Trials@uspto.gov
`571-272-7822
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`Paper: 25
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` Entered: August 29, 2016
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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.
`
`FINAL WRITTEN DECISION
`35 U.S.C. § 318 and 37 C.F.R. § 42.73
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`

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`IPR2015-00880
`Patent 8,329,458 B2
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`
`In this inter partes review, instituted pursuant to 35 U.S.C. § 314,
`Akermin, Inc. (“Petitioner”) challenges the patentability 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”), owned by CO2 Solutions Inc. (“Patent Owner”).
`We have jurisdiction under 35 U.S.C. § 6(c). This final written
`decision is issued pursuant to 35 U.S.C. § 318(a) and 37 C.F.R. § 42.73.
`For the reasons that follow, we determine that Petitioner has shown by
`a preponderance of the evidence that claims 1, 2, 15, 16, 22–26, and 40–43
`of the ’458 patent are unpatentable, but has not shown that claims 3, 4, 17–
`19, 27, and 28 of the ’458 patent are unpatentable.
`
`I. BACKGROUND
`A. Procedural History
`On March 20, 2015, Petitioner filed a Corrected Petition requesting
`inter partes review of claims 1–4, 15–19, 22–28, and 40–43 of the ’458
`patent. Paper 5 (“Pet.”). On June 17, 2015, Patent Owner filed a
`Preliminary Response. Paper 9 (“Prelim. Resp.”)
`On September 15, 2015, we instituted inter partes review of claims 1–
`4, 15–19, 22–28, and 40–43. Paper 10 (“Decision to Institute” or “Dec.”).
`On December 15, 2015, Patent Owner filed a Patent Owner Response.
`Paper 14 (“PO Resp.”) On March 17, 2016, Petitioner filed a Reply To
`Patent Owner’s Response. Paper 17 (“Pet. Reply”).
`Petitioner submitted a Declaration of Dr. Louis DeFilippi with the
`Petition. Ex. 1003 (“DeFilippi Decl.”). Patent Owner cross-examined
`Dr. DeFilippi and filed a transcript of the deposition testimony as Exhibit
`2017 (“DeFilippi Dep.”). Patent Owner submitted a Declaration of
`Dr. Louis Fradette with the Patent Owner Response. Ex. 2004 (“Fradette
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`Decl.”). Petitioner cross-examined Dr. Fradette and filed a transcript of the
`deposition testimony as Exhibit 1027 (“Fradette Dep.”).
`An oral hearing was held June 9, 2016. A transcript of the hearing
`was entered in the record. Paper 24 (“Tr.”).
`B. Related Proceedings
`No proceedings involving the ’458 patent have been identified by the
`parties. See Pet. 1; Paper 7, 2. Petitioner asserts that, on March 1, 2016,
`Patent Owner filed and served a complaint against Petitioner for
`infringement of patents involving “similar subject matter” and asserts that
`the lawsuit, captioned CO2 Solutions Inc. v. Akermin, Inc., Civil Action No.
`1:15-cv-01123 (D. Del.), “may be affected by a decision in this proceeding.”
`Paper 19, 2.
`
`C. 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. 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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`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, and liquid inlet 5, liquid outlet 6, and gas outlet 7
`in fluid communication with reaction chamber 2. Id. at 5:25–30. Gas 10 to
`be 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
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`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.
`Id. at 8:30–38.
`
`D. Illustrative Claims
`Claims 1 and 25 are illustrative of the challenged claims and are
`reproduced below, with bold emphasis added to identify phrases that are the
`focus of the parties’ arguments:
`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
`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:
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`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.
`
`E. Petitioner’s Asserted References
`Petitioner’s asserted grounds of unpatentability are based on the
`following references:
`Bonaventura et al., US 4,602,987, issued July 29, 1986
`(“Bonaventura ’987”), Ex. 1004;
`Bonaventura et al., US 4,427,416, issued January 24, 1984
`(“Bonaventura ’416), Ex. 1005;
`Douglas N. Dean et al., Batch Absorption of CO2 by Free and
`Microencapsulated Carbonic Anhydrase, 16 INDUS. ENG’G &
`CHEMISTRY FUNDAMENTALS 452–458 (1977) (“Dean”), Ex. 1006;
`Rau et al., WO 00/10691, published Mar. 2, 2000 (“Rau”), Ex.
