQ ID NO: 2 has tyrosine and not leucine at position 217. It is suggested that applicant amend the claim(s) appropriately to correct the inconsistency.
Claims 20 and 21 and inconsistent with claim 17 for reasons that follow. Claim 17 from which claims 20 and 21 depend recites NH-CHR1-CO, NH-CHR2-CO, and NH-CHR3-CO are “non-polar amino acids.” Claims 20 and 21 are indefinite for reciting polar amino acids such as serine (abbreviated as “Ser”), which is inconsistent with the requirement that NH-CHR1-CO, NH-CHR2-CO, and NH-CHR3-CO are non-polar amino acids in claim 17. It is suggested that applicant amend the claim(s) appropriately to correct the inconsistency.
Claim Rejections - 35 USC § 102/103
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.
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.
Claims 1-8, 11-14, and 17-21 are rejected under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Jenewein et al. (WO 2018/069158 A1; cited on Form PTO-892 filed November 20, 2025; hereafter “Jenewein”).
The claims are drawn to a composition comprising
a) a protease
a1) comprising an amino acid sequence which is at least 80% identical to SEQ ID NO: 1 and
a2) wherein the amino acid sequence of the protease comprises compared to SEQ ID NO: 1 at least two additional negative charges in the loop region of residues 98 to 104 according to the numbering of SEQ ID NO: 2;
b) a protease inhibitor selected from the group consisting of peptide aldehyde, peptide aldehyde hydrosulfite adduct, and combinations thereof; and
c) at least one second enzyme different from the protease (a).
Regarding claim 1, Jenewein teaches an aqueous solution comprising a protease and one or more natural inhibitors of said protease, wherein the protease comprises an amino acid sequence which is at least 80% identical to SEQ ID NO: 1 and which comprises compared to SEQ ID NO: 1 at least two additional negative charges in the loop region of residues 98 to 104 according to the numbering of SEQ ID NO: 2 (p. 3, lines 13-17). Instant SEQ ID NO: 1 is identical to SEQ ID NO: 1 of Jenewein (see Appendix B for sequence alignment). Jenewein teaches the aqueous solution can comprise one or more stabilizing agents, preferably a protease inhibitor (p. 23, lines 7-15) including a peptide aldehyde (p. 24, line 17). Jenewein teaches the aqueous solution comprises one or more detergent enzymes other than the disclosed protease (p. 22, lines 42-43).
Regarding claims 2-5, Jenewein teaches the protease comprises the amino acid substitution R101E or R101D and the amino acid substitutions S3T, V4I, and V205I according to the numbering of SEQ ID NO: 2 (p. 4, lines 26-28; p. 16, lines 42-43).
Regarding claims 6 and 19, Jenewein teaches the protease has an additional mutation at position 217 according to the numbering of SEQ ID NO: 2, preferably L217Q, L217D, L217E, or L217G (p. 19, lines 19-20).
Regarding claim 7, Jenewein teaches that in a preferred embodiment, the protease comprises the amino acid sequence of SEQ ID NO: 4 (p. 19, lines 22 and 36). Instant SEQ ID NO: 4 is identical to SEQ ID NO: 4 of Jenewein (see Appendix C for sequence alignment).
Regarding claim 8, Jenewein teaches the aqueous solution can comprise one or more stabilizing agents, preferably a protease inhibitor (p. 23, lines 7-15), which include a peptide aldehyde specially designed for the protease active site (p. 23, lines 10-15; p. 24, lines 17-19).
Regarding claim 11, Jenewein teaches the aqueous solution comprises one or more detergent components, which include surfactants (p. 22, lines 30-32).
Regarding claim 12, Jenewein teaches the one or more enzymes different from the disclosed protease include, e.g., protease, amylase, and lipase (p. 23, lines 2-3).
Regarding claim 13, Jenewein teaches the aqueous solution is a detergent composition (p. 28, lines 4-5).
Regarding claim 14, Jenewein teaches the detergent composition is for laundry (p. 11, lines 35-36) and Jenewein’s detergent composition for laundry is considered to be “a laundry detergent composition” in claim 14.
Regarding claims 17, 20, and 21, Jenewein teaches the peptide aldehyde comprises 3 amino acid residues, the N-terminal of the peptide aldehyde is protected by an N-terminal protection group, and discloses the amino acids of the peptide aldehyde, which include non-polar amino acids such as Val (p. 24, lines 18-38).
Regarding claim 18, Jenewein teaches the N-terminal protection group of the peptide aldehyde includes benzyloxycarbonyl (p. 24, lines 21-23).
Therefore, Jenewein anticipates claims 1-8, 11-14, and 17-21 as written.
Alternatively, in view of the cited teachings of Jenewein, the composition of claims 1-8, 11-14, and 17-21 would have been obvious to one of ordinary skill in the art before the effective filing date. One would have been motivated and expected success to make the composition of claims 1-8, 11-14, and 17-21 because of the explicit teachings of Jenewein set forth above.
Therefore, claims 1-8, 11-14, and 17-21 are anticipated by or, in the alternative, are obvious in view of Jenewein.
