Paper: 10
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`Entered: September 15, 2015
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`Trials@uspto.gov
`571-272-7822
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`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`AKERMIN, INC.,
`Petitioner,
`
`v.
`
`CO2 SOLUTIONS INC.,
`Patent Owner.
`____________
`
`Case IPR2015-00880
`Patent 8,329,458 B2
`____________
`
`
`
`Before MICHAEL P. TIERNEY, JON B. TORNQUIST, and
`ELIZABETH M. ROESEL, Administrative Patent Judges.
`
`ROESEL, Administrative Patent Judge.
`
`DECISION
`Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
`
`
`
`
`
`
`
`
`
`Entered: September 15, 2015
`
`
`
`
`
`
`Trials@uspto.gov
`571-272-7822
`
`
`
`
`
`
`
`
`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`AKERMIN, INC.,
`Petitioner,
`
`v.
`
`CO2 SOLUTIONS INC.,
`Patent Owner.
`____________
`
`Case IPR2015-00880
`Patent 8,329,458 B2
`____________
`
`
`
`Before MICHAEL P. TIERNEY, JON B. TORNQUIST, and
`ELIZABETH M. ROESEL, Administrative Patent Judges.
`
`ROESEL, Administrative Patent Judge.
`
`DECISION
`Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
`
`
`
`
`
`
`
`IPR2015-00880
`Patent 8,329,458 B2
`
`
`Petitioner, Akermin, Inc., filed a Corrected Petition seeking inter
`
`partes review of claims 1–4, 15–19, 22–28, and 40–43 of U.S. Patent No.
`
`8,329,458 B2 (Ex. 1001, “the ’458 patent”). Paper 5 (“Pet.”). Patent
`
`Owner, CO2 Solutions Inc., filed a Preliminary Response. Paper 9 (“Prelim.
`
`Resp.”) Pursuant to 35 U.S.C. § 314(a), we determine that the information
`
`presented in the Petition and the Preliminary Response shows that there is a
`
`reasonable likelihood that Petitioner would prevail with respect to at least
`
`one of the claims challenged in the Petition. For the reasons and on the
`
`grounds set forth below, we institute an inter partes review of claims 1–4,
`
`15–19, 22–28, and 40–43 of the ’458 patent.
`
`Our findings of fact and conclusions of law are based on the record
`
`developed thus far, before the filing of Patent Owner’s Response. This is
`
`not a final decision as to the patentability of any challenged claim. Our final
`
`decision will be based on the full record developed during the trial.
`
`I. BACKGROUND
`
`A. Related Proceedings
`
`The parties represent that they are not aware of any other judicial or
`
`administrative matter that would affect, or be affected by, a decision in this
`
`proceeding. Pet. 1; Paper 7, 2.
`
`B. Evidence Relied Upon
`
`Petitioner’s patentability challenges are based on the following
`
`references:
`
`2
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`Patent 8,329,458 B2
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`
`Reference
`
`Patent/Pub. No.
`
`Date
`
`Exhibit No.
`
`Bonaventura ’416 US 4,427,416
`
`issued Jan. 24, 1984
`
`Ex. 1005
`
`Bonaventura ’987 US 4,602,987
`
`issued Jul. 29, 1986
`
`Ex. 1004
`
`Rau
`
`WO 00/10691
`
`published Mar. 2, 2000 Ex. 1007
`
`
`Douglas N. Dean et al., Batch Absorption of CO2 by Free and
`
`Microencapsulated Carbonic Anhydrase, 16 INDUS. ENG’G & CHEMISTRY
`
`FUNDAMENTALS 260 (1977) (“Dean”), Ex. 1006.
`
`Arthur Kohl & Richard Nielsen, Gas Purification (5th ed. 1997)
`
`(“Kohl”), Ex. 1008.
`
`Jovica D. Badjic & Nenad M. Kostic, Effects of Encapsulation in Sol-
`
`Gel Silica Glass on Esterase Activity, Conformational Stability, and
`
`Unfolding of Bovine Carbonic Anhydrase II, 11 CHEMISTRY MATERIALS
`
`3671 (1999) (“Badjic”), Ex. 1009.