`
`1007;
`
`Arthur Kohl & Richard Nielsen, GAS PURIFICATION 330–414
`(5th ed. 1997) (“Kohl”), Ex. 1008; and
`Jovica D. Badjic & Nenad M. Kostic, Effects of Encapsulation
`in Sol-Gel Silica Glass on Esterase Activity, Conformational Stability,
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`and Unfolding of Bovine Carbonic Anhydrase II, 11 CHEMISTRY
`MATERIALS 3671–3679 (1999) (“Badjic”), Ex. 1009.1
`
`F. Instituted Grounds of Unpatentability
`Inter partes review was instituted based on the following five grounds
`of unpatentability asserted in the Petition:
`1. Claims 1–3, 15, 17, 24–27, 40, 41, and 43 under 35 U.S.C.
`§ 102(b) as anticipated by Bonaventura ’987;
`2. Claims 1–3, 15–17, 24–27, and 40–43 under 35 U.S.C.
`§ 103(a) as obvious over Bonaventura ’987 and Bonaventura ’416;
`3. Claims 1, 4, 25, and 28 under 35 U.S.C. § 103(a) as obvious
`over Bonaventura ’987 and Badjic;
`4. Claims 1, 18, and 19 under 35 U.S.C. § 103(a) as obvious
`over Bonaventura ’987 and Kohl; and
`5. Claims 1, 2, 15, 16, 22–26, and 40–43 under 35 U.S.C.
`§ 103(a) as obvious over Dean and Rau.
`
`II. DISCUSSION
`A. 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); Cuozzo Speed Techs.,
`LLC v. Lee, 136 S. Ct. 2131, 2144–46 (2016). Claim terms are presumed to
`have their ordinary and customary meaning, as understood by one of
`
`
`1 With the exception of Exhibit 1002 (the ’458 prosecution history), we cite
`to the Exhibits using the original page numbers, not those added by
`Petitioner or Patent Owner.
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`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).
`“[C]laim terms need only be construed ‘to the extent necessary to
`resolve the controversy.’” Wellman, Inc. v. Eastman Chem. Co., 642 F.3d
`1355, 1361 (Fed. Cir. 2011)) (quoting Vivid Techs., Inc. v. Am. Sci. & Eng’g,
`Inc., 200 F.3d 795, 803 (Fed. Cir. 1999)).
`The parties dispute the meaning of “entrapped in” (claims 1 and 25),
`as well as “in suspension” (claim 1) and “suspending” (claim 25). Pet. 10–
`12; PO Resp. 7–13.
`
`entrapped in
`In the Decision to Institute, we provided a preliminary construction
`for the phrase “entrapped in the porous substrates” based on the record
`existing at that time. Dec. 8–12. Based on the current record, we provide
`the following analysis and construction of this term.
`Petitioner argues that “entrapped in” the porous substrates should be
`construed to mean that “the enzyme is physically trapped within the
`structure of the substrate while retaining at least some of its activity.”
`Pet. 11.
`Patent Owner does not dispute that “entrapped” requires that enzymes
`be physically trapped within the structure of the substrate, as set forth in
`Petitioner’s proposed construction. The experts agree that “entrapped”
`refers to retention by physical means, as opposed to a chemical bond or link.
`Ex. 2004 (Fradette Decl.) ¶¶ 58 (enzyme immobilization techniques are
`generally classified as physical or chemical), 86(b) (skilled person would not
`understand entrapment to include chemical bonding or linking); Ex. 2017
`(DeFilippi Dep.) 39:12–40:8, 42:3–21. We determine that the experts’
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`agreement is not inconsistent with the intrinsic evidence. Compare Ex. 2004
`¶ 86(b) and Ex. 2017 40:2–8, with Ex. 1005, 5:40–43 (“oxygen carriers . . .
`[may be] entrapped and/or covalently linked to a polyurethane matrix or to
`comparable supports”). We therefore revise our preliminary construction to
`include a requirement that the enzyme is physically trapped within the
`structure of the substrate. Cf. Dec. 10.
`Patent Owner also does not dispute that an “entrapped” enzyme
`retains at least some of its activity, as stated in Petitioner’s proposed
`construction. Retention of activity is consistent with the claims and the
`Specification, both of which recite that the function of the entrapped
`carbonic anhydrase is to catalyze and promote 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), 3:35–37 (summary of the
`invention). Accordingly, we adopt this undisputed aspect of Petitioner’s
`proposed construction.
