DETAILED ACTION
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 .
Election/Restrictions
Applicant's election with traverse of Group II (claims 109-112) in the reply filed on 04/24/2026 is acknowledged. The traversal is on the ground(s) that:
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This is not found persuasive because the features of at least claim 109 are obvious as set forth under the rejections under 35 USC 103 below such that the claims do not all recite a special technical feature that makes a contribution over the prior art. It is noted that claim 109 does not recite the terms “cellulose” or “carbon dioxide.”
The requirement is still deemed proper and is therefore made FINAL.
Claims 87-91, 93-99, 101-108 and 113-118 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected Group/Invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 04/24/2026. New claims 115-118 depend from claims that are non-elected Group I or III and belong to those Groups as appropriate.
Claim Objections
Claim 109 is objected to because of the following informalities:
In claim 109, recitation of “the single reactor containing stabilized enzymes” in line 7 is understood as a structural requirement that the reactor physically contain stabilized enzymes. The antecedent basis for the same is “a single reactor configured to” as recited in line 5 without prior mention of containing stabilized enzymes. The claim should be placed in a better form by reciting “a single reactor containing stabilizing enzymes configured for.”
Appropriate correction is 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 121 and 122 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.
Claims 121 and 122 recites the limitation "the stabilizing components" in line 1. There is insufficient antecedent basis for this limitation in the claim. Claims 109 and 112 recite “wherein stabilized enzymes are (1) stabilized with surface- complementary intrinsically disordered polymer chains, (2) immobilized through adsorption and cross-linking, (3) stabilized through cross-linking the enzymes with themselves or other molecules,(4) in the form of an encapsulated enzyme, (5) immobilized in a reaction vessel, (6) enzymes not complexed with polymers and able to maintain activity and longevity in anon-native environment, or any combination thereof.” The term “component” is not employed prior in the claims such that there is no literal antecedent basis for recitation of “the stabilizing components.”
Further, it is not clear as to what claims terms may or may not provide for an inherent antecedent basis for “the stabilizing components.” “Components” implies a physical structures. However, “enzymes not complexed with polymers and able to maintain activity and longevity in anon-native environment” does not have any apparent “component” such that it is unclear if the same is encompassed by recitation of “the stabilizing components.” Further, the terminology of “the stabilizing components” is so different from the recitation of six categories (1) through (6) as to be unclear if recitation of “the stabilizing components” is a reference to these six categories recited in claims 109 and 112. For these reasons, an ordinarily skilled artisan is unable to determine how to avoid infringement of claims 121-122.
Further in claims 121 and 122, the claims recite “the enzyme.” “[I]f two different levers are recited earlier in the claim, the recitation of "said lever" in the same or subsequent claim would be unclear where it is uncertain which of the two levers was intended.” MPEP 2173.05(e). Claims 109 and 122 recite four different enzymes. It is not clear if “the enzyme” in claim 121 and 122 requires only one of these four different enzymes to satisfy the functional features of claims 121 and 122 or if all of these four enzymes must satisfy the functional features of claims 121 and 122, or in the alternative if “the enzyme” is a reference to a specific enzyme recited in claims 109 and 112.
It is noted that the indefinite scope of claims 121 and 122 above preclude a determination of whether claims 121 and 122 satisfy the requirements of 35 U.S.C. 112(d).
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 109, 111, 112, and 119-121 (all non-withdrawn claims) 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. For a broad generic claim, the specification must provide adequate written description to identify the genus of the claim.
“A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) (“In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus.”). Regents of the University of California v. Eli Lilly & Co., 119, F.3d 1559, 1568, 43 USPQ2d 1398, 1405 (Fed. Cir. 1997).
“The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice . . ., reduction to drawings . . ., or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.” MPEP 2163(II)(3)(a).
Furthermore, a “‘representative number of species’ means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure ‘indicates that the patentee has invented species sufficient to constitute the gen[us].’ See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) (‘[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.’). ‘A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.’ In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).” MPEP 2163(II)(3)(a).
