Court Opinion

ID: 6343334
Source: CourtListenerOpinion
Date Created: 2022-05-24 14:00:41.205663+00
Date Added: 2024-06-11T08:41:54.050917
License: Public Domain

Case: 20-2334   Document: 67     Page: 1   Filed: 05/24/2022

        NOTE: This disposition is nonprecedential.

   United States Court of Appeals
       for the Federal Circuit
                 ______________________

     CORNELL RESEARCH FOUNDATION, INC.,
                  Appellant

                            v.

  KATHERINE K. VIDAL, UNDER SECRETARY OF
  COMMERCE FOR INTELLECTUAL PROPERTY
    AND DIRECTOR OF THE UNITED STATES
      PATENT AND TRADEMARK OFFICE,
                  Intervenor
            ______________________

 2020-2334, 2020-2335, 2020-2337, 2020-2338, 2020-2339,
                       2020-2340
                ______________________

     Appeals from the United States Patent and Trademark
 Office, Patent Trial and Appeal Board in Nos. IPR2019-
 00577, IPR2019-00578, IPR2019-00579, IPR2019-00580,
 IPR2019-00581, IPR2019-00582.
                  ______________________

                 Decided: May 24, 2022
                 ______________________

     JULIE S. GOLDEMBERG, Morgan, Lewis & Bockius LLP,
 Philadelphia, PA, argued for appellant. Also represented
 by ROBERT CHRISTIAN BERTIN, ROBERT JOHN SMYTH, Wash-
 ington, DC; AJIT VAIDYA, Kenealy Vaidya LLP, Washing-
 ton, DC.
Case: 20-2334    Document: 67      Page: 2    Filed: 05/24/2022

 2              CORNELL RESEARCH FOUNDATION, INC.     v. VIDAL

     MAUREEN DONOVAN QUELER, Office of the Solicitor,
 United States Patent and Trademark Office, Alexandria,
 VA, argued for intervenor. Also represented by MICHAEL
 S. FORMAN, THOMAS W. KRAUSE, AMY J. NELSON, FARHEENA
 YASMEEN RASHEED.
                 ______________________

     Before PROST, REYNA, and TARANTO, Circuit Judges.
 PROST, Circuit Judge.
     Cornell Research Foundation, Inc. (“Cornell”) appeals
 from six inter partes reviews (“IPR”), each regarding a dif-
 ferent Cornell patent, in which the Patent Trial and Appeal
 Board (“Board”) concluded that the challenged claims were
 unpatentable as anticipated or obvious. E.g., Associated
 British Foods PLC v. Cornell Rsch. Found., Inc.,
 No. IPR2019-00577, Paper 117 (P.T.A.B. July 23, 2020)
 (“Final Written Decision”). Because substantial evidence
 supports the Board’s determinations that the claims were
 obvious, we affirm.
                         BACKGROUND
                               I
     The patents at issue relate to phytases in livestock
 feed. Phytases are enzymes that help certain animals ab-
 sorb phosphate, an important nutrient. Skilled artisans
 can produce phytase enzymes by taking a phytase gene
 from one organism and incorporating it into a host; the host
 then replicates and expresses the phytase protein, which
 can then be added to the feed.
     U.S. Patent No. 8,993,300 (“the ’300 patent”), repre-
 sentative in this appeal, describes a heterologous method
 of producing phytase: it uses a phytase gene derived from
 Escherichia coli, a species of bacteria, and a fungal host.
 There are different strains of E. coli, and different strains
 express different phytases. Two are relevant here: E. coli
Case: 20-2334    Document: 67      Page: 3       Filed: 05/24/2022

 CORNELL RESEARCH FOUNDATION, INC.    v. VIDAL                 3

 appA phytase and E. coli B phytase. There are also a vari-
 ety of fungal species. As is relevant here, the fungal king-
 dom includes yeast, of which Saccharomyces cerevisiae and
 Pichia pastoris are species.
     Independent claim 1 and dependent claims 10–12 of
 the ’300 patent are representative for the purposes of this
 consolidated appeal. They recite:
    1. A method of producing a phytase in fungal cells,
    the method comprising:
    providing a polynucleotide encoding an Escherichia
    coli phytase;
    expressing the polynucleotide in the fungal cells;
    and
    isolating the expressed Escherichia coli phytase
    wherein the Escherichia coli phytase catalyzes the
    release of phosphate from phytate.
    10. The method of claim 1 wherein the Escherichia
    coli phytase has an optimum activity at a temper-
    ature range of 57 degrees C. to 65 degrees C.
    11. The method of claim 1 wherein the Escherichia
    coli phytase retains at least 40% of its activity after
    heating the phytase for 15 minutes at 80 degrees
    C.
    12. The method of claim 1 wherein the Escherichia
    coli phytase retains at least 60% of its activity after
    heating the phytase for 15 minutes at 60 degrees
    C.
 Dependent claims 10–12 add so-called “thermostability
 limitations” to the phytases produced by the heterologous
 method described in independent claim 1.
Case: 20-2334    Document: 67      Page: 4   Filed: 05/24/2022