`
`In addition, Petitioner relies on the Declaration of Louis DeFilippi,
`
`Ex. 1003.1
`
`C. Asserted Grounds of Unpatentability
`
`Reference(s)
`
`Basis
`
`Claims
`
`Bonaventura ’987
`
`§ 102 1–3, 15, 17, 24–27, 40, 41, and 43
`
`Bonaventura ’987 and
`Bonaventura ’416
`
`§ 103 1–3, 15–17, 24–27, and 40–43
`
`Bonaventura ’987 and Badjic § 103 1, 4, 25, and 28
`
`
`
`1 Citations exhibits, other than Exhibit 1002, are to the original page or
`paragraph numbers, not the page numbers added by Petitioner or Patent
`Owner.
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`3
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`Reference(s)
`
`Basis
`
`Claims
`
`Bonaventura ’987 and Kohl
`
`§ 103 1, 18, and 19
`
`Dean and Rau
`
`§ 103 1, 2, 15, 16, 22–26, and 40–43
`
`
`
`II. ANALYSIS
`
`A. The ’458 Patent (Ex. 1001)
`
`The ’458 patent relates to a triphasic bioreactor and process using
`
`carbonic anhydrase for treating carbon dioxide (CO2)-containing gas for
`
`purposes of gas effluent treatment and air purification. Ex. 1001, Abstract,
`
`1:19–23, claims 1, 25. The triphasic bioreactor comprises a reaction
`
`chamber with a liquid and biocatalysts in suspension in the liquid, for
`
`catalyzing a reaction between the gas and the liquid to obtain a treated gas
`
`and a solution containing a reaction product. Id. at Abstract.
`
`Figure 1 of the ’458 patent is reproduced below:
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`4
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`Figure 1 is a cross-sectional side view of a triphasic bioreactor. Ex. 1001,
`
`4:66–67. The bioreactor includes reaction chamber 2 filled with biocatalysts
`
`4 in suspension in liquid 3, liquid inlet 5, liquid outlets 6, and gas outlet 7, in
`
`fluid communication with reaction chamber 2. Id. at 5:25–30. Gas 10 to be
`
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`treated is bubbled via means 8 into the liquid. Biocatalysts 4 biocatalyze a
`
`reaction between the gas to be treated and the liquid to obtain treated gas 11
`
`and solution 12 containing a reaction product. Solution 12 is released
`
`through liquid outlet 6, while retention device 9 retains the biocatalysts
`
`within the reaction chamber. Treated gas 11 is released through gas outlet 7.
`
`Id. at 5:39–52.
`
`The triphasic bioreactor is used for removing carbon dioxide from gas
`
`effluent 10 containing carbon dioxide. In such a case, liquid 3 is an aqueous
`
`solution, and biocatalysts 4 are preferably carbonic anhydrase enzymes,
`
`which are capable of catalyzing the conversion of dissolved carbon dioxide
`
`into an aqueous solution 12 containing hydrogen ions and bicarbonate ions.
`
`Ex. 1001, 8:30–38.
`
`B. Illustrative Claim
`
`Claims 1 and 25 are illustrative of the challenged claims and are
`
`reproduced below:
`
`1. A carbonic anhydrase bioreactor for treating a CO2-
`containing gas, comprising:
`a reaction chamber for receiving a liquid;
`carbonic anhydrase provided on or in substrates that are
`in suspension within the liquid for catalyzing a reaction of CO2
`into bicarbonate and hydrogen ions to obtain a treated gas and
`an ion-rich solution, wherein the substrates comprise porous
`substrates and the carbonic anhydrase are entrapped in the
`porous substrates;
`a liquid inlet in fluid communication with the reaction
`chamber for providing the reaction chamber with the liquid;
`a gas inlet connected to the reaction chamber for
`providing the CO2-containing gas to be treated into the reaction
`chamber in order to contact the liquid;
`a liquid outlet in fluid communication with the reaction
`chamber for releasing the ion-rich solution; and
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`a gas outlet in fluid communication with the reaction
`chamber to release the treated gas.
`
`25. A process using carbonic anhydrase for treating a
`CO2-containing gas, comprising:
`suspending substrates within a liquid provided to a
`reaction chamber, carbonic anhydrase being provided on or in
`the substrates, wherein the substrates comprise porous
`substrates and the carbonic anhydrase are entrapped in the
`porous substrates;
`contacting the CO2-containing gas to be treated with the
`liquid within the reaction chamber in the presence of the
`carbonic anhydrase, to promote the chemical conversion of the
`dissolved CO2 into an ion-rich solution containing hydrogen
`ions and bicarbonate ions and obtaining a treated gas; releasing
`the ion-rich solution from the reaction chamber; and
`releasing the treated gas from the reaction chamber.