`The parties’ dispute focuses on whether the term “entrapped in”
`encompasses “encapsulation,” which is disclosed in one of Petitioner’s
`asserted references (Dean). Petitioner contends “entrapped” includes
`encapsulation, Pet. 14, while Patent Owner argues that “entrapped”
`excludes encapsulation, PO Resp. 10–12. To distinguish encapsulation,
`Patent Owner proposes that “entrapped in” be construed to require that “the
`enzyme molecules are free in solution, but restricted in movement within the
`interstitial confines of the porous substrate lattice network.” PO Resp. 13.
`For the reasons discussed below, we determine that “entrapped,” as
`used in the ’458 patent, does not exclude encapsulation and does not require
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`“interstitial confines” or a “lattice network,” as set forth in Patent Owner’s
`proposed construction.
`Our analysis begins with the claim language, which recites: “the
`carbonic anhydrase are entrapped in the porous substrates.” Ex. 1001,
`10:21–22 (claim 1), 11:41–42 (claim 25). The claims do not describe the
`porous substrates as having “interstitial confines” or a “lattice network,” as
`set forth in Patent Owner’s proposed construction.
`Patent Owner agrees that the dictionary definition of “entrap” does not
`exclude encapsulation. The definition of “entrap” cited by both sides is: “to
`capture and hold (a substance).” Ex. 2012,2 758; see also PO Resp. 11
`(citing Ex. 2012, 758); Ex. 2004 (Fradette Decl.) ¶ 62 (quoting Ex. 2012,
`758); Pet. Reply 5 (same). At the oral hearing, Patent Owner agreed that if
`you encapsulate an enzyme, you “capture and hold it inside the shell.”
`Tr. 39:4–14.
`Turning next to the Specification, the term “entrapped” appears in the
`following three passages of the ’458 patent (with bold added for emphasis):
`Most preferably, the biocatalysts are entrapped in porous
`substrates pervading the reaction chamber. Alternatively, the
`biocatalysts may be carried by the liquid that feeds the reaction
`chamber.
`Ex. 1001, 4:6–9.
`Biocatalysts . . . may be selected from a wide variety of
`biological materials including enzymes, liposomes,
`microorganisms, animal cells and/or plant cells and the like.
`Fractions, complexes or combinations thereof may also be used
`simultaneously. . . . For the purpose of the invention, the
`
`
`2 WEBSTER’S THIRD NEW INTERNATIONAL DICTIONARY (3rd ed. 1986),
`Ex. 2012.
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`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.
`Id. at 6:13–31.
`The enzyme carbonic anhydrase, which is of relatively
`low molecular weight (30,000 daltons), may be made to form
`part of a complex in order to increase its size. This, in turn,
`allows the use of membranes with greater porosity and
`enhances liquid flow rates. Different types of enzyme
`complexes may be formed. Among these are those using whole
`cells such as red blood cells. 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. Packing made of
`polymers such as nylon, polystyrene, polyurethane, polymethyl
`methacrylate, functionalized silica gel, etc. may be used.
`Enzymes may also be entrapped in insoluble gel particles such
`as silica, alginate, alginate/chitosane or
`alginate/carboxymethylcellulose, etc. or covalently linked or
`non covalently linked in a network of albumin, PEG or other
`molecule. Such a network constitutes a loose type network. It
`may appear as a cloudy suspension, “filaments” of which are
`often visible to the naked eye. For the purpose of the invention,
`alginate particles should preferably possess a diameter
`comprised in a range from 1 to 9 mm, and preferably, a
`diameter inferior to 3 mm.
`Id. at 8:51–9:4.
`These Specification passages do not explicitly define “entrapped” and
`do not explain how biocatalysts (enzymes) are entrapped in the porous
`substrates. The Specification does not describe the porous substrates as
`having “interstitial confines” or a “lattice network,” as set forth in Patent
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`Owner’s proposed construction. Nor does the Specification require that the
`“porous substrates” be insoluble gel particles, as opposed, for example, to a
`semipermeable membrane or capsule.
`Patent Owner relies upon the above-quoted passages from columns 6
`and 8 to argue that entrapment is different from encapsulation. PO Resp.
`10–11; Ex. 2004 ¶¶ 79, 80 (quoting Ex. 1001, 6:23–31 and 8:51–9:4). We
`are not persuaded by Patent Owner’s argument.
