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
Applicant’s response filed on 08/11/2026 is duly acknowledged.
Claims 1-10 and 12 have been canceled by applicants.
Claim 22 has been newly presented.
Claims 11 and 13-22 as currently amended/presented are pending in this application.
NOTE: Applicants are advised not to recite the text of the canceled claim(s) as currently done for claim 12 (see MPEP 37 CFR 1.121(c)).
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Election/Restrictions
Applicant's election with traverse of Species A (directed to L-cysteine sulfinic acid decarboxylase with SEQ ID NO: 2, readable on the process of instant claims 11 and 13-22) in the reply filed on 08/11/2026 (see REM, p. 6-9) is acknowledged. First traversal is on the ground(s) that L-cysteine sulfinic acid decarboxylase with SEQ ID NO: 2, and its homologs “preferably at least 90% and particularly preferably at least 95% identical” amino acid sequences do not constitute distinct species (see REM, p. 7, 1st paragraph), which were in fact not stated by the examiner as distinct species per se (see CTRS dated 03/31/2026, p. 3), and would be examined as they relate to the scope of instant claims 17 and newly presented claim 22 along with SEQ ID NO: 2.
However, applicant’s second argument pertaining to the enzymes of species B and C as “all of them catalyze the decarboxylation of the same substrate and all belong to the group of carboxy-lases….”, is duly noted and considered, but is not found to be persuasive because as admitted by applicants, each enzyme has their own “primary substrates” and in addition have unique amino acid sequences, structural features, and/or properties. Thus, species A, B and C are deemed to be distinct. However, as noted in the previous office action (CTRS dated 03/31/2026, p. 4, 1st paragraph), upon the allowance of a generic claim, applicant will be entitled to consideration of claims to additional species which are written in dependent form or otherwise require all the limitations of an allowed generic claim.
Claims 11 and 13-22 as currently amended/presented (directed to “A process for producing taurine…”; with elected species A with traverse; pertaining to L-cysteine sulfinic acid decarboxylase with SEQ ID NO: 2) have been examined on their merits in this action hereinafter.
Priority
This application is a 371 of PCT/EP2021/083369 (filed on 11/29/2021).
Objection to Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see SPEC, p. 16, lines 2 and 12, for instances). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Appropriate correction is required.
Claim Objections
1. Claim 11 (as amended) is objected to because of the following informalities: Claim 11 recites the limitations “i) wherein in a first process step (biotransformation 1),…”, in which “wherein” is recited twice, and the term “transformation 1” is presented in parenthesis. Applicants are advised to delete the extra “wherein” and remove the parenthesis by reciting “i) in a first step of biotransformation 1…”, instead. Similarly, appropriate correction in step ii) to delete extra “wherein” is also required.
Additionally applicants are advised to amend claim 11 such that the steps i) and ii) are recited using active method steps, for instance- “i) in a first step of biotransformation 1, producing O-acetyl-L-serine (OAS)….”. appropriate correction is suggested.
In addition, claim 11 recites the term “CysM”, an abbreviation , which needs to be recited in full form, at least the first time it appears in a claim or claim set. Appropriate correction is required.
2. Claim 13 (as presented) is objected to because of the following informalities: claim 13 recites the limitation “strain E. coli”, wherein the genus of the bacterium should be recited in full form as “strain Escherichia coli”, at least the first time it appears in a claim or in a claim set. Appropriate correction is required.
3. Claims 14 and 18 (as presented) is objected to because of the following informalities: Claim 14 recites the limitations “wherein the OAS sulfhydrylase stems from fermentative production”, which should be amended to recite “wherein the OAS sulfhydrylase is obtained from a fermentation process” in order to clarify the process invention (as per instant SPEC, p. 11, lines 20-23, for instance). Similar situation is also pertinent to the recitation in instant claim 18, which should be corrected appropriately, as discussed above.
4. Claim 17 (as presented) is objected to because of the following informalities: claim 17 recites the limitations “or a sequence homologous to this sequence”, which should be amended to recite “or a sequence homolog thereof”, instead. Appropriate correction is suggested.
