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
Claims 1, 3, 5-17 are currently pending.
Priority
The instant application is a CON of PCT/JP2020/040189 filed on 27 October 2020, which claims priority to JP2019-195625 filed on 28 October 2019. A certified copy of this document was filed on 2 June 2022. No English translation has been filed to perfect the claim to priority.
Claim Rejections - 35 USC § 103
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 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 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 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 1, 3, 5-11 and 13-17 are rejected under 35 U.S.C. 103 as being unpatentable over Takakura (WO2017122747A1; 27 April 2022 IDS Document) in view of Okrasa (Okrasa, K. et al. In vitro bi-enzymatic synthesis of benzaldehyde from phenylalanine: practical and mechanistic studies, 2004, Journal of Molecular Catalysis B: Enzymatic, 97-101; 27 April 2022 IDS Document).
Regarding claims 1 and 3, Takakura teaches a method for producing benzaldehyde, comprising: (A) producing benzaldehyde by using at least one microorganism having four enzymes: amino acid deaminase, 4-hydroxymandelate synthase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase, wherein the at least one microorganism consists of a single microorganism solely having the four enzymes, or a combination of a plurality of microorganisms having the four enzymes as a whole (Takakura Claim 1).
Takakura does not teach producing benzaldehyde in the presence of catalase during a portion of said time period; does not specify at least 4-hydroxymandelate synthase is present during portion; and wherein the AAD does not produce hydrogen peroxide.
Okrasa discloses biotransformation of phenylalanine to benzaldehyde by cultures of microorganisms (Okrasa Pg. 97, Introduction, lines 1-4). Okrasa discloses enzymatic synthesis of alpha-keto acids from amino acids using d-amino acid oxidase [Instant Specification [33]: AAD is also referred to as “amino acid oxidase”] and that the formed hydrogen peroxide has a deleterious effect on the enzyme. The formed phenylpyruvic acid has been shown to be sensitive to H2O2; phenylpyruvate can be decarboxylated to phenylacetate in the presence of H2O2. Thus, hydrogen peroxide must be completely eliminated from the medium for the reaction [to benzaldehyde] to be completed. For this to occur, a third enzyme (catalase) should be used (Okrasa Pg. 99, left column, [2], lines 1-9).
First it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Takakura’s method for producing benzaldehyde by carrying out the reaction in the presence of catalase, because Okrasa discloses the presence of catalase can eliminate the presence of hydrogen peroxide and prevent the formation of phenylacetate (Okrasa Pg. 99, left column, [2], lines 1-9). There would have been a reasonable expectation of success in making this modification, because Takakura and Okrasa both disclose methods of producing benzaldehyde from phenylalanine with microorganisms. Second it would have been obvious that at least HMAS would have been present since Takakura teaches cultivating at least one microorganism in a culture medium to generate and accumulate benzoylformate in the culture medium, wherein at least one microorganism has amino acid deaminase, 4-hydroxymandelate synthase , and (S)-mandelate dehydrogenase; cultivating at least one microorganism in a culture medium to generate and accumulate benzoylformate in the culture medium. Therefore since Takakura suggests the presence of at HMAS during the process since the microorganism and/or plurality of microorganisms can comprise AAD, HMAS, SMDH, BFDC. See claim prior art claim 1 and [0018]. Thus, following the suggestion of Okrasa to utilize a catalase to prevent formation of hydrogen peroxide and Takakura’s suggestion of cultivating a microorganism comprising AAD, HMAS, SMDH, BFDC, producing of benzaldehyde would be “carried out in the present of catalase and at least HMAS during a portion.” Regarding the recitation the “wherein the AAD does not produce hydrogen peroxide” would be met since the catalase would prevent formation of the hydrogen peroxide.
Regarding claim 5, Takakura teaches benzaldehyde is produced from a carbon source or L-phenylalanine (Takakura Claim 3).
Regarding claim 6, Takakura teaches converting L-phenylalanine into benzoylformate by using at least one microorganism having amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase and then converting the generated benzoylformate into benzaldehyde by using a microorganism having benzoylformate decarboxylase (Takakura Claim 8).