`As support for its position, Patent Owner relies on Dr. Fradette’s
`testimony, which inserts bracketed numbers in the above-quoted passages
`from columns 6 and 8 to designate what he avers are “distinct ways to retain
`the enzyme.” Ex. 2004 (Fradette Decl.) ¶¶ 79, 80. The Specification as
`written, however, does not include numerical designations inserted by
`Dr. Fradette and does not define “entrapped” as excluding encapsulation.
`See In re Paulsen, 30 F.3d 1475, 1480 (Fed. Cir. 1994) (“Although an
`inventor is indeed free to define the specific terms used to describe his or her
`invention, this must be done with reasonable clarity, deliberateness, and
`precision.”)
`The above-quoted passage from column 6 does not mention
`encapsulation and is therefore not persuasive to show that encapsulation and
`entrapment are distinct forms of enzyme immobilization. The above-quoted
`passage from column 8 discloses that a problem associated with enzyme
`complexation using red blood cells may be overcome by “[e]ncapsulation
`techniques.” Ex. 1001, 8:55–59. The passage then discusses various
`materials that may be used as alternatives to red blood cells. Id. at 8:59–66.
`As part of this discussion, the passage states: “[e]nzymes may also be
`entrapped in insoluble gel particles . . . .” Id. at 8:62–63. When read as a
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`whole, the above-quoted passage from column 8 does not suggest with
`“reasonable clarity, deliberateness, and precision” that entrapment and
`encapsulation are mutually exclusive. In re Paulsen, 30 F.3d at 1480.
`Instead, the passage may reasonably be interpreted as suggesting that
`encapsulation is a form of entrapment. Ex. 1001, 8:62–63 (“Enzymes may
`also be entrapped . . . .”). Our interpretation is consistent with the
`Summary of the Invention, which uses the term “entrapped” broadly to
`distinguish entrapped enzymes from enzymes that are free in solution, i.e.,
`not immobilized. Id. at 4:6–9.
`Bonaventura ’416 and Bonaventura ’987 were both cited during
`prosecution of the ’458 patent. Ex. 1001, page 2 (listing cited references).
`Bonaventura ’987 is cited in the Specification of the ’458 patent, id. at 2:44,
`2:53, and a divisional having the same disclosure as Bonaventura ’987 —
`U.S. Patent No. 4,761,209—was relied upon to reject the claims during
`prosecution of the ’458 patent. Ex. 1002, 51, 83. We, therefore, consider
`Bonaventura ’416 and Bonaventura ’987 intrinsic evidence for purposes of
`claim construction. V-Formation v. Benetton Group & Rollerblade, Inc.,
`401 F.3d 1307, 1311 (Fed. Cir. 2005) (“prior art cited in a patent or cited in
`the prosecution history of the patent constitutes intrinsic evidence” (quoting
`Kumar v. Ovonic Battery Co., 351 F.3d 1364, 1368 (Fed. Cir. 2003)).
`Both sides rely on the following discussion of “entrapped” in
`Bonaventura ’416:
`This invention relates to the incorporation of an oxygen
`carrier, which can be a biological macromolecule, into an
`insolubilized form, which can be a polymeric matrix. More
`particularly, the preferred embodiment of the invention involves
`a biochemical engineering technique known as molecular
`entrapment. The oxygen carrier used by man and other
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`mammals, as well as by most other vertebrates, is hemoglobin.
`By molecular entrapment, hemoglobin can be made insoluble
`and consequently more amenable for use in a recycling and
`regenerable system. 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 entrapment insolubilizes the material and
`renders it amenable to manipulation. The degree to which
`function is maintained varies greatly with the type of
`entrapment process used. In the preferred polyurethane
`matrices of this invention, the material retains essentially full
`biological activity.
`Ex. 1005, 6:28–46 (emphasis added). According to Petitioner, “placing a
`cage around the [enzyme],” id. at 6:39–40, includes the use of “a synthetic
`or natural polymeric network or membrane” and does not exclude micro-
`encapsulation. Pet. 14; Ex. 1003 ¶ 20. Patent Owner, on the other hand,
`relies on the same language to argue that “entrapment” is different from
`“encapsulation, in which the enzyme is enveloped in a semipermeable
`membrane.” PO Resp. 12–13, 39; see also Ex. 1027 (Fradette Dep.) 71:17–
`73:7 (differentiating “entrapment” within a cage from “encapsulation”
`within a membrane).
