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
This application is a 371 of PCT/US2021/019690.
The amendment filed on November 10, 2025 has been entered.
Election/Restrictions
Applicant elected without traverse of Group I in the reply filed on May 30, 2025.
Applicant elected with traverse of (I) the species of enzyme of one or more of galactose oxidase, pyranose 2-oxidase, glucarate dehydratase, and catalase in the reply filed on May 30, 2025 and (II) the species of intermediates of one or more of D- glucodialdose, 2-keto-glucodialdose, 2-keto-glucaric acid, 2,5-furandicaboxaldehyde, D- glucaric acid, 5-keto-4-deoxy glucodialdose, and 2-keto-glucose.
During a telephone conversion with Ryan D. Jenlink, the enzymes and intermediates recited in claims 2-3 were elected: galactose oxidase, catalase, and pyranose 2-oxidase as the enzymes and D-glucodialdose, 2-keto-glucodialdose, 2-keto-glucoglucaric acid, and 2,5-furanodicarboxaldehyde (schemes 1 and 2). SEQ ID NO:7 as the pyranose-2-oxidase was also elected.
Applicant elected without traverse of heterogenous metal catalyst and heterogenous acid catalyst in the reply filed on May 30, 2025.
Claim 21 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on May 30, 2025.
Status of Claims
Claims 1-3, 6-8, 11-16, and 19-22 are pending.
Claim 21 is withdrawn.
Claims 1-3, 6-8, 11-16, 19-20, and 22 are under examination.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on October 31, 2025 and February 4, 2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Response to Amendments/Arguments
Claim Rejections - 35 USC § 112(b)
Applicant’s arguments, see page 5 of the Remarks, filed November 10, 2025, with respect to claims 6-8 and 11-12 have been fully considered and are persuasive. Claims 6-8 and 11-12 have been amended to recite that the recited enzymes have an amino acid sequence of any of the recited sequence identifiers. Therefore, the rejection of claims 6-8 and 11-12 under 35 U.S.C. 112(b) has been withdrawn.
Applicant’s arguments, see page 5 of the Remarks, filed November 10, 2025, with respect to claim 19 have been fully considered and are persuasive. Claim 19 has been amended to recite a proper antecedent basis. Therefore, the rejection of claim 19 under 35 U.S.C. 112(b) has been withdrawn.
Claim Rejections - 35 USC § 112(a)
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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Claims 1-3, 6-8, 11-16, 19-20, and 22 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, 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 or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
It is noted that MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The claims encompass a chemoenzymatic process for the preparation of FDCA by (a) contacting glucose with any galactose oxidase or the galactose oxidase having the amino acid sequence of SEQ IDNO:1 with a catalase to form D-glucodialdose, (b) contacting D-glucodialdose with any pyranose-2-oxidase or the pyranose-2-oxidase having the amino acid sequence of SEQ ID NO:7 and catalase to form 2-keto-glucodialose, and (c) contacting 2-keto-glucodialose or any intermediate/2-keto-glucaric acid with any metal catalyst and acid catalyst to form FDCA or form FDCA having a purity greater than about 80%. Therefore, the claims are drawn to a chemoenzymatic process for the preparation of FDCA from glucose using a genus of galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst to produce FDCA or produce FDCA having a purity greater than about 80%.
MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention.
MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention.
According to MPEP 2163.II.A.3.(a).ii), “Satisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’"
The recitations of “galactose oxidase”, “pyranose-2-oxidase”, “metal catalyst”, and “acid catalyst” to “form FDCA” or “form FDCA having a purity greater than about 80%” fail to provide a sufficient description of the claimed method as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus.
The art discloses that the main approach for FDCA production from sugars is based on the dehydration of fructose to HMF via acid catalysis and subsequent oxidation of HMF to FDCA with an appropriate metal catalyst (see page 1, 2nd full paragraph of Zeng. Efficient One-Pot Synthesis of 2,5-Furandicarboxylic Acid from Sugars over Polyoxometalate/Metal-Organic Framework Catalysts. ChemSusChem. 2023 Nov 8;16(21):e202300836. Epub 2023 Aug 14 – form PTO-892). The prior art discloses that galactose oxidase is essentially inactive towards D-glucose (see page 973, 1st full paragraph of Deacon. Enhanced fructose oxidase activity in a galactose oxidase variant. Chembiochem. 2004 Jul 5;5(7):972-9 – form PTO-892). The chemoenzymatic production of FDCA or production of FDCA having a purity greater than 80% from glucose using galactose oxidase, catalase, pyranose-2-oxidase, metal catalyst, and acid catalyst was not known.
The specification is limited to a method of producing 2-keto-gucodialdose by reacting D-glucose, glucose oxidase, mutant galactose oxidase having one of the amino acid sequences selected from SEQ ID NO:1-6 having the function of converting D-glucose to D-glucodialdose, and a pyranose-2-oxidase having one of the amino acid sequences selected from SEQ ID NO:7-11. The specification is limited to a prophetic chemoenzymatic process for preparing FDCA using galactose oxidase, catalase, pyranose-2-oxidase, a metal catalyst, and an acid catalyst. In view of the widely variant species encompassed by the genus, the example described above is not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus.