`
`C. Claim Construction
`
`In an inter partes review, claim terms in an unexpired patent are given
`
`their broadest reasonable interpretation in light of the specification of the
`
`patent in which they appear. 37 C.F.R. § 42.100(b); In re Cuozzo Speed
`
`Tech., LLC, 793 F.3d 1268, 1275–79 (Fed. Cir. 2015). Claim terms are
`
`given their ordinary and customary meaning, as understood by one of
`
`ordinary skill in the art in the context of the entire disclosure. In re
`
`Translogic Tech., Inc., 504 F.3d 1249, 1257 (Fed. Cir. 2007).
`
`We construe claim terms consistent with the specification of the
`
`patent. Microsoft Corp. v. Proxyconn, Inc., 789 F.3d 1292, 1298 (Fed. Cir.
`
`2015) (“claims should always be read in light of the specification and
`
`teachings in the underlying patent”) (quoting In re Suitco Surface, Inc., 603
`
`F.3d 1255, 1260 (Fed. Cir. 2010)).
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`Petitioner and Patent Owner each propose constructions for several
`
`claim terms. Pet. 10–12; Prelim. Resp. 17–22. For purposes of this
`
`decision, only the claim term “entrapped” requires explicit construction.
`
`entrapped in the porous substrates
`
`The phrase “entrapped in the porous substrates” appears in
`
`independent claims 1 and 25, each of which recites: “the carbonic anhydrase
`
`are entrapped in the porous substrates.”
`
`Applying the broadest reasonable construction, we start with the plain
`
`and ordinary meaning of “entrap,” which is “captured and held.” Ex. 3001
`
`(Webster’s Third New International Dictionary definition for “entrap”: “to
`
`capture and hold (a substance)”). As discussed below, we accept some, but
`
`not all, of the parties’ proposals to further define the term.
`
`Petitioner proposes the following construction for “entrapped in”: the
`
`enzyme is physically trapped within the structure of the substrate while
`
`retaining at least some of its activity. Pet. 11. Patent Owner argues that
`
`“entrapped in” excludes encapsulation and should be construed to mean that
`
`the enzyme molecules are free in solution, but restricted in movement within
`
`the interstitial confines of the porous substrate lattice network and accessible
`
`to reactants (e.g., CO2). Prelim. Resp. 20–22.
`
`The claims themselves describe the function of the entrapped enzymes
`
`as catalyzing and promoting a reaction by which carbon dioxide (CO2) is
`
`converted into bicarbonate and hydrogen ions. Ex. 1001, 10:17–22 (claim
`
`1), 11:40–12:3 (claim 25). This description in the claims supports a
`
`requirement that the entrapped enzymes retain at least some of their activity,
`
`as set forth in Petitioner’s proposed construction, and that the enzymes be
`
`accessible to reactants (e.g., CO2), as set forth in Patent Owner’s proposed
`
`8
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`Patent 8,329,458 B2
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`construction. The former requirement is further supported by Bonaventura
`
`’416, which is cited by Petitioner and is cited art in the ’458 patent. Pet. 11;
`
`Ex. 1005, 6:38–41 (“Optimally, entrapment is analogous to placing a cage
`
`around the biologically active material. This cage, or network, entraps the
`
`material but does not render it inactive.”) The latter requirement is further
`
`supported by the claims themselves, which describe the substrates as
`
`“porous.”2
`
`As support for their respective constructions for “entrapped,”
`
`Petitioner and Patent Owner cite the following passages from the
`
`specification of the ’458 patent:
`
`For the purpose of the invention, the biocatalysts may also be
`entrapped in a porous substrate, for example, an insoluble gel
`particle such as silica, alginate, alginate/chitosane,
`alginate/carboxymethylcellulose, etc. For the purpose of the
`invention, biocatalysts may also be immobilized on solid
`packing in suspension in the liquid, such as enzymes covalently
`bound to plastic packing. Alternatively, enzymes might be in a
`free state, or chemically linked in an albumin or PEG network.
`
`Ex. 1001, 6:23–31; see Pet. 11.
`
`The enzyme carbonic anhydrase, . . . may be made to form part
`of a complex . . . Different types of enzyme complexes may be
`formed. . . . However, with red blood cells, the enzymes rapidly
`leak out and are lost. Encapsulation techniques may therefore
`overcome this problem. Enzymes may be immobilized on solid
`packing. . . . Enzymes may also be entrapped in insoluble gel
`particles . . . or covalently linked or non[-]covalently linked in a
`network . . . .