5. Claim 19 (as presented) is objected to because of the following informalities: claim 19 recites abbreviation “CSAD enzyme” in section d), which needs to be recited in full form with the abbreviated version in parenthesis, if desired, at least the first time it appears in a claim or a claim set.
Appropriate corrections are required.
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 11 and 13-22 (as presented) 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.
Claim 11 recites the limitation "the batch" in line 9. There is insufficient antecedent basis for this limitation in the claim. Claim 11 as recited does not provide for the limitation of “a batch’ per se, and therefore it lacks antecedent basis for said limitation, and therefore the metes and bounds of the claimed process “wherein the OAS concentration in the batch is at least 10 g/L” the does not appear to be properly defined. Since, none of the dependent claims correct this situation as discussed above, they are also rejected as being indefinite for the same reasons of record. Appropriate correction is required.
Claim 17 recites the limitations “or a sequence homologous to this sequence”, which is ambiguous and confusing because it is unclear if the term “homologous” refers to actual amino acid sequence “identity”, or sequence “similarity”. The fact that no standards have been provided on record to ascertain sequence “similarity” or extent/degree thereof, the limitations of “a sequence homologous to this sequence”, renders the claimed process indefinite as the metes and bounds of the claim does not appear to be properly defined. Appropriate correction is required.
Claim 19 recites the limitation “wherein the class of cysteine sulfinic acid decarboxylases (EC 4.1.1.29) are produced by fermentation” (in lines 4-5). There is insufficient antecedent basis for this limitation in the claim. Claim 19 as currently recited directly depends from independent claim 11, which does not provide a reasonable basis for the limitation of “a class of cysteine sulfinic acid decarboxylases (EC 4.1.1.29)” per se. Appropriate correction is required.
Claim 21 as presented recites the limitations “preferably at least 60%” in line 2 of the claim, wherein the term “preferably” (taken herein as “for example”) renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Also, claim 21 recites the limitation "the molar yield" in line 1. There is insufficient antecedent basis for this limitation in the claim. Claim 21 directly depends from independent claim 11 that does not provide a reasonable basis for the limitation of “molar yield” per se. Appropriate correction is required.
Claim 22 (new) recites the limitations “wherein the sequences homologous to the L-cysteine sulfinic acid decarboxylase of SEQ ID NO: 2” (see lines 1 and 4). There is insufficient basis for this limitation in the claim. Claim 22 as newly recited directly depends from claim 16 that does not reasonably provide the basis for “a sequences homologous to L-cysteine sulfinic acid decarboxylase of SEQ ID NO: 2” per se. Applicants are advised to amend the dependency of instant claim 22 to claim 17, instead.
Appropriate corrections for the entire claim set are required.
NOTE: 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 (i.e., changing from AIA to pre-AIA ) 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.
Claim Rejections - 35 USC § 103
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 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 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.
Claims 11 and 13-22 (as presented) are rejected under 35 U.S.C. 103 as being unpatentable over Ono et al (2017, NPL cited in applicant’s IDS dated 06/12/2024, citation no. 9) taken with Feinberg et al (WO2019/083351 A1; FOR cited as ref. [N] on PTO 892 form) and Turano et al (WO 2012/158296 A1; FOR cited as ref. [O] on PTO 892 form).
NOTE: for the prior art purposes herein, any biochemical reaction that employs biosynthetic enzymes (in vitro and/or in vivo) has been taken as part of “biotransformation” reaction (see instant SPEC, p. 5, last paragraph).
Ono et al (2017) disclose a preparation method of cysteine derivatives from O-acetyl-L-serine (OAS) substrate using OAS sulfhydrylase (or cysteine synthase, CysM) enzyme (from a bacterial source, and expressed in Escherichia coli) in the presence of hydrogen sulfide (see Title, Abstract, Materials and Methods, section 2.4, Fig 2C and page 78, under “Discussion”). Ono et al also disclose other salts suitable for use in the method, such as sodium hydrogen sulfide (NaHS), sodium sulfite (Na2SO3), and sodium thiosulfate (Na2S2O3), wherein Na2SO3 is a salt of sulfurous acid of this invention (see instant SPEC, p. 4, 4th paragraph, for instance); wherein they disclose the step of producing (at a fixed pH in the reaction mix, with pH of 7.6; see section 2.4 on p. 70) various L-cysteine derivatives including L-Cysteine sulfonate (see Ono et al, p. 77, Fig. 10; and p. 74, Table 3, for instance).