The claimed invention requires a defined set of galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst to produce FDCA or produce FDCA having a purity greater than about 80% from glucose. Although the specification discloses exemplary galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst, a “laundry list” disclosure of every possible moiety does not necessarily constitute a written description of every species in a genus because it would not “reasonably lead” those skilled in the art to any particular species, see Fujikawa v. Wattanasin, 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) or MPEP 2163. While some of the exemplary galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst were known in the art, this knowledge alone would not allow one level of skill in the art to immediately envisage the claimed genus. Therefore, the level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which combination of galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst to use to produce FDCA or produce FDCA having a purity greater than about 80% from glucose
Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 1-3, 6-8, 11-16, 19-20, and 22.
Applicant's arguments filed November 10, 2025 have been fully considered but they are not persuasive.
Applicant argues that the amendment of claim 1, which includes the steps of contacting D-glucose with galactose oxidase and catalase to form D- glucodialdose, contacting the D-glucodialdose with pyranose-2-oxidase and catalase under conditions suitable for the formation of 2-keto-glucodialdose, and contacting the 2-keto-glucodialdose or an intermediate with a metal catalyst and acid catalyst to form 2,5-furan dicarboxylic acid, overcomes the rejection.
This is not found persuasive. Applicant’s argument has not presented any specific reasoning as to why the amended claims meet the written description requirement. The claims are drawn to a chemoenzymatic process for the preparation of FDCA from glucose using a genus of galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst to produce FDCA or produce FDCA having a purity greater than about 80%. The art discloses that the main approach for FDCA production from sugars is based on the dehydration of fructose to HMF via acid catalysis and subsequent oxidation of HMF to FDCA with an appropriate metal catalyst (see page 1, 2nd full paragraph of Zeng. Efficient One-Pot Synthesis of 2,5-Furandicarboxylic Acid from Sugars over Polyoxometalate/Metal-Organic Framework Catalysts. ChemSusChem. 2023 Nov 8;16(21):e202300836. Epub 2023 Aug 14 – form PTO-892). The prior art discloses that galactose oxidase is essentially inactive towards D-glucose (see page 973, 1st full paragraph of Deacon. Enhanced fructose oxidase activity in a galactose oxidase variant. Chembiochem. 2004 Jul 5;5(7):972-9 – form PTO-892). The chemoenzymatic production of FDCA or production of FDCA having a purity greater than 80% from glucose using galactose oxidase, catalase, pyranose-2-oxidase, metal catalyst, and acid catalyst was not known.
The specification is limited to a method of producing 2-keto-gucodialdose by reacting D-glucose, glucose oxidase, mutant galactose oxidase having one of the amino acid sequences selected from SEQ ID NO:1-6 having the function of converting D-glucose to D-glucodialdose, and a pyranose-2-oxidase having one of the amino acid sequences selected from SEQ ID NO:7-11. The specification is limited to a prophetic chemoenzymatic process for preparing FDCA using galactose oxidase, catalase, pyranose-2-oxidase, a metal catalyst, and an acid catalyst. In view of the widely variant species encompassed by the genus, the example described above is not enough and does not constitute a representative number of species to describe the whole genus. The claimed invention requires a defined set of galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst to produce FDCA or produce FDCA having a purity greater than about 80% from glucose. Although the specification discloses exemplary galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst, a “laundry list” disclosure of every possible moiety does not necessarily constitute a written description of every species in a genus because it would not “reasonably lead” those skilled in the art to any particular species, see Fujikawa v. Wattanasin, 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) or MPEP 2163. While some of the exemplary galactose oxidase, pyranose-2-oxidase, metal catalyst, and acid catalyst were known in the art, this knowledge alone would not allow one level of skill in the art to immediately envisage the claimed genus. Therefore, the specification fails to describe a representative species of the claimed genus.
Hence the rejection has been maintained.
Claim Rejections - 35 USC § 102
Applicant’s arguments, see pages 6-7 of the Remarks, filed November 10, 2025, with respect to claims 1, 13, and 19-20 have been fully considered and are persuasive. Claim 1 has been amended to recite contacting D-glucose with a galactose oxidase and a catalase to form D-glucodialdose, which is converted to D-glucodialdose by a pyranose-2-oxidae and catalase, which is not taught or suggested by Kambourakis (US 2014/0106414 – form PTO-1449). Therefore, the rejection of claims 1, 13, and 19-20 under 102(a)(1) as being anticipated by Kambourakis has been withdrawn.
Conclusion
Claims 1-3, 6-8, 11-16, and 19-22 are pending.
Claim 21 is withdrawn.
Claims 1-3, 6-8, 11-16, 19-20, and 22 are rejected.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm.
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/YONG D PAK/Primary Examiner, Art Unit 1652