DETAILED CORRESPONDENCE Summary This is the initial Office Action based on the Dodds, et al. application filed with the Office on 31 July 2023. Claims 1 -3, 5-12, 16, 17, and 19-26 are currently pending and have been fully considered. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. The preliminary amendment filed on 29 February 2024, is acknowledged and has been entered. Priority The instant application is a US National Stage Application of an International Patent Application, PCT/US2022/014640, filed on 31 January 2022, which claims priority to a US Provisional Patent Application, 63/143,918, filed on 31 January 2021. Thus, 31 January 2021 is the effective filing date of the present application. Information Disclosure Statement The information disclosure statement (IDS) submitted regarding the present application filed on 31 January 2024, is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS has been considered by the Examiner. Claim Interpretation Some of the instant limitations are recited as optional (by virtue of the use of the term, “optionally”) . Said limitations are not considered to be positively recited and do not detail necessarily present elements within the present claims. 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 appl icant regards as his invention. Claim s 1-3 and 5-10 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. The term “ at an enhanced rate ” in claim s 1 and 6 is a relative term which renders the claim indefinite. The term “ at an enhanced rate ” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. There is no comparison as to what constitutes an enhanced rate of molecular hydrogen dissolving in the processing stream . Therefore, claim 1 and 6 are rejected. Claims 2, 3, 5, and 7-10 are also rejected due to their ultimate dependence from rejected claim 1. Claim 21 recites the limitation "the in vitro or cell-free system". There is insufficient antecedent basis for this limitation in the claim. 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 . Claim s 1 , 3 , and 5 are rejected under 35 U.S.C. 103 as being unpatentable over a US Patent Application Publication to Biocheminsights , Inc. (US 2017/0335473 A1; hereinafter, “ Biocheminsights ' 473”) in view of a US Patent to Higgins, et al. (US 4,318,784; hereinafter, “Higgins”). Regarding claim 1, Biocheminsights '473 teaches a system for providing NA D (P)H2 reducing equivalents to an in vitro system (para [ 0043] "a device or apparatus used to provide electrochemically generated reducing power or reducing equivalents to a redox enzyme for the purpose of catalyzing a desired reduction of a substrate molecule. By providing electrochemically generated reducing equivalents, this disclosure allows the use of redox enzymes in a non-physiological or non-cellular environment" i.e. in vitro), comprising: a. a chamber configured to receive hydrogen and to contain a liquid phase, said liquid phase comprising a cofactor that can be reduced by hydrogen from an oxidized form to a reduced form (para [0080] "a device for producing a desired product via a reaction requiring reducing equivalents is provided. The device includes: para [ 0081] "(a) an anode contained in an anode chamber and a cathode contained in a cathode chamber; para [ 0082] (b) deionized water in the anode chamber in contact with the anode"; para [ 0084] "(d) a liquid phase in the cathode chamber continuously in contact with the cathode, for use in a desired redox reaction performed by an in vitro process", Fig 2 shows the reduction, by hydrogen of an NA D cofactor); b. a catalyst which enhances a reduction rate of the oxidized form by the hydrogen, thus forming the reduced form (para [ 0016] "If electrons could be provided from an external source, that is, an electrical current ... enzymes could be used as conventional catalysts, performing redox reactions without the need for living cells", see Fig. 2, ETM is an enzyme catalyst, supplying electrons (hydrogen) (i.e. to NA D (P)+, forming NA D (P)H.); c. a process stream comprising a substrate to be transformed via the desired redox reaction which oxidizes the reduced form of the cofactor with concomitant production of a desired product (para [ 0085] "a process stream containing a substrate to be catalyzed by the redox enzyme system into a desired product", see Fig 2); and d. optionally, a membrane enabling containment within the chamber, the cofactor in the oxidized and/or reduced forms, the catalyst, and the process stream (para [ 0086] "a membrane located between the cathode and the process stream, said membrane capable of preventing the optional ETM and the redox enzyme system from significantly entering into the process stream", see Fig. 2). Biocheminsights '473 does not explicitly teach a source of molecular hydrogen. However, Higgins discloses electrochemical regeneration of NAD (Col. 1, lines 24-25), wherein is taught reducing equivalents are derived e lectrochemically, including electrochemically from molecular hydrogen (Abstract). At the time of the filing of the instant application, it would have been obvious to one of ordinary skill in the art to have utilized the molecular hydrogen taught by Higgins for reduction a cofactor as it is a known alternative to conventional