Regarding claims 7-10, Takakura discloses cultivating at least one microorganism in a culture medium containing the carbon source to generate and accumulate benzoylformate in the culture medium, which at least one microorganism has amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase and has L-phenylalanine-producing ability; cultivating at least one microorganism in a culture medium containing L-phenylalanine to generate and accumulate benzoylformate in the culture medium, or allowing cells of the at least one microorganism to coexist with L-phenylalanine in a reaction mixture to generate and accumulate benzoylformate in the reaction mixture, which at least one microorganism has amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase; (F2) cultivating a microorganism in a culture medium containing benzoylformate generated in the step (F1) to generate and accumulate benzaldehyde in the culture medium, or allowing cells of the microorganism to coexist with benzoylformate generated in the step (F1) in a reaction mixture to generate and accumulate benzaldehyde in the reaction mixture, which microorganism has benzoylformate decarboxylase (Takakura Claim 10).
Regarding claim 11, Takakura teaches the cells consist of a culture broth of the microorganism(s), cells collected from the culture broth, a processed product thereof, or a combination thereof (Takakura Claim 13).
Regarding claim 13, Takakura teaches at least one microorganism is a bacterium or yeast (Takakura Claim 20).
Regarding claim 14, Takakura teaches at least one microorganism is a bacterium belonging to the family Enterobacteriaceae or a coryneform bacterium (Takakura Claim 21).
Regarding claim 15, Takakura teaches at least one microorganism is a bacterium belonging to the genus Escherichia (Takakura Claim 22).
Regarding claim 16, Takakura teaches the at least one microorganism is Escherichia coli (Takakura Claim 23).
Regarding claim 17, Takakura teaches the method further comprising collecting benzaldehyde (Takakura Claim 24).
Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Takakura (WO2017122747A1; 27 April 2022 IDS Document) in view of Okrasa (Okrasa, K. et al. In vitro bi-enzymatic synthesis of benzaldehyde from phenylalanine: practical and mechanistic studies, 2004, Journal of Molecular Catalysis B: Enzymatic, 97-101; 27 April 2022 IDS Document) as applied to claim 1 above, and further in view of Masignani (US8758764B2).
Takakura and Okrasa do not teach the catalase is: (a) a protein comprising the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32; (b) a protein comprising the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32 but including substitution, deletion, insertion, and/or addition of 1 to 10 amino acid residues, and having catalase activity; or (c) a protein comprising an amino acid sequence showing an identity of 90% or higher to the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32, and having catalase activity.
Masignani discloses polypeptides comprising amino acid sequences, including SEQ ID NO: 9098 for catalase-peroxidase HPI (Masignani Col. 181, ORF04549: 9097 & 9098; catalase-peroxidase HPI (katG) [1.11.1.6]). Masignani’s SEQ ID NO:9098 has 99.8% sequence identity with instant SEQ ID NO:4. A sequence alignment is provided in the appendix.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute Masignani’s SEQ ID NO:9098/catalase-peroxidase for Okrasa’s catalase with yielded predictable results, because they both have catalase activity.
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 §§ 706.02(l)(1) - 706.02(l)(3) for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1, 3, 5-11 and 13-17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 9-11, 14 and 21-25 of U.S. Patent No. 10808264 in view of Okrasa (Okrasa, K. et al. In vitro bi-enzymatic synthesis of benzaldehyde from phenylalanine: practical and mechanistic studies, 2004, Journal of Molecular Catalysis B: Enzymatic, 97-101; 27 April 2022 IDS Document).
Instant claims are directed to an invention not patentably distinct from claims 1-6, 9-11, 14 and 21-25 of commonly assigned U.S. Patent No. 10808264. Specifically, the instant claims are obvious over the patent claims in view of Okrasa.