Claim Rejections – 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 reconsideration 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 upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-8, 11-14, and 17-21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6, 9, and 16 of copending Application No. 18/245,849 (reference application) in view of Branner et al. (WO 1991/000345; cited on the IDS filed March 21, 2023; hereafter “Branner”) and Jenewein. Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding instant claims 1, 8, 11, 13, 17, 18, 20, and 21, claim 1 of the reference application recites a liquid composition, comprising
component (a): at least one peptide aldehyde, and
component (b): at least two organic solvents, wherein one organic solvent is 1,2-propane diol and at least one further organic solvent is selected from the group consisting of diols other than 1,2-propane diol in a weight ratio of 1,2-propane diol: at least one diol other than 1,2-propane diol of 25:1 to 1:4;
claim 6 of the reference application recites the composition according to claim 1, wherein the composition additionally comprises
component (c): at least one hydrolase comprising as a catalytic triad the amino acids aspartate, histidine and serine;
claim 9 of the reference application recites a liquid detergent formulation comprising the liquid composition according to claim 1 and at least one detergent component selected from the group consisting of surfactants and non-phosphate based builders; and
claim 16 of the reference application recites the liquid composition according to claim 1, wherein the at least one peptide aldehyde is a tripeptide aldehyde selected from the group consisting of compounds according to formula (PA)
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228
759
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wherein
R1 and R2 are groups such that NH-CHR1-CO and/or NH-CHR2-CO are non-polar amino acids;
R3 is a group such that NH-CHR3-CO is an L or D-amino acid residue of Tyr, Phe, Val, Ala or Leu;
and
the N-terminal protection group Z is selected from the group consisting of benzyloxycarbonyl (Cbz), p-methoxybenzyl carbonyl (MOZ), benzyl (Bn), benzoyl (Bz), p-methoxybenzyl (PMB), p-methoxyphenyl (PMP), formyl, acetyl (Ac), methyloxy, alkoxycarbonyl, methoxycarbonyl, fluorenylmethyloxycarbonyl (Fmoc), and tert-butyloxycarbonyl (Boc).
The differences between instant claims 1, 8, 11, 13, 17, 18, 20, and 21 and the claims of the reference application are the claims of the reference application do not recite the protease of part a) of instant claim 1, and the claims of the reference application do not recite the at least one second enzyme of part c) of instant claim 1.
Branner teaches subtilisin proteases comprise a catalytic triad of Asp – His – Ser (p. 21, lines 12-14).
Jenewein teaches a modified subtilisin protease that is resistant against natural protease inhibitors in stains, the protease comprising an amino acid sequence which is at least 80% identical to SEQ ID NO: 1 and which comprises compared to SEQ ID NO: 1 at least two additional negative charges in the loop region of residues 98 to 104 according to the numbering of SEQ ID NO: 2 (p. 3, lines 6-17). Instant SEQ ID NO: 1 is identical to SEQ ID NO: 1 of Jenewein (see Appendix B for sequence alignment).
Jenewein teaches a detergent composition comprising one or more detergent enzymes other than the disclosed modified subtilisin protease (p. 22, lines 42-43).
In view of teachings of Branner and Jenewein, it would have been obvious to one of ordinary skill in the art for the at least one hydrolase comprising as a catalytic triad the amino acids aspartate, histidine and serine of the claims of the reference application to be the modified subtilisin protease of Jenewein and for the detergent composition of the claims of the reference application to comprise one or more detergent enzymes other than the recited hydrolase. One would have been motivated and expected success for the at least one hydrolase comprising as a catalytic triad the amino acids aspartate, histidine and serine of the claims of the reference application to be the modified subtilisin protease of Jenewein because claim 6 of the reference application recites the composition additionally comprises component (c): at least one hydrolase comprising as a catalytic triad the amino acids aspartate, histidine and serine, Branner teaches subtilisin proteases comprise a catalytic triad of Asp – His – Ser, and Jenewein teaches a modified subtilisin protease that is resistant against natural protease inhibitors in stains. One would have been motivated and expected success for the detergent composition of the claims of the reference application to comprise one or more detergent enzymes other than the recited hydrolase because the claims of the reference application recite a detergent composition and Jenewein teaches a detergent composition comprises one or more detergent enzymes other than a protease.
Regarding instant claims 2-5, Jenewein teaches the modified subtilisin protease comprises the amino acid substitution R101E or R101D and the amino acid substitutions S3T, V4I, and V205I according to the numbering of SEQ ID NO: 2 (p. 4, lines 26-28; p. 16, lines 42-43).
Regarding claims 6 and 19, Jenewein teaches the protease has an additional mutation at position 217 according to the numbering of SEQ ID NO: 2, preferably L217Q, L217D, L217E, or L217G (p. 19, lines 19-20).
Regarding claim 7, Jenewein teaches that in a preferred embodiment, the protease comprises the amino acid sequence of SEQ ID NO: 4 (p. 19, lines 22 and 36). Instant SEQ ID NO: 4 is identical to SEQ ID NO: 4 of Jenewein (see Appendix C for sequence alignment).
Regarding claim 12, Jenewein teaches the one or more enzymes different from the disclosed protease include, e.g., protease, amylase, and lipase (p. 23, lines 2-3).