electrochemical cell usage (Higgins, Col. 4, lines 40-43). Regarding claim 3, Biocheminsights '473 teaches a system for providing NAO(P)H2 reducing equivalents to an in vitro system, comprising a catalyst, as discussed for claim 1. Biocheminsights '473 further teaches attachment of the catalyst to the membrane surface by physical or chemical methods (para [ 0105] "the ETM and/or the cofactor can be chemically modified by methods such as grafting to a soluble polymer, such that they cannot pass through the pores of the membrane that communicate to the cathode chamber. In this manner, the ETM is held inside the cathode chamber, and the cofactor is held inside the porous matrix of the membrane; even while the aqueous phase in the cathode chamber and the aqueous phase held in the membrane are continuous with each other, thus permitting the ETM to transfer electrons to the cofactor , and hence to the redox enzyme"). Regarding claim 5, Biocheminsight 473 teaches containment of the catalyst in the membrane (para [ 0086] "a membrane located between the cathode and the process stream, said membrane capable of preventing the optional ETM and the redox enzyme system from significantly entering into the process stream", see Fig. 2). Claim s 2 and 7 are rejected under 35 U.S.C. 103 as being unpatentable over Biocheminsights '473 in view of Higgins as applied to claim 1 above, and further in view of a US Patent Application Publication to the Board of Trustees of the Leland Stanford Junior University (US 2013/0273628 A1; hereinafter, “Stanford”) . Regarding claim 2, Biocheminsights'473 teaches a system for providing NAD(P)H2 reducing equivalents to an in vitro system, comprising a catalyst, as discussed for claim 1. Biocheminsights'473 does not expressly teach that the catalyst is a hydrogenase enzyme . H owever, Stanford teaches hydrogenase enzymes useful in reducing NA D enzymes (para [ 0025] "Compositions of a fusion protein comprising a spatially tethered ferredoxin-NA D P-reductase (FNR) and an active [ FeFe ] hydrogenase, genetic sequences encoding such fusion proteins, and methods of use thereof are provided. The fusion proteins of the invention link an FNR polypeptide to an active [ FeFe ] hydrogenase through a polypeptide linker. The fusion protein facilitates improved electron transfer "). Based on Stanford's teaching, it would have been obvious to an artisan of ordinary skill in the art to experiment with Stanford's hydrogenase as a catalyst in the transfer of electrons from the cathode of Biocheminsights '473, because the hydrogenase protein of Stanford facilitates improved electron transfer, such as in sequential redox reactions used in the method Biocheminsights '473. Regarding claim 7, the distance between the redox enzyme and the hydrogenase enzyme is not detailed. However, it has been held that, where the only difference between the prior art and the claims was a recitation of relative dimensions of the claimed device and a device having the claimed relative dimensions would not perform differently than the prior art device, the claimed device was not patentably distinct from the prior art device (MPEP 2144.04 IV A). Claims 8-10 are rejected under 35 U.S.C. 103 as being unpatentable over Biocheminsight ‘473 in view of Higgins as applied to claim 1 above, and further in view of a US Patent Application Publication to Biocheminsights , Inc. (US 2019/0078127; hereinafter, “ Biocheminsights ' 127”) . Regarding claims 8-10, Biocheminsight ‘473 in view of Higgins teaches the limitations of instant claim 1. Biocheminsight ‘473 and Higgins do not teach renalase enzyme and/or Mung Bean Phenol Oxidase enzyme. Biocheminsights ‘127 teaches a system including the renalase enzyme and the Mung Bean Phenol Oxidase enzyme ([0032]). At the time of the filing of the instant application, it would have been obvious to one of ordinary skill in the art to have utilized the renalase enzyme and the Mung Bean Phenol Oxidase enzyme as taught by Biocheminsights ‘127 because it constitutes the selection of a known material based on its suitability for its intended use (MPEP 2144.07). Claim 26 is rejected under 35 U.S.C. 103 as being unpatentable over Biocheminsights '473 in view of Stanford. Regarding claim 26 Biocheminsights '473 teaches a cathode, comprising a porous carbon material (para [ 0092] "the cathode chamber comprises a cathode primarily composed of carbon", para [0093] "the cathode chamber comprises a carbon electrode that is a thin sheet of carbon, carbon felt, or porous carbon"), and further teaches a catalyst (para [ 0016] "If electrons could be provided from an external source, that is, an electrical current ... enzymes could be used as conventional catalysts, performing redox reactions without the need for living cells", see Fig. 2, ETM is an enzyme catalyst") incorporated into and/or attached onto the porous carbon material (para [ 0104] "In the case of a non-aqueous or partially aqueous cathode liquid phase (e.g., organic), the ETM can be chosen to have suitable solubility therein"). Biocheminsights'473 does not expressly teach that the catalyst is a hydrogenase enzyme . H owever, Stanford teaches hydrogenase enzymes useful in reducing NAD enzymes (para (0025] "Compositions of a fusion protein