`
`Id. at 8:51–65; see Prelim. Resp. 21.
`
`
`
`2 Petitioner proposes to construe “porous” as having minute spaces or holes
`through which liquid or air may pass, Pet. 11, and Patent Owner does not
`contest Petitioner’s proposed construction.
`
`9
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`The cited passages describe covalent, non-covalent, and chemical
`
`bonding or linking as one way to immobilize enzyme biocatalysts. These
`
`passages do not exclude such bonding or linking from the scope of the term
`
`“entrapped.” Nor do they require physical (as opposed to chemical)
`
`entrapment. Bonaventura ’416 describes “entrapment” as “analogous to
`
`placing a cage around the biologically active material.” Ex. 1005, 6:38–40.
`
`That description also does not exclude chemical bonding or linking, as
`
`disclosed in the ’458 patent. We therefore decline to construe “entrapped”
`
`as requiring the enzyme to be physically trapped within the structure of the
`
`substrate, as proposed by Petitioner.
`
`Patent Owner argues that the ’458 patent defines encapsulation and
`
`entrapment as mutually exclusive and distinct forms of enzyme
`
`immobilization, citing the above-quoted passage from column 8. Prelim.
`
`Resp. 21. The cited passage describes several encapsulation techniques that
`
`may overcome a problem encountered when using red blood cells to
`
`complex with enzymes. Ex. 1001, 8:51–65. One such technique is
`
`entrapment. Id. Accordingly, we are not persuaded by Patent Owner’s
`
`argument that the ’458 patent defines entrapment as excluding
`
`encapsulation. See Thorner v. Sony Computer Entertainment Am. LLC, 669
`
`F.3d 1362, 1365 (Fed. Cir. 2012) (“To act as its own lexicographer, a
`
`patentee must clearly set forth a definition of the disputed claim term other
`
`than its plain and ordinary meaning.”) (internal quotes and citation omitted).
`
`Patent Owner further argues that “entrapped” should be construed as
`
`requiring that the enzyme molecules be free in solution, but restricted in
`
`movement within the interstitial confines of the porous substrate lattice
`
`network. Prelim. Resp. 13–16, 22 (citing Ex. 2002). Patent Owner proposes
`
`10
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`this construction in an effort to distinguish entrapment from encapsulation,
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`which is not supported by the ’458 patent, as just discussed. The treatise
`
`cited by Patent Owner supports that entrapment is similar to encapsulation,
`
`with the difference relating to the structure and composition of the porous
`
`substrates (gel lattice vs. semipermeable membrane). Ex. 2002, 8–9.3
`
`Independent claims 1 and 25 require porous substrates, but in contrast to the
`
`dependent claims, they do not specify any particular structure or
`
`composition, such as a gel lattice. Compare Ex. 1001, claims 1 and 25 (“the
`
`carbonic anhydrase are entrapped in the porous substrates”), with id. claims
`
`3 and 27 (“the porous substrates comprise particles composed of an
`
`insoluble gel”). See Phillips v. AWH Corp., 415 F.3d 1303, 1315 (Fed. Cir.
`
`2005) (en banc) (“the presence of a dependent claim that adds a particular
`
`limitation gives rise to a presumption that the limitation in question is not
`
`present in the independent claim”). The ’458 patent does not describe the
`
`porous substrates as having interstitial confines or a lattice network. Nor
`
`does the ’458 patent exclude a semipermeable membrane as a means for
`
`immobilizing the enzymes. Accordingly, we are not persuaded by Patent
`
`Owner’s proposed construction to the extent that it seeks to incorporate these
`
`limitations into the meaning of “entrapped.”
`
`Accordingly, consistent with the plain and ordinary meaning of
`
`“entrap,” Ex. 3001, for purposes of this decision, we construe “entrapped in
`
`the porous substrates” to mean captured and held in the porous substrates,
`
`while retaining at least some of their activity and being accessible to
`
`reactants (e.g., CO2).
`
`
`
`3 Excerpts from Gordon F. Bickerstaff, Immobilization of Enzymes and
`Cells, 1 METHODS IN BIOTECHNOLOGY 1 (1997).
`
`11
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`Our claim construction should not be viewed as final. The parties
`
`may submit additional arguments and evidence regarding claim construction.
`
`Our final decision will be based on the full record developed during the trial.