Regarding claim 14, Jenewein teaches a detergent composition can be used for laundry (p. 11, lines 35-36).
Therefore, claims 1-8, 11-14, and 17-21 of this application are unpatentable over claims 1, 6, 9, and 16 of the reference application. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Status of the claims:
Claims 1-8, 11-15, and 17-21 are pending.
Claim 15 is withdrawn from consideration.
Claims 1-8, 11-14, and 17-21 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, 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 published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
Alignment of SEQ ID NO: 1 (Query 1) with SEQ ID NO: 2 (Sbjct)
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356
694
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Alignment of SEQ ID NO: 1 (Query 1) with SEQ ID NO: 4 (Sbjct)
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358
690
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APPENDIX B
BFF08053
ID BFF08053 standard; protein; 269 AA.
XX
AC BFF08053;
XX
DT 31-MAY-2018 (first entry)
XX
DE Bacillus lentus alkaline protease (BLAP) (Wild type), SEQ:1.
XX
KW Protease; enzyme inhibition; mutation; surfactant.
XX
OS Bacillus lentus.
XX
CC PN WO2018069158-A1.
XX
CC PD 19-APR-2018.
XX
CC PF 05-OCT-2017; 2017WO-EP075391.
XX
PR 11-OCT-2016; 2016EP-00193375.
XX
CC PA (BADI ) BASF SE.
XX
CC PI Jenewein S, Spangenberg O, Nielsen JD;
XX
DR WPI; 2018-30468Y/31.
XX
CC PT Reducing inactivation of protease by natural inhibitors of protease in
CC PT process of cleaning textile or hard surface comprising stains comprising
CC PT natural protease inhibitors involves using protease comprising amino acid
CC PT sequence.
XX
CC PS Claim 1; SEQ ID NO 1; 53pp; English.
XX
CC The present invention relates to subtilisin variants, which are resistant
CC against protease inhibitors. The invention further discloses a method for
CC reducing the inactivation of protease by one or more natural inhibitors
CC of the protease. The subtilisin variants of the invention are useful for
CC lowering the proteolytic activity in a detergent solution. The present
CC sequence represents a Bacillus lentus alkaline protease (BLAP) (Wild
CC type), which is involved in preparation of mutated variant of alkaline
CC protease.
XX
SQ Sequence 269 AA;
ALIGNMENT:
Query Match 100.0%; Score 1362; Length 269;
Best Local Similarity 100.0%;
Matches 269; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
Qy 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVA 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVA 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
APPENDIX C
BFF08056
ID BFF08056 standard; protein; 269 AA.
XX
AC BFF08056;
XX
DT 31-MAY-2018 (first entry)
XX
DE Alkaline protease (BLAP) variant (S3T/V4I/R101E/V205I), SEQ:4.
XX
KW Protease; enzyme inhibition; mutation; mutein; surfactant.
XX
OS Bacillus lentus.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Misc-difference 3
FT /note= "Wild-type Ser substituted by Thr"
FT Misc-difference 4
FT /note= "Wild-type Val substituted by Ile"
FT Misc-difference 99
FT /note= "Wild-type Arg substituted by Glu"
FT Misc-difference 199
FT /note= "Wild-type Val substituted by Ile"
XX
CC PN WO2018069158-A1.
XX
CC PD 19-APR-2018.
XX
CC PF 05-OCT-2017; 2017WO-EP075391.
XX
PR 11-OCT-2016; 2016EP-00193375.
XX
CC PA (BADI ) BASF SE.
XX
CC PI Jenewein S, Spangenberg O, Nielsen JD;
XX
DR WPI; 2018-30468Y/31.
XX
CC PT Reducing inactivation of protease by natural inhibitors of protease in
CC PT process of cleaning textile or hard surface comprising stains comprising
CC PT natural protease inhibitors involves using protease comprising amino acid
CC PT sequence.
XX
CC PS Example 1; SEQ ID NO 4; 53pp; English.
XX
CC The present invention relates to subtilisin variants, which are resistant
CC against protease inhibitors. The invention further discloses a method for
CC reducing the inactivation of protease by one or more natural inhibitors
CC of the protease. The subtilisin variants of the invention are useful for
CC lowering the proteolytic activity in a detergent solution. The present
CC sequence represents a alkaline protease (BLAP) variant
CC (S3T/V4I/R101E/V205I), which is useful for reducing protease inhibition
CC in detergents.
XX
SQ Sequence 269 AA;
ALIGNMENT:
Query Match 100.0%; Score 1363; Length 269;
Best Local Similarity 100.0%;
Matches 269; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 AQTIPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 AQTIPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN 60
Qy 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGEGAISSIAQGLEWAGNNGMHVA 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGEGAISSIAQGLEWAGNNGMHVA 120
Qy 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNR 180
Qy 181 ASFSQYGAGLDIVAPGVNIQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 ASFSQYGAGLDIVAPGVNIQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI 240
Qy 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269
|||||||||||||||||||||||||||||
Db 241 RNHLKNTATSLGSTNLYGSGLVNAEAATR 269