comprising a spatially tethered ferredoxin-NADP-reductase (FNR) and an active [ FeFe ] hydrogenase, genetic sequences encoding such fusion proteins, and methods of use thereof are provided. The fusion proteins of the invention link an FNR polypeptide to an active [ FeFe ] hydrogenase through a polypeptide linker. The fusion protein facilitates improved electron transfer''). Based on Stanford's teaching, it would have been obvious to an artisan of ordinary skill in the art to experiment with Stanford's hydrogenase as a catalyst in the transfer of electrons from the cathode of Biocheminsights '473, because the hydrogenase protein of Stanford facilitates improved electron transfer, such as in sequential redox reactions used in the method Biocheminsights '473, and could be incorporated into and/or attached onto the porous carbon material. Claim s 11, 12 , 16 , 19-20, 22, and 23 are rejected under 35 U.S.C. 103 as being unpatentable over a US Patent Application Publication to Biocheminsights , Inc. (US 2019/0078127; hereinafter, “ Biocheminsights ' 127”) in view of Biocheminsights '473 . Regarding claim s 11 and 19-20 , Biocheminsights '127 teaches a system for providing NAD(P)H.sub.2 reducing equivalents to an in vitro or cell-free system (para [ 0024] "The present disclosure, in one aspect, provides a system for e lectrochemically generating NAD(P)H.sub.2 reducing equivalents", para [ 0009] "It is possible to isolate the needed oxidoreductase enzyme and use it to catalyze reactions in vitro .... A further advantage of using isolated enzymes in a cell-free system is that multiple enzymes can be used"), comprising: a . an eIec t roc h emicaI cell comprising an anode contained in an anode chamber and a cathode contained in a cathode chamber (para [0024] "the system comprising:", para [ 0025] "(a) an electrochemical cell comprising an anode contained in an anode chamber and a cathode contained in a cathode chamber"); b. deionized water in the anode chamber in contact with the anode (para [ 0061] ''The present disclosure, in some embodiments, is directed to an improved ... "Electrochemical Bioreactor Module" (EBM)", para [ 0062] "An EBM can include", para [0064] "deionized water in the anode chamber in contact with the anode"); c. a proton permeable membrane that separates the anode and cathode chambers (para [0065] "a proton permeable membrane that separates the anode and cathode chambers"); e. a liquid phase in the cathode chamber continuously in contact with the cathode, said liquid phase containing the cofactor required for the desired redox reaction (para (0066] "a liquid phase in the cathode chamber continuously in contact with the cathode, said liquid phase optionally comprising an electron transfer mediator (ETM) capable of transferring reducing equivalents to a redox enzyme system, said redox enzyme system comprising a redox enzyme and a cofactor ''); h. a process stream containing a substrate to be transformed via catalysis by the redox enzyme system which oxidizes the reduced from the cofactor with concomitant production of a desired product (para (0067] "e. a process stream containing a substrate to be transformed via catalysis by the redox enzyme system into a desired product"); I. an external power source providing a voltage between the anode and the cathode (para [ 0069] "an external power source providing a voltage between the anode and the cathode."). Although Biocheminsights '127 does not expressly recite that the power source is capable of controlling the voltage applied between the anode and the cathode, and the current provided, such that the voltage and the current may be controlled in order to prevent or enhance the formation of hydrogen at the c athode, and thus prevent or enhance the production of bulk amount of hydrogen gas formed in the cathode chamber, a power source providing voltage commonly (universally for modern instruments) is equipped with a voltage controller to allow said instrument to deliver an appropriate voltage/current required, in the case of an electrochemical device, this entails H2 gas formation proportional to the voltage applied, thus, it would have been obvious to an artisan of ordinary skill in the art to specify that the power source of Biocheminsights '127 have the capacity to control the voltage applied to the cathode and thus the H2 gas evolved from it. Biocheminsights '127 does not expressly teach: d. a cathode, optionally constructed of porous material capable of allowing convective flow of the process stream through the geometric volume of the cathode . H owever, Biocheminsights '473 teaches a system for providing NAD(P)H2 reducing equivalents that includes carbon electrodes made of porous material (para [ 0043] "a device or apparatus used to provide electrochemically generated reducing power or reducing equivalents", para [ 0066] "a general Electron Transport Mediator (ETM) that is cycled between its oxidized and reduced states by accepting electrons from the cathode and delivering electrons to the NAD(P) cofactor.", para [ 0092] "the cathode chamber comprises a cathode primarily composed of carbon. This may be a solid piece of carbon that has been machined to have flow-channels or other physical shaping that increases surface area and contact