`
`D. Analysis of Asserted Grounds of Unpatentability
`
`i. Anticipation by Bonaventura ’987
`
`Petitioner asserts that claims 1–3, 15, 17, 24–27, 40, 41, and 43 are
`
`anticipated by Bonaventura ’987. Patent Owner argues that Bonaventura
`
`’987 does not disclose carbonic anhydrase provided on or in substrates that
`
`are in suspension within the liquid.
`
`1. Bonaventura ’987 (Ex. 1004)
`
`Bonaventura ’987 discloses, in relevant part, a method and apparatus
`
`for removing carbon dioxide from a fluid using carbonic anhydrase as an
`
`enzyme catalyst. Ex. 1004, 22:55–63, 23:40–44, 25:7–20, 30:1–32:38, Figs.
`
`5–8. The method is illustrated in Figure 5, which is reproduced below:
`
`
`
`Figure 5 is a schematic diagram of a generalized process for removing
`
`carbon dioxide from a fluid. Id. at 6:55–58. According to Bonaventura
`
`’987, water and a fluid containing carbon dioxide are brought into contact
`
`with immobilized carbonic anhydrase, which results in the removal of
`
`carbon dioxide from the fluid and produces an aqueous solution of
`
`bicarbonate. Id. at 24:19–28, 30:1–11.
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`An apparatus for carrying out the method is illustrated in Figure 6,
`
`which is reproduced below:
`
`
`
`Figure 6 is a schematic diagram of an apparatus for removing carbon dioxide
`
`from a fluid. Ex. 1004, 6:59–62. Figure 6 shows: container 21,
`
`compartment 22 through which flows fluid containing carbon dioxide to be
`
`removed, compartment 23 containing immobilized enzyme 24, gas
`
`permeable membrane 25 separating compartment 22 from compartment 23,
`
`inlet 27 for fluid containing carbon dioxide, outlet 28 for fluid from which
`
`carbon dioxide has been removed, water inlet 29, and outlet 30 for aqueous
`
`carbonic acid. Id. at 30:15–21, 30:30–37. According to Bonaventura ’987,
`
`the carbon dioxide passes from chamber 22 across gas permeable membrane
`
`25 into chamber 23, where it is converted by immobilized enzyme 24 into
`
`carbonic acid.4 Id. at 30:37–47. Regarding enzyme immobilization,
`
`Bonaventura ’987 discloses:
`
`If immobilized enzyme 24 is attached to the walls of
`compartment 23 or if immobilized enzyme 24 is present on a
`solid substrate which is not capable of flowing out of
`compartment 24, no further entrappment [sic] of the enzyme or
`
`
`4 According to Patent Owner, when the hydration of CO2 is catalyzed by
`carbonic anhydrase, carbonic acid is predominantly converted to bicarbonate
`and hydrogen ions in solution. Prelim. Resp. 36 n.3.
`
`13
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`its support material is needed. However, in the event that the
`support material is small (for example, gel particles capable of
`flowing with water) means for entrapping the flowable
`substrate, shown in FIG. 6 as screens 26a and 26b, are required.
`
`Id. at 30:20–30.
`
`Another embodiment of an enzyme reactor is shown in Figure 7,
`
`which is reproduced below:
`
`
`
`Figure 7 shows a vertical enzyme reactor for removing carbon dioxide by
`
`the countercurrent flow of water and a gas stream containing carbon dioxide.
`
`Ex. 1004, 6:63–65, 30:54–60. In the Figure 7 embodiment, gas containing
`
`carbon dioxide to be removed is injected through inlet 27 into container 21
`
`and diffuses upwardly through the reaction zone. Water is injected through
`
`inlet 29 and flows downwardly through the reaction zone. Carbon dioxide
`
`reacts with water under the influence of immobilized enzyme 24 and is
`
`converted into carbonic acid.5 Gas from which carbon dioxide has been
`
`removed exits the reactor through outlet 28, and a carbonic acid solution
`
`
`
`5 See n.7, supra.
`
`14
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`exits through outlet 30. Id. at 30:66–31:11. Regarding enzyme
`
`immobilization in the Figure 7 embodiment, Bonaventura ’987 discloses:
`
`[C]arbonic anhydrase is immobilized on a porous substrate . . .
`24[, which] is held in place by a substrate support 26c, which
`may be a fine screen when the support by which the enzyme is
`immobilized is a porous gel.
`
`Id. 30:59–63.