Independent claims 109 and 112 recite: stabilized triosephosphate isomerase, stabilized aldolase, stabilized fructose 1,6-bisphosphatase, and stabilized phosphoglucose isomerase, and wherein stabilized enzymes are (1) stabilized with surface- complementary intrinsically disordered polymer chains, (2) immobilized through adsorption and cross-linking, (3) stabilized through cross-linking the enzymes with themselves or other molecules,(4) in the form of an encapsulated enzyme, (5) immobilized in a reaction vessel, (6) enzymes not complexed with polymers and able to maintain activity and longevity in anon-native environment, or any combination thereof.
That is, the rejected claims recite four types of “stabilized” enzymes stabilized via one of six specifically enumerated mechanisms (e.g. surface-complementary intrinsically disordered polymer chains, cross-linking, immobilization, etc.). The recitation of “enzymes not complexed with polymers and able to maintain activity and longevity in anon-native environment” is understood to include enzymes that are stabilized through amino acid substitutions or other changes in the primary amino acid sequence of the enzyme in addition to other non-enumerated means. Each of these recited genera being a pairing of one of the recited four stabilized enzymes with one of the six recited mechanisms or means of stabilization is a specific chemical genus of stabilized enzymes recited in the claims.
Silva et al. (Practical insights on enzyme stabilization, Critical Rev. Biotechnol. 38, 2018, 335-50), abstract, states: “Enzymes are efficient catalysts designed by nature to work in physiological environments of living systems. The best operational conditions to access and convert substrates at the industrial level are different from nature and normally extreme. . . . The stability of enzymes is therefore a key issue on the implementation of the catalysts in industrial processes which require the use of extreme environments that can undergo enzyme instability.”
Silva, Fig. 2, and related text, reviews several approaches to stabilizing enzymes for industrial use that overlay in part with those recited directly in the claims, e.g. Pegylation (stabilized with surface-complementary intrinsically disordered polymer chains), immobilization, crosslinking, encapsulation, etc. Silva, pages 337-338, further discusses “Engineering of enzymes” wherein “Protein engineering is the design and construction of novel proteins, usually by manipulation of their genes. The rational protein design or direct evolution allows the alteration of enzyme properties to meet the limitations in their applications,” which includes amino acid substitution or modifying the amino acid sequence of enzymes.
“The achievement of stable and active enzymes is often a challenging effort because they have not evolved naturally to be used in industrial environments. Their biological activity depends on the three-dimensional native structure, hence catalytically active, and any significant conformational change can lead to their inactivation.” Silva, page 336, right col. Reference 6 of Silva is Gianfreda et al. (Enzyme stabilization, Mol. Cellular Biochem. 100, 1991, 97-128) stating: “In the last years, several methods to immobilize biologically active proteins have been developed and it is very difficult to identify an universal suitable technique for all enzymes: the proper choice of the immobilization method depends very closely on the type of enzyme to be immobilized.” Gianfreda, page 99, left col.
In addition to immobilization, all the means of stabilization stated in the claims are unpredictable to implement wherein the claims require that the four recited enzymes actually be stabilized as to be a stabilized enzyme. For example, for engineering enzymes by amino acid substitution or otherwise, “Rational design uses structural and mechanistic information together with molecular modeling for the prediction of changes in the protein structure in order to alter or induce the desired properties. Advances in computer technology have helped to create better protein models to improve predictions for rational design, but structure–activity relationships are still not trivial.” Silva, page 338, left col. Silva, page 338, left col., also discusses directed evolution and screening of mutant libraries of enzymes, wherein “screened for the desired property and the variants showing promising results are subjected to further rounds of evolution” is a description of unpredictability wherein variant enzymes with desired properties cannot be determined or predicted and can only be identified by testing. Regarding surface modification of enzymes, whether by crosslinking or polymer/pegylation, Silva, page 340, left col., states “Examples of succeeded enzyme pegylation are presented in Table 1,” which directly implies that such techniques can also be unsuccessful, i.e. that success in stabilization is variable and unpredictable.