 4              CORNELL RESEARCH FOUNDATION, INC.    v. VIDAL

                              II
     We recount only the relevant procedural history below.
 Associated British Foods PLC (“ABF”) filed six IPR peti-
 tions, each challenging a different Cornell patent. The
 Board instituted review for all six and found all challenged
 claims unpatentable.
      ABF asserted two varieties of prior-art combinations in
 its petitions—those involving Kretz 1 and those not involv-
 ing Kretz. The Kretz-based challenges apply only to
 the ’300 patent. But the parties agree that all six Board
 decisions “stand and fall” with the Board’s non-Kretz obvi-
 ousness analysis for the ’300 patent. Reply Br. 26–27. We
 accordingly focus our discussion on the Board’s Final Writ-
 ten Decision for the ’300 patent.
     Beginning with the non-Kretz grounds, ABF asserted
 that all challenged claims of the ’300 patent would have
 been obvious over two combinations: (1) Dassa, 2 Greiner, 3
 and Cheng 4 and (2) Dassa, Greiner, Romanos, 5 and
 Van Gorcom 6      (collectively,   “the    Dassa/Greiner

     1   U.S. Patent No. 5,876,997 (“Kretz”).
     2   Janie Dassa, Christian Marck, & Paul L. Boquet,
 The Complete Nucleotide Sequence of the Escherichia coli
 Gene appA Reveals Significant Homology Between pH 2.5
 Acid      Phosphatase      and     Glucose-1-Phosphatase,
 172 J. BACTERIOLOGY 5497 (1990) (“Dassa”).
     3   R. Greiner, U. Konietzny, & Kl.-D. Jany, Purifica-
 tion and Characterization of Two Phytases from Esche-
 richia coli, 303 ARCHIVES BIOCHEMISTRY & BIOPHYSICS 107
 (1993) (“Greiner”).
     4   U.S. Patent No. 5,985,605 (“Cheng”).
     5   Michael A. Romanos, Carol A. Scorer, & Jeffrey J.
 Clare, Foreign Gene Expression in Yeast: A Review, 8 YEAST
 423 (1992) (“Romanos”).
     6   U.S. Patent No. 5,436,156 (“Van Gorcom”).
Case: 20-2334     Document: 67      Page: 5       Filed: 05/24/2022

 CORNELL RESEARCH FOUNDATION, INC.     v. VIDAL                 5

 combinations”). ABF argued that the thermostability
 claims of the ’300 patent would have been obvious for two
 independent reasons: (1) they were inherent properties of
 the Dassa/Greiner combinations, and (2) they were dis-
 closed by Olsen. 7 In its Final Written Decision, the Board
 concluded that there was a motivation to combine and rea-
 sonable expectation of success for the Dassa/Greiner com-
 binations and that the thermostability dependent claims of
 the ’300 patent were obvious due to inherency. See Final
 Written Decision, at 127–31, 141, 172–73.
      For the Kretz-based invalidity arguments, ABF as-
 serted that Kretz (1) anticipated certain challenged claims
 of the ’300 patent as § 102(e) prior art 8 and (2) rendered all
 challenged claims obvious in combination with other refer-
 ences. See id. at 10–11. The Board determined that Cor-
 nell failed to antedate Kretz, id. at 34, and that Kretz
 anticipated certain claims and rendered obvious the rest in
 light of those other references, see id. at 172–73.
      Cornell appeals from all six final written decisions in
 this consolidated appeal. The Patent and Trademark Of-
 fice Director intervened to defend the Board’s decisions af-
 ter ABF filed a notice of non-participation. We have
 jurisdiction under 28 U.S.C. § 1295(a)(4)(A).
                          DISCUSSION
     Cornell asserts primarily that three Board conclusions
 lack substantial evidence: (1) that there was a motivation
 to combine and reasonable expectation of success for the
 Dassa/Greiner combinations; (2) that the thermostability
 properties of the phytases produced by the claimed heter-
 ologous method are inherent; and (3) that Cornell failed to