`
`2. Claims 1–3, 15, 17, 24–27, 40, 41, and 43
`
`Petitioner and its declarant assert that claims 1–3, 15, 17, 24–27, 40,
`
`41, and 43 are anticipated by at least the Figure 6 embodiment of
`
`Bonaventura ’987. Pet. 20; Ex. 1003 ¶ 78. In support of this assertion,
`
`Petitioner and its declarant provide claim charts citing to particular
`
`disclosures in Bonaventura ’987. Pet. 21–28; Ex. 1003 ¶¶ 78–90.
`
`Regarding the “in suspension” limitation of claim 1 and the “suspending”
`
`limitation of claim 25, Petitioner and its declarant cite Bonaventura ’987’s
`
`disclosure, Ex. 1004, 30:26–30, that “in the event that the support material is
`
`small (for example, gel particles capable of flowing with water) means for
`
`entrapping the flowable substrate, shown in FIG. 6 as screens 26a and 26b,
`
`are required.” Pet. 19–20, 21–22, 26; Ex. 1003 ¶¶ 54, 79 (p. 35), 85 (p. 44).
`
`Patent Owner argues that Bonaventura ’987 does not disclose the “in
`
`suspension” or “suspending” feature of the claims. Prelim. Resp. 23–26.
`
`Patent Owner agrees that Bonaventura ’987 discloses enzyme-containing
`
`substrates that are capable of flowing with water, but argues that “being
`
`‘capable’ of flowing does not mean that particles of the enzyme-containing
`
`substrate would flow, much less be ‘in suspension’ during operation of the
`
`apparatus. . . .” Id. at 25. Patent Owner further argues that, in Bonaventura
`
`’987’s Figure 6 embodiment, substrate particles that are capable of flowing
`
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`would form a packed mass of particles, rather than remaining “in
`
`suspension,” as recited in the claims. Id.
`
`On this record, we are persuaded that Petitioner’s evidence, including
`
`Bonaventura ’987’s Figure 6 showing enzyme-supporting substrate particles
`
`24 dispersed throughout a fluid and Bonaventura ’987’s disclosure of “gel
`
`particles” that are “capable of flowing with water” resulting in a “flowable
`
`substrate,” Ex. 1004, Fig. 6, 30:26–30, is sufficient to demonstrate a
`
`reasonable likelihood of prevailing on its assertion that Bonaventura ’987
`
`discloses the “in suspension” and “suspending” features of the claims.
`
`We are not persuaded by Patent Owner’s arguments to the extent they
`
`are inconsistent with Patent Owner’s characterization of the “in suspension”
`
`feature during prosecution of the ’458 patent. Compare Prelim. Resp. 25
`
`(“being ‘capable’ of flowing does not mean that particles of the enzyme-
`
`containing substrate would . . . be ‘in suspension’”), with Ex. 1002, 72
`
`(describing “in suspension” feature as requiring that “the substrates flow
`
`with and within the liquid”); see Prelim. Resp. 7–8. Furthermore, we do not
`
`discern a meaningful difference between “capable of flowing” and “would
`
`flow” in the context of Bonaventura ’987’s Figure 6 embodiment, in which
`
`water is disclosed as flowing through compartment 23 containing
`
`immobilized enzyme 24, such as gel particles. Ex. 1004, Fig. 6, 30:26–30,
`
`30:35–37, 30:42–47. Patent Owner does not direct us to evidence, in
`
`Bonaventura ’987 or elsewhere in the current record, sufficient to
`
`demonstrate that flowable substrate particles 24 in Bonaventura ’987’s
`
`Figure 6 embodiment would form a packed mass of particles or that that
`
`these particles differ from flowable substrate particles 4 in the Figure 1
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`embodiment of the ’458 patent in a way that only the latter can be “in
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`suspension.”
`
`Patent Owner next argues that the Patent Office has already
`
`determined that a reference having the same disclosure as Bonaventura ’9876
`
`does not disclose the “in suspension” or “suspending” feature of the claims.
`
`Prelim. Resp. 26–28. During prosecution of the ’458 patent, Patent Owner
`
`argued that Bonaventura ’209’s substrates are mounted or fixed within the
`
`reaction chamber, Ex. 1002, 29, 72, and did not draw the Examiner’s
`
`attention to Bonaventura ’209’s disclosure of “gel particles” that are
`
`“capable of flowing with water.” Patent Owner does not direct us to
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`evidence showing that the Patent Office considered the disclosures relied
`
`upon by Petitioner as teaching the “in suspension” and “suspending”
`
`features of the claims. We therefore decline to exercise our authority to
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`deny institution pursuant to 35 U.S.C. § 325(d), as requested by Patent
`
`Owner.