“A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.”
The specification contains no working examples of the claims. That is, the specification does not describe any working species of:
A stabilized triosephosphate isomerase;
Stabilized aldolase;
Stabilized fructose 1,6-bisphosphatase, or
Stabilized phosphoglucose isomerase,
that are stabilized by one of the six mechanisms recited in the claims or otherwise. From the group of triosephosphate isomerase, aldolase, fructose 1,6-bisphosphatase and phosphoglucose isomerase, based upon no working examples and no credible theoretic discussion of what stabilization techniques will be successful with these enzymes, an ordinarily skilled artisan at time of filing cannot predict species of any of the these enzymes that can be successfully stabilized by any of (1) stabilized with surface- complementary intrinsically disordered polymer chains, (2) immobilized through adsorption and cross-linking, (3) stabilized through cross-linking the enzymes with themselves or other molecules,(4) in the form of an encapsulated enzyme, (5) immobilized in a reaction vessel, (6) enzymes not complexed with polymers and able to maintain activity and longevity in anon-native environment, or any combination thereof, where possession of the recited genera of stabilized enzyme requires ability to predict which enzymes can be stabilized by which of the recited six mechanisms and then specifically the structure that will lead to stabilization, e.g. extent and quality of pegylation, nature and structure of crosslinking, prediction of specific amino acid substitutions that will lead to stabilization, manner of encapsulation or immobilization that will lead to stabilization, etc.
Stated in other words, “The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice . . ., reduction to drawings . . ., or by disclosure of relevant, identifying characteristics.” The claims recite genera of biomolecules wherein member species have a specific structure that leads to stabilization. For example, a crosslinked aldolase that is not stabilized is not a species of a genus of stabilized aldolase, etc. For the four classes of enzymes recited (triosephosphate isomerase, aldolase, fructose 1,6-bisphosphatase and phosphoglucose isomerase), there is not description of any specific stabilized enzyme species, which does not constitute a representative number of species, and no creditable description of relevant, identifying characteristics being specific structural modifications that would be expected to successful for stabilization as to differentiate between structures that would fall within the recited genera of stabilized enzymes and those that would fall outside the recited genera of stabilized enzymes. “In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus.” Here, for the reasons discussed, the claims recite a genus of all stabilized triosephosphate isomerase, aldolase, fructose 1,6-bisphosphatase and phosphoglucose isomerase falling within the broadly-recited six mechanisms of stabilization as recited in the claims and reviewed above. Evidence is presented regarding the unpredictability of determining in the performance of any given species of these enzymes to be stabilized by any of these six mechanisms and the specific structural requirements for stabilization such that outside the presentation of any specific enumerated examples and the unpredictability of the structure of specific stabilized enzymes “one skilled in the art may be found not to have been placed in possession of [[a]] gen[era]” of stabilized enzymes as recited and as discussed above.
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 (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.
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.
Claim(s) 109, 111, 112, and 119-122 is/are rejected under 35 U.S.C. 103 as being unpatentable over Montemagno et al. (WO 2011/084540 A1) further in view of Wong et al. (Synthesis of sugars by aldolase-catalyzed condensation, J. Org. Chem. 48, 1983, 3199-3205) (previously cited).
Montemagno, abstract, states:
Bubble architectures are formed using biologically-derived surfactant, for example, the protein Ranaspumin-2 and other biologically derived surfactants, to create functional materials that mimic cellular physiological processes. In one embodiment, the bubble architecture is used to form an artificial photosynthesis platform for converting light and CO2 to a value-added product, for example, simple sugar.
“FIG. 8 is an illustration of a sol-gel design for a foam encasement in accordance with one embodiment of the present invention.” Montemagno, pg. 5, ln, 22-23.
“In one aspect, the artificial photosynthesis platform is encased in a multifunctional material for the production of solar derived liquid fuels. The encasement provides a robust environment for the foam without compromising optical transparency and enables the separation of the liquid fuel (G3P) from the other constituents, while providing antifouling and antimicrobial protection. In one embodiment, the encasement will be synthesized via a sol-gel process which enables control of materials chemistry and micro structure.” Montemagno, pg. 36, ln. 8-13.