`Even if we interpret the term “cage” as referring to a network rather
`than a membrane, however, that distinction does not support Patent Owner’s
`proposed construction. The claims recite that carbonic anhydrase is
`entrapped in porous substrates, not in a cage. Ex. 1001, 10:21–22 (claim 1);
`11:40–42 (claim 25). Furthermore, the discussion of a “cage” begins with
`the term “optimally” indicating that the analogy is exemplary rather than
`definitional. Ex. 1005, 6:38–41. There is also discussion of variation that
`depends on “the type of entrapment process used.” Id. at 6:43–44.
`Accordingly, the cited passage from Bonaventura ’416 does not persuade us
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`that that “entrapment” is limited to retention within the “interstitial confines”
`of a “lattice network,” as argued by Patent Owner.
`Patent Owner argues that Bonaventura ’987 uses the terms
`“entrapped” and “encapsulation” separately in referring to enzyme
`immobilization techniques. PO Resp. 11 (citing Ex. 1004, 4:46–5:35). The
`cited portion of Bonaventura ’987 discusses “[v]arious techniques for the
`insolubilization (or immobilization) of biological materials,” Ex. 1004,
`4:46–47, one of which involves “encapsulation,” id. at 4:62, and another of
`which is the method of Bonaventura ’416 involving entrapment, id. at 5:28–
`35. The cited disclosure does not, however, indicate that “entrapped,” as
`used in the claims of the ’458 patent, excludes encapsulation.
`Patent Owner directs us to the prosecution history, where the
`independent claims were amended to include the “entrapped” limitation
`from originally-filed dependent claims 8 and 41, which the Examiner
`indicated were allowable. Ex. 1002, 117, 121 (independent claims amended
`to recite “the substrates comprise porous substrates and the carbonic
`anhydrase are entrapped in the porous substrates”);3 Tr. 34:16–35:3 (Patent
`Owner’s argument regarding prosecution history). The identified portions of
`the prosecution history do not, however, indicate that “entrapped” is
`different from “encapsulation.”
`The parties cite various books and articles to support their respective
`positions regarding the meaning of “entrapped.” Both parties rely on
`
`
`3 See also id. at 125 (applicant remarks), 188 (Examiner’s indication of
`allowable subject matter), 289–90, 293–294 (originally filed claims).
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`Perry’s4 and Zaborsky.5 Patent Owner additionally relies on Bickerstaff,6
`and Petitioner additionally relies on Roig7 and Dumitriu.8 PO Resp. 11–12;
`Pet. Reply 6–7. These references show that “entrapped” (or another form of
`that word) is sometimes used in a broad sense to refer to a class of physical
`immobilization techniques that includes encapsulation and is sometimes
`used in a narrower sense to refer to entrapment within a gel or polymer,
`which does not include encapsulation. Roig and Dumitriu, for example,
`each provide a tree diagram showing “entrapped” or “entrapment” as a class
`of immobilization techniques that includes “micro encapsulated” or
`“microencapsulation,” as well as “polymer entrapped” or “gel entrapment.”
`Ex. 1024, 181; Ex. 1028, 631. Like Roig and Dumitriu, Perry’s uses the
`term “entrapment” first in a broad sense and then in a narrower sense. More
`specifically, Perry’s first identifies the methods of immobilization as
`“adsorption, covalent bonding, or entrapment” and then provides specific
`examples, including gel “entrapment” and “encapsulation.” Ex. 2006, 24-
`21. Zaborsky uses the word “entrapped” not only with respect to
`
`
`4 PERRY’S CHEMICAL ENGINEER’S HANDBOOK 23-52 to 23-55, 24-21, 24-22
`(Robert H. Perry & Don W. Green eds., 7th ed. 1997), Ex. 2006.
`5 O. Zaborsky, IMMOBILIZED ENZYMES 83–101 (1973), Ex. 2011.
`6 Gordon F. Bickerstaff, Methods in Biotechnology, in IMMOBILIZATION OF
`ENZYMES AND CELLS 1–11 (1997), Ex. 2002.
`7 M.G. Roig, et al., Methods for Immobilizing Enzymes, 14 BIOCHEMICAL
`EDUC. 180–185 (1986), Ex. 1024.
`8 S. Dumitriu & E. Chornet, Polysaccharides as Support for Enzyme and
`Cell Immobilization, in POLYSACCHARIDES: STRUCTURAL DIVERSITY AND
`FUNCTIONAL VERSATILITY 629–748 (Severian Dumitriu, ed., 1998), Ex.