`
`Next, Patent Owner argues that Bonaventura ’987 does not disclose
`
`that the CO2-containing gas to be treated contacts the liquid, as recited in
`
`claims 1 and 25 of the ’458 patent. Prelim. Resp. 28–29. Patent Owner
`
`explains that, in Bonaventura ’987’s Figure 6 embodiment, only CO2, and
`
`not the fluid accompanying the CO2, passes through membrane 25 and
`
`contacts the liquid in chamber 23. Id. Based on the current record,
`
`however, we are not persuaded that this argument is sufficient to distinguish
`
`
`
`6 According to Patent Owner, Bonaventura ’209 (US 4,761,209, issued
`August 2, 1988, Ex. 2001) is a division of Bonaventura ’987, contains the
`same disclosure as Bonaventura ’987, and was cited by the Examiner during
`prosecution of the ’458 patent. Prelim. Resp. 7 n.2, 27; see also Pet. 7.
`
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`the claimed reactor and process from Bonaventura ’987 because there is no
`
`requirement in claims 1 or 25 that the gas that contacts the liquid comprises
`
`any gas other than CO2.
`
`Petitioner and its declarant identify disclosures relating to at least
`
`Bonaventura ’987’s Figure 6 embodiment as corresponding to each of the
`
`remaining limitations of claims 1–3, 15, 17, 24–27, 40, 41, and 43. Pet. 21–
`
`28; Ex. 1003 ¶¶ 79–91. Aside from the “in suspension”/“suspending” and
`
`gas/liquid contact limitations, Patent Owner does not challenge Petitioner’s
`
`identifications at this stage. Accordingly, on this record, we are persuaded
`
`that Petitioner demonstrates a reasonable likelihood of prevailing on its
`
`assertion that Bonaventura ’987 anticipates each of claims 1–3, 15, 17, 24–
`
`27, 40, 41, and 43.
`
`ii. Obviousness in view of Bonaventura ’987 and Bonaventura ’416
`
`Petitioner asserts that claims 1–3, 15–17, 24–27, and 40–43 are
`
`unpatentable under 35 U.S.C. § 103 as obvious over Bonaventura ’987 and
`
`Bonaventura ’416.
`
`Petitioner asserts that Bonaventura ’987’s Figure 7 embodiment has
`
`all of the reactor limitations of the ’458 patent claims. Pet. 29. Petitioner
`
`acknowledges that Bonaventura ’987’s description of Figure 7 does not
`
`expressly disclose the “in suspension” or “suspending” feature of claims 1
`
`and 25, but asserts that this feature is disclosed by Bonaventura ’987’s
`
`description of Figures 6 and 8. Id. at 29–30. Petitioner further asserts that
`
`Bonaventura ’987 references Bonaventura ’416, which teaches using
`
`polyurethane gel particles for enzyme immobilization. Id. at 30 (citing
`
`Ex. 1004, 27:35–40 and Ex. 1005, 6:25–7:55, 10:20–12:29, Figs. 1–3).
`
`According to Petitioner and its declarant, it would have been obvious to one
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`of ordinary skill in the art to implement Bonaventura ’987’s Figure 7
`
`embodiment using polyurethane gel particles, as taught by Bonaventura
`
`’416, and to use such gel particles as the porous substrate 24, as taught by
`
`Bonaventura ’987 in connection with Figures 6 and 8. Id. at 31; Ex. 1003
`
`¶ 96. Petitioner and its declarant assert that one of ordinary skill in the art
`
`would have been motivated to use polyurethane gel in the form of particles
`
`(as opposed to an intact mass) because particles are easier to replace in a
`
`reactor than a fixed substrate. Id. (citing Ex. 1018, 464–4657); Ex. 1003
`
`¶ 97.
`
`Patent Owner argues that Bonaventura ’416 does not teach or suggest
`
`using particles “in suspension” in a liquid while contacting the liquid with a
`
`gas and that this feature is not disclosed by a combination of the
`
`Bonaventura patents. Prelim. Resp. 37–39 (relying on previously presented
`
`arguments regarding Bonaventura ’987). Patent Owner further argues that
`
`the Petition and the Declaration do not explain how using particles, as taught
`
`by Bonaventura ’416, would have motivated a skilled person to use those
`
`particles “in suspension” in a liquid while contacting CO2-containing gas
`
`with the liquid. Id. at 39–40.