     7   Ole Olsen & Karl Kristian Thomsen, Improvement
 of Bacterial β-Glucanase Thermostability by Glycosylation,
 137 J. GEN. MICROBIOLOGY 579 (1991) (“Olsen”).
     8   35 U.S.C. § 102(e) (2010).
Case: 20-2334    Document: 67      Page: 6    Filed: 05/24/2022

 6              CORNELL RESEARCH FOUNDATION, INC.     v. VIDAL

 antedate Kretz. We affirm the Board on the first two issues
 and accordingly do not reach the third.
                               I
     Putting aside the thermostability limitations of the
 ’300 patent’s dependent claims (discussed below), Cornell
 does not dispute that the Dassa/Greiner combinations dis-
 close all limitations of the relevant claims. Cornell dis-
 putes only the Board’s findings of motivation to combine
 and reasonable expectation of success for an E. coli phytase
 with a fungal host. Those are both fact questions that we
 review for substantial evidence, which is “such relevant ev-
 idence as a reasonable mind might accept as adequate to
 support a conclusion.” In re Mouttet, 686 F.3d 1322, 1331
 (Fed. Cir. 2012); PAR Pharm., Inc. v. TWI Pharms., Inc.,
 773 F.3d 1186, 1196 (Fed. Cir. 2014).
     In finding a motivation to combine, the Board credited
 ABF’s expert testimony that P. pastoris yeast was known
 to “produce high yields of heterologous protein [e.g., bacte-
 rial protein] and, thus, reduce industrial costs—an im-
 portant factor in producing phytases for livestock feed” on
 an industrial level. Final Written Decision, at 128. The
 Board found this to be “persuasive evidence setting forth
 reasons why [a] skilled artisan would have been motivated
 to express an E. coli appA [enzyme] in a fungal cell.” Id.
 This constitutes substantial evidence for a motivation to
 combine. KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 420
 (2007) (“[A]ny need or problem known in the field of en-
 deavor at the time of invention and addressed by the patent
 can provide a reason for combining the elements in the
 manner claimed.”).
     Cornell’s two main arguments to the contrary are un-
 persuasive. First, Cornell asserts that the Board’s motiva-
 tion-to-combine conclusion is contrary to ABF’s expert
Case: 20-2334    Document: 67      Page: 7       Filed: 05/24/2022

 CORNELL RESEARCH FOUNDATION, INC.    v. VIDAL                 7

 testimony that the Wodzinski reference 9 taught away from
 using a bacterial phytase in animal feed. We note that
 Wodzinski is not a part of the Dassa/Greiner combinations;
 additionally, the Board did not make any determination as
 to whether Wodzinski does or does not teach away. Final
 Written Decision, at 84. And even if the Board concluded
 that Wodzinski’s suggestions about bacterial phytases in
 animal feed, generally, were outweighed by the rest of the
 record evidence about producing E. coli appA phytase via a
 fungal host for use in animal feed, specifically, we would
 see no error. See In re Young, 927 F.2d 588, 591 (Fed. Cir.
 1991).
     Second, Cornell contends that the art suggested that
 pairing a bacterial phytase with a bacterial host was more
 advantageous than pairing such a phytase with a fungal
 host. Even if that’s true, as the Board correctly noted, “the
 law ‘does not require that the motivation be the best option,
 only that it be a suitable option.’” Final Written Decision,
 at 81–82 (emphasis omitted in original) (quoting PAR
 Pharm., 773 F.3d at 1197–98).
     Cornell’s challenge to the substantial evidence of the
 Board’s reasonable-expectation-of-success finding is simi-
 larly flawed. Cornell asserts a skilled artisan would have
 “had no reason to expect ‘that expressing the E. coli
 phytase in a fungal host would have produced an active en-
 zyme’” due to increased glycosylation, as its expert testi-
 fied. Appellant’s Br. 33 (quoting J.A. 4084–89). Cornell’s
 expert provided two examples of unsuccessful heterologous
 systems “where one of ordinary skill . . . may have at-
 tributed the lack of enzyme activity to glycosylation.” Fi-
 nal Written Decision, at 90. But the Board was free to
 weigh ABF’s expert testimony more heavily, and that’s
 what it did. The Board credited ABF’s expert testimony
 providing “nine or ten” contrary examples of systems that

