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NOTE: This disposition is nonprecedential.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.
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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”).
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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).
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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
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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.
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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
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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.