`
`As acknowledged by Petitioner, Bonaventura ’987’s description of the
`
`Figure 7 embodiment does not expressly disclose gel particles capable of
`
`flowing with water or a flowable substrate. Instead, the description of
`
`Figure 7 discloses a “porous gel,” without specifying whether the gel is in
`
`the form of particles or an intact mass. Ex. 1004, 30:60–63. At this stage,
`
`
`
`7 A.A.C.M. Beenackers & W.P.M. van Swaaij, Slurry Reactors,
`Fundamentals and Applications,110 CHEMICAL REACTOR DESIGN & TECH.
`463 (H. I. DE LASA ED., 1986).
`
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`Patent Owner does not dispute Petitioner’s evidence that one of ordinary
`
`skill in the art would have been motivated to use porous gel in the form of
`
`particles, rather than an intact mass. Compare Pet. 31 (citing Ex. 1003 ¶ 97
`
`and Ex. 1018, 464–465), with Prelim. Resp. 38 (conceding that “a skilled
`
`person may have been motivated to use the ground particles of Bonaventura
`
`’416 in reactors disclosed [in] Bonaventura ’987”); id. at 39 (conceding that
`
`“[i]nactive catalyst in the form of substrate particles may be more easily
`
`removed from within a reaction chamber than a fixed substrate”).
`
`Bonaventura ’416 discloses that “gel material can be ground and
`
`sorted into gel particles of defined size.” Ex. 1005, 7:33–34. Bonaventura
`
`’987 discloses that small gel particles are “capable of flowing with water,”
`
`resulting in a “flowable substrate,” and Figure 7 shows enzyme-supporting
`
`substrate particles 24 dispersed throughout a fluid. Ex. 1004, Fig. 7, 30:26–
`
`30. Because Bonaventura ’987 discloses that gel particles are “capable of
`
`flowing with water,” and depicts such particles as being dispersed
`
`throughout a fluid, we are persuaded that Petitioner’s evidence is sufficient
`
`to demonstrate a reasonable likelihood of prevailing on its assertion that the
`
`“in suspension” and “suspending” features of the claims would have been
`
`obvious in view of the combined teachings of Bonaventura ’416 and
`
`Bonaventura ’987.
`
`Patent Owner argues that, in Bonaventura ’987’s Figure 7
`
`embodiment, the solid support is a packed bed that would remain packed
`
`regardless of whether it is an intact mass or ground particles. Prelim. Resp.
`
`40. Patent Owner does not direct us to evidence, in Bonaventura ’987 or
`
`elsewhere in the current record, sufficient to demonstrate that the substrate
`
`particles 24 in Bonaventura ’987’s Figure 7 embodiment would form a
`
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`packed bed of particles or that that these particles differ from flowable
`
`substrate particles 4 in the Figure 1 embodiment of the ’458 patent in a way
`
`that only the latter can be “in suspension.” Accordingly, on this record, we
`
`are not persuaded that using gel particles “in suspension” would require a
`
`change in operation of Bonaventura ’987’s Figure 7 embodiment, as argued
`
`by Patent Owner. Prelim. Resp. 41–42.
`
`Regarding claims 16 and 42, Petitioner and its declarant submit
`
`evidence that the recited filtration techniques (microfiltration and
`
`ultrafiltration) were well known, readily available, and effective for the same
`
`purpose as screens 26a, 26b, and 26c of Bonaventura ’987. Pet. 30, 37, 42
`
`(citing Ex. 1011,8 3 (Table 1.1) & 6 and Ex. 10209); Ex. 1003 ¶¶ 104–105,
`
`113–114; see KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007)
`
`(“when a patent claims a structure already known in the prior art that is
`
`altered by the mere substitution of one element for another known in the
`
`field, the combination must do more than yield a predictable result”).
`
`Petitioner and its declarant identify disclosures relating to at least
`
`Bonaventura ’987’s Figure 7 embodiment as corresponding to each of the
`
`remaining limitations of claims 1–3, 15, 17, 24–27, 40, 41, and 43. Pet. 32–
`
`42; Ex. 1003 ¶¶ 99–103, 106–112, 115. Aside from the “in
`
`suspension”/“suspending” limitations, Patent Owner does not challenge
`
`Petitioner’s obviousness contentions based on Bonaventura ’987 and
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