However, Ono et al do not disclose the method for producing taurine from OAS that employs the step ii) wherein L-cysteic acid is decarboxylated to taurine” (instant claim 11), using L-cysteine sulfinic acid decarboxylase (CSAD with SEQ ID NO: 2, or a homolog thereof; see instant claims 16-17, and new claim 22).
Feinberg et al (2017), while teaching heterologous expression of taurine and/or taurine precursors such as hypotuarine, sulfoacetaldehyde, or cysteate in non-naturally occurring microorganisms that comprise heterologous nucleic acids expressing required enzymes such as cysteine sulfinic acid decarboxylase, CSAD (see Title, Abstract, [09], and claims on p. 92-93), disclose the step of wherein CSAD enzyme (see CSAD enzyme sequence from Synechoccocus sp. designated with SEQ ID NO: 11 on p. 70, for instances; taken herein as “a sequence homolog”) is used to convert taurine precursors into taurine (see Figs. 2 and 4-9, for instance) in recombinant bacteria (see Example 1 and Table 2, for instance).
Although , Feinberg et al do not disclose the CSAD enzyme that has the sequence as recited in instant claims 17 and 22 with SEQ ID NO: 2, such would have been obvious to an artisan of ordinary skill in the art because CSAD enzyme from Cyprinus carpio was well known in the art to be a promiscuous sulfinoalanine decarboxylase (SAD) enzyme involved in the multistep pathway for taurine biosynthesis (see disclosure from Turano et al, 2012; Title, Abstract, [0006], [0013], [0035], [0112], and claim 3, for instance) that was designated as SEQ ID NO: 10, the enzyme having 100% sequence identity to instantly claimed SEQ ID NO: 2 in instant claims 17 and 22 (see sequence homology provided below), and that has been known to convert cysteic acid into taurine (see Turano et al, [0112], for instance):
SEQ ID NO: 2 SEQUENCE HOMOLOGY (A_Genseq database)
RESULT 1
BAG82670
(NOTE: this sequence has 4 duplicates in the database searched.
See complete list at the end of this report)
ID BAG82670 standard; protein; 500 AA.
XX
AC BAG82670;
XX
DT 17-JAN-2013 (first entry)
XX
DE Cyprinus carpio sulfinoalanine decarboxylase (SAD), SEQ 10.
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KW SAD protein; abiotic stress tolerance; artificial seed; cold tolerance;
KW crop improvement; drought resistance; feedstuff; freezing tolerance;
KW heat tolerance; insect resistance; nematode resistance;
KW pathogen resistance; salt tolerance; sulfinoalanine decarboxylase;
KW transgenic plant; BOND_PC; cysteine sulfinate decarboxylase; GO3824;
KW GO16829; GO16831; GO19752; GO30170.
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OS Cyprinus carpio.
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CC PN WO2012158296-A1.
XX
CC PD 22-NOV-2012.
XX
CC PF 17-APR-2012; 2012WO-US033916.
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PR 18-MAY-2011; 2011US-0487412P.
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CC PA (PLAN-) PLANT SENSORY SYSTEMS LLC.
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CC PI Turano FJ, Turano KA;
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DR WPI; 2012-Q20695/81.
DR N-PSDB; BAG82664.
DR PC:NCBI; gi84778155.
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CC PT New cell comprising expression cassette comprising promoter operably
CC PT linked to polynucleotide that encodes sulfinoalanine decarboxylase that
CC PT is operably linked to terminator, useful for producing crop of plants
CC PT e.g. apple or apricot.