“Alternatively, we can convert the G3P to sugar using isomerase and aldolase enzymes and elute the sugar. The G3P to sugar conversion can be accomplished by adding a "conversion chamber" to the encasement. The conversion chamber can be a sol-gel derived inorganic, porous matrix involving the use of metal alkoxides which undergo hydrolysis and condensation polymerization reactions to give rigid solids (gels) of metal oxides such as SiO2, TiO2, AI2O3, ZrO2, etc. with immobilized aldolase and isomerase. Upon entering the conversion chamber, G3P will be converted to sugar due to the immobilized aldolase and isomerase, and the sugar can be subsequently eluted from the conversion chamber. The encasement will be fabricated with an inlet and outlet to facilitate the addition of foam and separation of the biofuel (G3P or sugar).” Montemagno, pg. 38, ln. 13-23.
“By incorporating, for example, short chain diacylphosphotidylcholine into sol-gel derived S1O2, the hygroscopic nature of the lipid and their organization into the uniform SiC -lipid structure suppresses overall water loss so that a water-rich microenvironment is retained. Water evaporation through the porous sol-gel encasement can also be minimized by incorporating polyethylene glycol (PEG) into the sol-gel starting solution to retain a water-rich environment in the foam.” Montemagno, pg. 37, ln. 19-24. That is, the sol-gel containing enzymes in which G3P is converted to sugar is an aqueous media within the broadest reasonable meaning of that term.
Montemagno directly describes the various enzymes needed to convert G3P (glyceraldehyde-3-phosphate) to sugar (i.e. glucose). “The conversion of G3P to hexose is accomplished using triosephosphate isomerase, fructose 1,6-biphosphate aldolase, fructose-1 ,6-bisphosphatase, phosphoglucose isomerase and glucose-6-phosphatase.” Montemagno, pg. 27, ln. 19-21.
Wong, Scheme III, evidences the reactions catalyzed by these enzymes in a pathway for producing glucose. Triosephosphate isomerase (TPI) interconverts G3P and dihydroxyacetone phosphate (DHAP), fructose 1,6-bisphosphate aldolase (FDP) condenses G3P and DHAP to form fructose-1,6-bisphosphate, and phosphoglucose isomerase (PGI) isomerizes fructose-6-phosphate to glucose-6-phosphate (G-6-P). An ordinarily skilled artisan at time of filing would readily understand that fructose-1,6-bisphosphatase hydrolyzes fructose-1,6-bisphosphate to fructose-6-phosphate, which is then convertible to glucose by glucose-6-phosphatase.
As such, Montemagno discloses the following method:
A method for producing glucose 6-phosphate from glyceraldehyde 3-phosphate, comprising: (i) combining glyceraldehyde 3-phosphate, aldolase, triosephosphate isomerase, fructose 1,6-bisphosphatase and phosphoglucose isomerase in an aqueous media/medium and producing glucose 6-phosphate.
Regarding recitation that triosephosphate isomerase, aldolase, fructose 1,6-bisphosphatase and phosphoglucose isomerase are “stabilized” as recited in the rejected claims, the following is noted.
As discussed above, Montemagno directly states that aldolase (i.e. fructose 1,6-bisphosphatase) and isomerase (i.e. phosphoglucose isomerase) are “immobilized” in sol-gel that retains a water-rich microenvironment. “It has been shown that it is possible to immobilize biomolecules which retain their characteristic reactivities and spectroscopic properties in the pores of the sol-gel glass.” Montemagno, pg. 36, ln. 24-26. “Relatively large biomolecules such as proteins and enzymes are trapped inside the pores of the inorganic matrix while small analytes can diffuse in and out. Important benefits of sol-gel technology include a marked improvement in the stability of the biomolecules as well as protection from protease and microorganisms.” Montemagno, pg. 36, ln. 32 through pg. 37, ln. 1.