`1028.
`
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`immobilization within the interstitial space of crosslinked polymers, but also
`with respect to immobilization within microcapsules. Ex. 2011, 83–91
`(Chapter 6: “Entrapment within Crosslinked Polymers”); id. at 93–95
`(Chapter 7: “Microencapsulation”). Figure 18, for example, shows a
`“microcapsule” with “entrapped enzyme molecules.” Id. at 93. In contrast
`to these references, Bickerstaff characterizes entrapment and encapsulation
`as separate methods of immobilization of enzymes. Ex. 2002, 2–9.
`As noted above, 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. Cf. Ex. 2002 (Bickerstaff) 9 (encapsulation is
`achieved by “enveloping the biological components within various forms of
`semipermeable membranes”). We, therefore, conclude that “entrapped,” as
`used in the ’458 patent, is properly construed consistent with the broader of
`the two meanings suggested by the extrinsic evidence.
`Accordingly, based on the arguments and evidence on this record and
`applying the broadest reasonable interpretation,9 we adopt Petitioner’s
`proposed construction for “entrapped”: “the enzyme is physically trapped
`within the structure of the substrate while retaining at least some of its
`activity.”
`
`
`9 Neither party contends that application of the claim construction standard
`of Phillips v. AWH Corp., 415 F.3d 1303 (Fed. Cir. 2005), would require a
`different construction for “entrapped.” Tr. 17:17–18:16 (Petitioner);
`Tr. 35:9–24 (Patent Owner).
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`in suspension/suspending
`Construction of the terms “in suspension” (claim 1) and “suspending”
`(claim 25) is discussed below in connection with our analysis of Petitioner’s
`Ground 1.
`
`B. Asserted Grounds of Unpatentability
`Ground 1: Anticipation by Bonaventura ’987
`Petitioner asserts that claims 1–3, 15, 17, 24–27, 40, 41, and 43 of the
`’458 patent are unpatentable under 35 U.S.C. § 102(b) as anticipated by
`Bonaventura ’987.
`
`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 shows 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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`Bonaventura ’987 discloses an apparatus for carrying out the carbon
`dioxide removal method in Figure 6, which is reproduced below:
`
`
`Figure 6 shows an apparatus for removing carbon dioxide from a fluid.
`Ex. 1004, 6:59–62. The apparatus includes: 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. Id. at 30:37–47. Bonaventura ’987 discusses ways of
`retaining immobilized enzyme 24 within compartment 23 as follows:
`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 [sic, 23], no further entrappment [sic] of the
`enzyme or 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
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`the flowable substrate, shown in FIG. 6 as screens 26a and 26b,
`are required.
`Id. at 30:20–30.
`Bonaventura ’987 discloses another embodiment of an enzyme reactor
`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 enzyme
`reactor 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. Gas from which carbon
`dioxide has been removed exits the reactor through outlet 28, and a carbonic
`acid solution exits through outlet 30. Id. at 30:66–31:11. Regarding
`retention of immobilized enzymes 24 within reactor container 21 in the
`Figure 7 embodiment, Bonaventura ’987 discloses:
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`[C]arbonic anhydrase is immobilized on a porous substrate
`(24). Substrate 24 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.
`
`Claims 1–3, 15, 17, 24–27, 40, 41, and 43
`Petitioner contends that claims 1–3, 15, 17, 24–27, 40, 41, and 43 are
`anticipated by the Figure 6 embodiment of Bonaventura ’987. Pet. 18–28;
`Ex. 1003 ¶¶ 77–91. Regarding the “in suspension” limitation of claim 1 and
`the “suspending” limitation of claim 25, Petitioner asserts that Bonaventura
`’987 “teaches using immobilized carbonic anhydrase in suspension” in the
`reactor of Figure 6. Pet. 19; see also Ex. 1003 (DeFilippi Decl.) ¶ 54
`(same). Petitioner cites Bonaventura ’987’s disclosure 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. 20 (quoting Ex. 1004,
`30:26–30); see also id. at 21–22 (chart for claim 1); id. at 26 (chart for claim
`25); see also Ex. 1003 ¶¶ 79 (p. 35—chart for claim 1), 85 (p. 44—chart for
`claim 25).
`Patent Owner argues that Bonaventura ’987 does not disclose the “in
`suspension