time between the ETM and the cathode.", para [ 0078] "ETMs are generally considered desirable for facilitating the transfer of electrons from the actual cathode surface to the cofactors of redox enzyme systems", para [0093] "a carbon electrode that is a thin sheet of carbon, carbon felt, or porous carbon ... Multiple sheets of carbon paper, electrically connected, may be used as the cathode and thus provide increased surface area"). Since Biocheminsights '473 teaches porous carbon electrodes having increased surface area in which electrons from the actual cathode surface are transferred to the cofactors (e.g. NAD(P)), thus improving the amount of reducing equivalents produced, it would have been obvious to an artisan of ordinary skill in the art to include the porous carbon cathode of Biocheminsights '473 among cathodes of the system of Biocheminsights '127, and Biocheminsights '473. Biocheminsights '473 further teaches: f. optionally, a catalyst which acts upon the hydrogen formed at the cathode to reduce the oxidized form of the cofactor, thus forming the desired reduced form of the cofactor, such catalyst being capable of accepting hydrogen molecules formed at the cathode and catalyzing the reduction of the oxidized form of the cofactor (para [ 0016] "If electrons could be provided from an external source, that is, an electrical current ... enzymes could be used as conventional catalysts, performing redox reactions without the need for living cells", see Fig. 2, ETM is an enzyme catalyst, supplying electrons (hydrogen) (i.e. to NAD(P)+, forming NAD(P)H)). Based on the teaching of Biocheminsights '473, it would have been obvious to one of ordinary skill in the art to combine a catalyst accepting hydrogen at the cathode and reducing and NAD cofactor, because the electrons (and reducing power) of the electric current would efficiently transfer NAD(P)H.sub.2 reducing equivalents to the end products, for example to redox enzymes in the adjacent asymmetric membrane shown in Fig. 2 of Biocheminsights '473. Regarding claim 12, Biocheminsights '127 and Biocheminsights '473 teach a system for providing NAD(P)H.sub.2 reducing equivalents to an in vitro or cell-free system, as discussed for claim 11. Biocheminsights '473 further teaches that the cathode comprises porous or foamed carbon (para [ 0093] "a carbon electrode that is a thin sheet of carbon, carbon felt, or porous carbon"). Regarding claim 16 , Biocheminsights '127 and Biocheminsights '473 teach a system for providing NAD(P)H.sub.2 reducing equivalents to an in vitro or cell-free system, as discussed for claim 11. Biocheminsights '473 further teaches that the catalyst is capable of accepting hydrogen molecules formed at the cathode in the liquid phase prior to the formation of hydrogen bubbles (para [ 0004] "The transfer of electrons from an electrode to a chemical species, that is a reduction reaction, occurs at the cathode", para [ 0045] "The device further allows the capture of any hydrogen gas which may be adventitiously generated at the cathode surface during the process of providing reducing equivalents"). Regarding claims 22 and 23, Biocheminsights ‘127 teaches a system including the renalase enzyme and the Mung Bean Phenol Oxidase enzyme ([0032]). Claim s 17 and 25 is rejected under 35 U.S.C. 103 as being unpatentable over Biocheminsights ' 127 and Biocheminsights ' 473 as applied to claim 16 above, and further in view of Stanford . Regarding claim 17, Biocheminsights '127 and Biocheminsights '473 teach a system for providing NAD(P)H.sub.2 reducing equivalents via a catalyst that transfers hydrogen to cofactors and subsequently to redox enzymes, as discussed for claims 11, 12 and 16. Biocheminsights '127 and Biocheminsights '473 do not expressly teach that the catalyst is a hydrogenase enzyme . H owever, Stanford teaches hydrogenase enzymes useful in reducing NAD enzymes (para [ 0025 ] "Compositions of a fusion protein comprising a spatially tethered ferredoxin-NADP-reductase (FNR) and an active [ FeFe ] hydrogenase, genetic sequences encoding such fusion proteins, and methods of use thereof are provided. The fusion proteins of the invention link an FNR polypeptide to an active [ FeFe ] hydrogenase through a polypeptide linker. The fusion protein facilitates improved electron transfer"). Based on Stanford's teaching, it would have been obvious to an artisan of ordinary skill in the art to experiment with Stanford's hydrogenase as a catalyst in the transfer of electrons from the cathode of Biocheminsights '127 and Biocheminsights '473, because the hydrogenase protein of Stanford facilitates improved electron transfer, such as in sequential redox reactions used in the method of Biocheminsights '127 and Bincheminsights '473. Regarding claim 25, the distance between the redox enzyme and the hydrogenase enzyme is not detailed. However, it has been held that, where the only difference between the prior art and the claims was a recitation of relative dimensions of the claimed device and a device having the claimed relative dimensions would not perform differently than the prior art device, the claimed device was not patentably distinct from the prior art device (MPEP 2144.04 IV A). 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