Patent claim 1 recites a method for producing benzaldehyde, the method comprising: (A) producing benzaldehyde by using one or more microorganisms having one or more benzaldehyde generation enzymes, wherein said benzaldehyde generation enzymes consist of amino acid deaminase, 4-hydroxymandelate synthase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase, and wherein said one or more microorganisms is: 1) one microorganism which has all four of said benzaldehyde generation enzymes, or 2) a plurality of microorganisms comprising all four of said benzaldehyde generation enzymes among said plurality of microorganisms. Patent claim 2 recites the method according to claim 1, wherein said producing is carried out by a method selected from the group consisting of: (a) cultivating the one or more microorganisms so that benzaldehyde is produced from a carbon source via fermentation; (b) producing an intermediate of benzaldehyde from a carbon source and then converting said intermediate into benzaldehyde using the cells of the one or more microorganisms; and (c) combinations thereof. Patent claim 3 recites the method according to claim 1, wherein said benzaldehyde is produced from a carbon source. Patent claim 4 recites the method according to claim 1, wherein said benzaldehyde is produced from L-phenylalanine. Patent claim 5 recites the method according to claim 1, wherein said producing comprises: (B) producing benzaldehyde from a carbon source by using the one or more microorganisms, wherein the one or more microorganisms have L-phenylalanine-producing ability; or (C) converting L-phenylalanine into benzaldehyde by using the one or more microorganisms. Patent claim 6 recites the method according to claim 1, wherein said producing comprises: (B1) cultivating the one or more microorganisms in a culture medium containing a carbon source to generate and accumulate benzaldehyde in the culture medium, wherein the one or more microorganisms have L-phenylalanine-producing ability; (C1) cultivating the one or more microorganisms in a culture medium containing L-phenylalanine to generate and accumulate benzaldehyde in the culture medium; or (C2) allowing cells of the one or more microorganisms to coexist with L-phenylalanine in a reaction mixture to generate and accumulate benzaldehyde in the reaction mixture. Patent claim 9 recites the method according to claim 1, wherein said producing comprises: (E1) a method selected from the group consisting of: (E1a) generating benzoylformate from a carbon source by using a first of said one or more microorganisms having amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase, and having L-phenylalanine-producing ability; and (E1b) converting L-phenylalanine into benzoylformate by using a first of said one or more microorganisms having amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase; and (E2) converting benzoylformate generated or converted in (E1) into benzaldehyde by using a second microorganism having benzoylformate decarboxylase. Patent claim 10 recites the method according to claim 9, wherein said generating of (E1a) is carried out by cultivating said first of said one or more microorganisms recited in (E1a), wherein said converting of (E1b) is carried out by using cells of said first of said one or more microorganisms recited in (E1b) or by cultivating said first of said one or more microorganisms recited in (E1b), and wherein said converting of (E2) is carried out by using cells of said second microorganism or by cultivating said second microorganism. Patent claim 11 recites the method according to claim 1, wherein said producing comprises: (F1) a method selected from the group consisting of: (F1a) cultivating a first of said one or more microorganisms in a culture medium containing a carbon source to generate and accumulate benzoylformate in the culture medium, wherein said first of said one or more microorganisms has amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase, and has L-phenylalanine-producing ability; and (F1b) cultivating a first of said one or more microorganisms in a culture medium containing L-phenylalanine to generate and accumulate benzoylformate in the culture medium, or allowing cells of a first of said one or more microorganisms to coexist with L-phenylalanine in a reaction mixture to generate and accumulate benzoylformate in the reaction mixture, wherein said first one or more microorganisms has amino acid deaminase, 4-hydroxymandelate synthase, and (S)-mandelate dehydrogenase; and (F2) cultivating a second microorganism in the culture medium containing said benzoylformate generated in (F1) to generate and accumulate benzaldehyde in the culture medium, or allowing cells of a second microorganism to coexist with said benzoylformate generated in (F1) in a reaction mixture to generate and accumulate benzaldehyde in the reaction mixture, wherein said second microorganism has benzoylformate decarboxylase. Patent claim 14 recites the method according to claim 2, wherein said one or more microorganisms is present in a culture broth or a processed product of a culture broth; or is collected from a culture broth or processed product of a culture broth. Patent claim 21 recites the method according to claim 1, wherein the one or more microorganisms is a bacterium or yeast. Patent claim 22 recites the method according to claim 1, wherein the one or more microorganisms is a bacterium belonging to the family Enterobacteriaceae or a coryneform bacterium. Patent claim 23 recites the method according to claim 1, wherein the one or more microorganisms is a bacterium belonging to the genus Escherichia. Patent claim 24 recites the method according to claim 1, wherein the one or more microorganisms is Escherichia coli. Patent claim 25 recites the method according to claim 1, the method further comprising collecting the benzaldehyde.
The patent claims do not teach producing benzaldehyde in the presence of catalase during a portion of said time period, wherein during said portion, at least HMAS is present as recited, and wherein the AAD does not produce hydrogen peroxide as recited.