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CC PS Claim 3; SEQ ID NO 10; 54pp; English.
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CC The present invention relates to a novel cell comprising an expression
CC cassette. The expression cassette comprises a promoter operably linked to
CC a polynucleotide of SEQ ID NO: 1-7 (see BAG82661-BAG82667) that encodes a
CC sulfinoalanine decarboxylase (SAD) of SEQ ID NO: 8-13 (see BAG82668-
CC BAG82673) that is operably linked to a terminator. The invention also
CC provides: a plant storage organ comprising the cell, where the plant
CC storage organ is a seed, tuber, fruit or root; a seed having stably
CC incorporated in its genome the exogenous polynucleotide encoding a
CC sulfinoalanine decarboxylase protein; a plant grown from the seed, where
CC the plant has stably incorporated in its genome the exogenous
CC polynucleotide encoding a sulfinoalanine decarboxylase protein; a method
CC for producing a crop of plants having stably incorporated in their genome
CC an exogenous polynucleotide encoding a sulfinoalanine decarboxylase
CC protein; a pharmaceutical composition comprising an extract; a
CC nutritional supplement comprising an extract of the plant; and an animal
CC feed comprising the plant storage organ, seed and plant. The transgenic
CC plant has increased tolerance to biotic stress (pests, pathogens,
CC bacteria, microbes, viruses, viroids, microorganisms, invertebrates,
CC insects, nematodes, and vertebrates) or abiotic stress (osmotic stress,
CC oxidative damage, drought, salt, cold, freezing, heat, UV light,
CC limitations of nutrients such as nitrogen, sulfur, phosphorus or other
CC minerals). The present sequence represent the specifically claimed
CC Cyprinus carpio SAD, which can be expressed by the transgenic plant used
CC in the invention.
CC
CC Revised record issued on 03-JAN-2013 : Enhanced with precomputed
CC information from BOND.
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SQ Sequence 500 AA;
Query Match 100.0%; Score 2648; Length 500;
Best Local Similarity 100.0%;
Matches 500; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSSSKEYMNGHVHLEESDMYESDGKLFLTEAFNVIMEEILHKGTDSEEKVCEWKDPDQLR 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSSSKEYMNGHVHLEESDMYESDGKLFLTEAFNVIMEEILHKGTDSEEKVCEWKDPDQLR 60
Qy 61 ALLDLDLREHGESHKQLLQRVRDVARYSVKTCHPRFFNQLFAGVDYHALTGRLLTETLNT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ALLDLDLREHGESHKQLLQRVRDVARYSVKTCHPRFFNQLFAGVDYHALTGRLLTETLNT 120
Qy 121 SQYTYEVAPVFVLMEEEVLCKLRSLVGWSEGDGIFCPGGSMSNMYAMNVARYWAFPQVKT 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SQYTYEVAPVFVLMEEEVLCKLRSLVGWSEGDGIFCPGGSMSNMYAMNVARYWAFPQVKT 180
Qy 181 QGLWATPRMAIFTSQQGHYSMKKAAAFLGIGTDNVFIVQVDESGSMRPEDLEAKIVQAKS 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 QGLWATPRMAIFTSQQGHYSMKKAAAFLGIGTDNVFIVQVDESGSMRPEDLEAKIVQAKS 240
Qy 241 QDAVPFFVNATAGTTVQGAFDPLNRIADISERNGMWMHVDAAWGGSVLFSKKHKHLVAGI 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 QDAVPFFVNATAGTTVQGAFDPLNRIADISERNGMWMHVDAAWGGSVLFSKKHKHLVAGI 300
Qy 301 ERANSVTWNPHKMLLAGLQCSVVLFRDTTNLLMHCHSAKATYLFQQDKFYDTSLDTGDKS 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 ERANSVTWNPHKMLLAGLQCSVVLFRDTTNLLMHCHSAKATYLFQQDKFYDTSLDTGDKS 360
Qy 361 IQCGRKVDCLKLWLMWKAIGTHGLSERVEKAFALARYLVEEMEKRDNFKLVCKGPFVNVC 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 IQCGRKVDCLKLWLMWKAIGTHGLSERVEKAFALARYLVEEMEKRDNFKLVCKGPFVNVC 420
Qy 421 FWFIPPSLRRKENSADYQERLSKVAPVIKERMMKRGTMMVGYQPMDGHVNFFRMVVVSPQ 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 FWFIPPSLRRKENSADYQERLSKVAPVIKERMMKRGTMMVGYQPMDGHVNFFRMVVVSPQ 480
Qy 481 LTTKDMDFFLDEIEDLGKDL 500
||||||||||||||||||||
Db 481 LTTKDMDFFLDEIEDLGKDL 500