     9   See J.A. 22462–63; see also J.A. 15187–89.
Case: 20-2334     Document: 67      Page: 8   Filed: 05/24/2022

 8               CORNELL RESEARCH FOUNDATION, INC.     v. VIDAL

 produced active bacterial enzymes in yeast hosts. Id.
 at 90–91. In addition, the Board pointed to Cornell’s expert
 testimony that, “in the majority of cases[,] glycosylation did
 not have an effect on the activity of the enzyme.” Id.
 at 91–92.
     We accordingly affirm the Board’s determination that
 there was a motivation to combine and reasonable expecta-
 tion of success for the Dassa/Greiner combinations. 10
                               II
     Cornell also challenges the Board’s finding that the
 thermostability limitations in the ’300 patent’s dependent
 claims are inherent results of the Dassa/Greiner combina-
 tions. Whether prior art inherently discloses a claim limi-
 tation is a question of fact that we review for substantial
 evidence. PAR Pharm., 773 F.3d at 1194.
     The Board found the thermostability limitations inher-
 ent to a heterologous system expressing the Dassa/Greiner
 E. coli appA phytase in a fungal host disclosed by Cheng,
 Romanos, or Van Gorcom, including P. pastoris and S. cere-
 visiae. The Board cited Cornell’s expert testimony, ABF’s
 expert testimony, the ’300 patent, and prosecution history
 as support. Final Written Decision, at 78–79. Indeed, the
 Board credited Cornell’s expert, who confirmed that “ex-
 press[ing] the same enzyme in the same host under the
 same conditions” produces “inherent results,” like thermo-
 stability characteristics. J.A. 7694–95 (emphasis added);
 Final Written Decision, at 78 (citing J.A. 7695). This con-
 stitutes substantial evidence supporting the Board’s deter-
 mination.

     10  We are not persuaded by Cornell’s contention that
 the Board’s analysis of the non-Kretz combinations is in-
 fected by analysis of Kretz.
Case: 20-2334     Document: 67     Page: 9       Filed: 05/24/2022

 CORNELL RESEARCH FOUNDATION, INC.    v. VIDAL                 9

      Cornell’s two arguments to the contrary are not per-
 suasive. First, Cornell faults the Board for citing no data
 outside of the ’300 patent to support its inherency finding.
 But the Board permissibly cited the ’300 patent’s disclo-
 sure that an E. coli appA phytase expressed in a P. pastoris
 host has optimum activity at 60 degrees Celsius as well as
 the patent’s teaching that an E. coli appA phytase ex-
 pressed in a S. cerevisiae host retained 69 percent of its ac-
 tivity after heating it for 15 minutes at 80 degrees Celsius.
 Final Written Decision, at 78–79; see Hospira, Inc. v. Frese-
 nius Kabi USA, LLC, 946 F.3d 1322, 1329–30 (Fed. Cir.
 2020). That data is consistent with the thermostability
 limitations of claims 10–12. Although it may be possible
 that the conditions of the Dassa/Greiner combinations
 were not the same as those described in the ’300 patent,
 Cornell did not make that argument and offered no evi-
 dence to that effect. Oral Arg. at 26:27–27:10, No. 20-2334,
 https://oralarguments.cafc.uscourts.gov/default.aspx?fl=20
 -2334_05032022.mp3.
      Second, Cornell asserts that the Board’s inherency
 finding for the Dassa/Greiner combinations is at odds with
 its finding of no inherency with respect to Kretz as antici-
 patory art. Cornell argues that this is especially concern-
 ing because the standard for inherency under § 103 is
 higher than that under § 102. In this case, we find no error.
 The Board explained that it did not find the thermostabil-
 ity limitations inherent under Kretz because ABF was re-
 lying on Kretz’s teachings using the E. coli B phytase
 whereas the thermostability data from the ’300 patent re-
 sulted from using the E. coli appA phytase. Final Written
 Decision, at 58. This is consistent with the Board’s reliance
 on Cornell’s expert testimony that the same enzyme is
 needed for the thermostability characteristics of an enzyme
 produced by a particular enzyme-host combination to be in-
 herent.
    We thus also affirm the Board’s inherency finding as
 supported by substantial evidence. Since that resolves this
Case: 20-2334    Document: 67     Page: 10    Filed: 05/24/2022

 10             CORNELL RESEARCH FOUNDATION, INC.     v. VIDAL

 appeal as to all patents and all claims, we do not reach Cor-
 nell’s other arguments, including those about antedating
 Kretz.
                        CONCLUSION
      We have considered the parties’ remaining arguments
 but find them unpersuasive. For the foregoing reasons, we
 affirm the Board’s obviousness conclusions.
                        AFFIRMED
                            COSTS
 Costs to Intervenor.