Okrasa discloses biotransformation of phenylalanine to benzaldehyde by cultures of microorganisms (Okrasa Pg. 97, Introduction, lines 1-4). Okrasa discloses previous reports on the enzymatic synthesis of alpha-keto acids from amino acids using d-amino acid oxidase [AAD] indicate that the formed hydrogen peroxide has a deleterious effect on the enzyme. The formed phenylpyruvic acid has been shown to be sensitive to H2O2; phenylpyruvate can be decarboxylated to phenylacetate in the presence of H2O2. Thus, hydrogen peroxide must be completely eliminated from the medium for the reaction [to benzaldehyde] to be completed. For this to occur, a third enzyme (catalase) should be used (Okrasa Pg. 99, left column, [2], lines 1-9).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method for producing benzaldehyde in the patent claims by carrying out the reaction in the presence of catalase, because Okrasa discloses the presence of catalase can eliminate the presence of hydrogen peroxide and prevent the formation of phenylacetate (Okrasa Pg. 99, left column, [2], lines 1-9). There would have been a reasonable expectation of success in making this modification, because the patent claims and Okrasa both disclose methods of producing benzaldehyde from phenylalanine with microorganisms wherein the microorganism contains all enzymes claimed including HMAS.
The U.S. Patent and Trademark Office may not institute a derivation proceeding in the absence of a timely filed petition. The USPTO normally will not institute a derivation proceeding between applications or a patent and an application having common ownership (see 37 CFR 42.411). Commonly assigned U.S. Patent No. 10808264, discussed above, may form the basis for a rejection of the noted claims under 35 U.S.C. 102 or 103 if the commonly assigned case qualifies as prior art under 35 U.S.C. 102(a)(2) and the patentably indistinct inventions were not commonly owned or deemed to be commonly owned not later than the effective filing date under 35 U.S.C. 100(i) of the claimed invention.
In order for the examiner to resolve this issue the applicant or patent owner can provide a statement under 35 U.S.C. 102(b)(2)(C) and 37 CFR 1.104(c)(4)(i) to the effect that the subject matter and the claimed invention, not later than the effective filing date of the claimed invention, were owned by the same person or subject to an obligation of assignment to the same person. Alternatively, the applicant or patent owner can provide a statement under 35 U.S.C. 102(c) and 37 CFR 1.104(c)(4)(ii) to the effect that the subject matter was developed and the claimed invention was made by or on behalf of one or more parties to a joint research agreement that was in effect on or before the effective filing date of the claimed invention, and the claimed invention was made as a result of activities undertaken within the scope of the joint research agreement; the application must also be amended to disclose the names of the parties to the joint research agreement.
A showing that the inventions were commonly owned or deemed to be commonly owned not later than the effective filing date under 35 U.S.C. 100(i) of the claimed invention will preclude a rejection under 35 U.S.C. 102 or 103 based upon the commonly assigned case. Alternatively, applicant may take action to amend or cancel claims such that the applications, or the patent and the application, no longer contain claims directed to patentably indistinct inventions.
Claim 12 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 9-11, 14 and 21-25 of U.S. Patent No. 10808264 in view of Okrasa (Okrasa, K. et al. In vitro bi-enzymatic synthesis of benzaldehyde from phenylalanine: practical and mechanistic studies, 2004, Journal of Molecular Catalysis B: Enzymatic, 97-101; 27 April 2022 IDS Document) as applied to claim 1 above, and further in view of Masignani (US8758764B2).
The patent claims and Okrasa do not teach the catalase is: (a) a protein comprising the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32; (b) a protein comprising the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32 but including substitution, deletion, insertion, and/or addition of 1 to 10 amino acid residues, and having catalase activity; or (c) a protein comprising an amino acid sequence showing an identity of 90% or higher to the amino acid sequence of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, or 32, and having catalase activity.
Masignani discloses polypeptides comprising amino acid sequences, including SEQ ID NO: 9098 for catalase-peroxidase HPI (Masignani Col. 181, ORF04549: 9097 & 9098; catalase-peroxidase HPI (katG) [1.11.1.6]). Masignani’s SEQ ID NO:9098 has 99.8% sequence identity with instant SEQ ID NO:4. A sequence alignment is provided in the appendix.