The above is understood as a direct statement that aldolase and triosephosphate isomerase as present in sol-gel as described are both 1) immobilized in a reaction vessel being the described “conversion chamber” and encapsulated by the sol-gel, and 2) “stabilized” by being trapped inside pores of the sol-gel matrix as to be stabilized aldolase and stabilized triosephosphate isomerase.
Regarding the recitation that fructose 1,6-bisphosphatase and phosphoglucose isomerase are “stabilized” as recited, “Upon entering the conversion chamber, G3P will be converted to sugar due to the immobilized aldolase and isomerase.” However, as reviewed above, more enzymes that aldolase and triosephosphate isomerase are required to convert G3P to glucose-6-phosphate and/or glucose. “The conversion of G3P to hexose is accomplished using triosephosphate isomerase, fructose 1,6-biphosphate aldolase, fructose-1 ,6-bisphosphatase, phosphoglucose isomerase and glucose-6-phosphatase.”
Due to the explicit teachings of Montemagno that “The conversion of G3P to hexose is accomplished using triosephosphate isomerase, fructose 1,6-biphosphate aldolase, fructose-1 ,6-bisphosphatase, phosphoglucose isomerase and glucose-6-phosphatase,” an ordinarily skilled artisan at the time of filling would have been motivated to include all of these enzymes in the conversion chamber as described including such enzymes being present and encapsulated within the sol-gel. That is, while Montemagno explicitly discuss only the aldolase and isomerase (presumed to be triosephosphate isomerase that utilizes G3P directly as a substrate), Montemagno in fact teach that five enzymes as described are required to convert G3P to glucose through a glucose-6-phosphate intermediate. As such, at the time of filing an ordinarily skilled artisan would have been motivated to include all five enzymes taught to be required for conversion of G3P to glucose within the conversion chamber of Montemagno with the same immobilized in the conversion chamber (i.e. reaction vessel) and/or encapsulated via the described sol-gel with the same enzymes “stabilized” thereby such that the same are stabilized triosephosphate isomerase, stabilized aldolase, stabilized fructose-1,6-bisphosphatase and stabilized phosphoglucose isomerase as to meet the features of claims 112, 120 and 122. With regards to claim 122, the taught “a marked improvement in the stability of the biomolecules,” is understood as a description of enablement of enzyme activity in a reaction environment non-native to the enzymes discussed above.
Regarding claims 109, 111, 119 and 121, the discussed conversion chamber is shown in Fig. 8 of Montemagno with underlined annotation added by the examiner:
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As discussed by Montemagno, the “soft gel” encasement contains components for producing G3P that is then output to the conversion chamber as to be a G3P source configured to output G3P. “There will be a semi-permeable membrane dividing the encasement from the sol-gel derived SiO2 capture or conversion chamber, which will permit the diffusion of G3P” from the encasement wherein G3P is generated as to be outputted to the capture/conversion chamber. Montemagno, page 38, lines 22-24.
“The encasement will be fabricated with an inlet and outlet to facilitate the addition of foam and separation of the biofuel (G3P or sugar).” Montemagno, page 38, lines 21-22, Such “foam” contains water such that the described inlet is a water source configured to output water. “Because of drainage, evaporation, and hydrophilicity water-based foams are inherently fragile and relatively short-lived.” Montemagno, page 3, lines 9-10.
The capture/conversion chamber is discussed above as being a single reactor as illustrated in Fig. 8 configured to receive G3P and contains stabilized triosephosphate isomerase, stabilized aldolase, stabilized fructose-1,6-bisphosphatase and stabilized phosphoglucose isomerase immobilized in such reaction vessel, as suggested by Montemagno, for the reasons discussed above as to meet the features of claims 109, 111, 119 and 121. Regarding claim 121, the taught “a marked improvement in the stability of the biomolecules,” is understood as a description of enablement of enzyme activity in a reaction environment non-native to the enzymes discussed above.
Conclusion
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652
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