Thus, given the details for the process for making taurine in the recombinant bacterial cells by expressing required enzymes including CSAD as disclosed by Feinberg et al (when taken with the disclosure from Turano et al, as discussed above), an artisan in the art of making taurine would be able to successfully combine the teachings of Ono et al for making cysteic acid using OAS sulfhydrylase enzyme (see teachings of Ono et al, as discussed above) and the heterologously expressed CSAD enzyme in microbes such that the substrate OAS is converted to cysteic acid and then to the final taurine product in a reaction mixture with the help of activity of said OAS sulfhydrylase and CSAD enzymes (akin to a coupled enzymatic conversion/reaction that can be performed in the same growth medium and/or a suitable reaction mix). Since, taurine has already been known to have several beneficial effects on variety of agricultural, nutritional, as well as pharmaceutical applications (see disclosure from Feinberg et al, [04]-[08], for instance; and Turano et al, [0015], for instance), an artisan of ordinary skill in the art would have been motivated in making such combination of heterologous expression of required enzymes in microbes for producing taurine with a reasonable expectation of success, unless evidence/data provided on record to the contrary. Also, since the reaction conditions were already disclosed in the cited prior art of Ono et al (see teachings above), the adjustment in pH or concentrations of substrates in the reaction mix would have been obvious to an artisan of ordinary skill in the art of taurine (or hypotaurine that finally converts to taurine) production using recombinant microbes, or lysates thereof having suitable expression of the biosynthetic enzymes including OAS sulfhydrylase and CSAD, as already disclosed and/or suggested by the combined teachings from the cited prior art references discussed above, unless evidence/data provided on record to the contrary for the entire scope of the invention as claimed (which is currently lacking on record; see instant SPEC, Examples 7-11).
Thus, the claim as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the invention as claimed.
As per MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. In re American Academy of Science Tech Center, F.3d, 2004 WL 1067528 (Fed. Cir. May 13, 2004)(The USPTO uses a different standard for construing claims than that used by district courts; during examination the USPTO must give claims their broadest reasonable interpretation.). This means that the words of the claim must be given their plain meaning unless applicant has provided a clear definition in the specification. In re Zletz, 893 F.2d 319, 321, 13 USPQ2d 1320, 1322 (Fed. Cir. 1989).
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.
Claim 11 and 13-22 (as presented) are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over at least claim 16 of co-pending Application No. 18/709,817 (reference application; filed on the same day by common inventors and assignee). Although the claims at issue are not identical, they are not patentably distinct from each other because claim 16 of the co-pending application ‘817 is also directed to a method for producing L-cysteic acid from substrate O-acetyl-L-serine in the presence of “a salt of sulfurous acid” (also using the bacterial OAS sulfhydrylase enzyme EC 4.2.99.8; see also claim 17 of co-pending application ‘817), an intermediate step in the process as currently recited in the instant application under examination.
The conflicting Claim 16 has been reproduced as follows:
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Since, the two sets of claims are clearly co-extensive in scope, an ODP rejection is deemed proper.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
NO claims are currently allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SATYENDRA K. SINGH whose telephone number is (571)272-8790. The examiner can normally be reached M-F 8:00- 5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LOUISE W HUMPHREY can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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SATYENDRA K. SINGH
Primary Examiner
Art Unit 1657
/SATYENDRA K SINGH/Primary Examiner, Art Unit 1657
Prosecution Insights