The substitution of a protein with Masignani’s SEQ ID NO:9098/catalase-peroxidase with the Okrasa’s catalase would have yielded predictable results, because they both have catalase activity.
Response to Arguments
Applicant argues that the present application describes that the presence of hydrogen peroxide results in the decrease in HMAS and the presence of catalase results in the degradation of the hydrogen peroxide. Applicant argues that in the presence of a catalase HMAS activity can be increased by removing the hydrogen peroxide and enhancing the production of benzaldehyde. Applicant argues that the AAD employed does not produce hydrogen peroxide. Applicant argues that the obviousness double patenting rejection should also be withdrawn in light of the arguments presented regarding Takakura and Okrasa.
Applicant's arguments filed 6/4/2025 regarding both the prior art rejections and the double patenting rejections have been fully considered but they are not persuasive. Applicant’s independent claim recites a broad method of “using” 4 AAD, HMAS, SMDH, BFDC over a time period (no parameters claimed) wherein during a portion HMAS and a catalase are present and AAD does not produce hydrogen peroxide.
As discussed in the rejection Takakura teaches cultivating at least one microorganism in a culture medium to generate and accumulate benzoylformate in the culture medium, wherein at least one microorganism or a plurality of microorganisms have amino acid deaminase, 4-hydroxymandelate synthase , (S)-mandelate dehydrogenase, and benzoylformate decarboxylase; cultivating at least one microorganism in a culture medium to generate and accumulate benzoylformate in the culture medium or reaction mixture.[0018]; [0023]. Okrasa teaches the use of a catalase to prevent the formation of hydrogen peroxide formed during has a deleterious effect and must be “completely eliminated” from the medium for the reaction to benzaldehyde to be completed. Thus, Okrasa provides motivation to add a catalase to the culture medium (also referred to as the reaction medium in the prior art) to prevent the formation of hydrogen peroxide to allow for the production of benzaldehyde. Following the suggestion of the prior art one would have expected the production of benzaldehyde and the prevention of the formation of hydrogen peroxide in the reaction by the use of a catalase.
Regarding applicant’s argument that applicant has found that hydrogen peroxide effects HMAS activity, Okrasa recognizes the “deleterious effect” of hydrogen peroxide. Again it is reiterated that by following the suggestion of Takakura of cultivating a microorganism comprising AAD, HMAS, SMDH, BFDC to produce benzaldehyde and Okrasa of adding a catalase to prevent hydrogen peroxide during reaction, applicant has merely found another property that occurs from following the prior art’s suggestion.
Regarding applicant’s argument that AAD does not produce hydrogen peroxide, this again would flow from following the suggestion of Okrasa. Adding a catalase to prevent the formation of hydrogen peroxide to allow the reaction to complete. [page 99, left paragraph].
The prevention of hydrogen peroxide from the reaction means hydrogen peroxide is not produced. Applicant argues the AAD employed does not product hydrogen peroxide. It is noted that the instant specification states that FERM BP-941 does not produce hydrogen peroxide. [0034-0035]. Takakura also teaches use of a combination of AADs including FERM BP-941 [0038]. Thus, even if applicant is arguing some distinction, the prior art already teaches AAD that does not produce hydrogen peroxide. Regarding applicant’s argument that there would be no motivation to add a catalase if the AAD does not produce hydrogen peroxide, the motivation to use a catalase to is to ensure complete conversion as taught by Okrasa. Okrasa teaches the reaction is sensitive to hydrogen peroxide which prevents complete reaction; thus the motivation to add a catalase would be to prevent any production of hydrogen peroxide in the reaction and ensure complete conversion.
Regarding applicant’s argument that the instant method increases the production of benzaldehyde, the instant claims do not claim any parameters and merely claim a broad method of “using” 4 AAD, HMAS, SMDH, BFDC over a time period (no parameters claimed). Even assuming arguendo applicant argued some unexpected results, the claims would not be commensurate in scope. The claims recite a broad process using known enzymes without reciting any specific parameters including any concentrations or time periods. Takakura teaches the claimed process. Okrasa teaches the use of a catalase in the same process. If the purported enhanced production is due to a specific feature, then applicant must specifically claim it. See MPEP 716.02
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/SHARMILA G LANDAU/ Supervisory Patent Examiner, Art Unit 1653
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