Ex Parte Mori

Patent Trial and Appeal Board

Feb 26, 2018

14235833 (P.T.A.B. Feb. 26, 2018)

United States Patent and Trademark Office
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O.Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
14/235,833 01/29/2014 Masaaki Mori Q209635 8502
23373 7590 02/28/2018
SUGHRUE MION, PLLC
2100 PENNSYLVANIA AVENUE, N.W.
SUITE 800
WASHINGTON, DC 20037
EXAMINER
RAO, MANJUNATH N
ART UNIT PAPER NUMBER
1656
NOTIFICATION DATE DELIVERY MODE
02/28/2018 ELECTRONIC
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the
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PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte MASAAKI MORI
Appeal 2017-002434
Application 14/235,8331
Technology Center 1600
Before DONALD E. ADAMS, FRANCISCO C. PRATS, and
DEVON ZASTROW NEWMAN, Administrative Patent Judges.
PRATS, Administrative Patent Judge.
DECISION ON APPEAL
This appeal under 35 U.S.C. § 134(a) involves claims to a
recombinant yeast capable of synthesizing alkane, and a method of using
that yeast to produce alkane. The Examiner rejected the claims for
obviousness.
We have jurisdiction under 35 U.S.C. § 6(b). We affirm.
1 Appellant states that the “real party in interest in this appeal is the
Assignee, TOYOTA JIDOSHA KABUSHIKI KAISHA.” Appeal Br. 2.
Appeal 2017-002434
Application 14/235,833
STATEMENT OF THE CASE
The following rejections are before us for review:
(1) Claims 1 and 9-11, under 35 U.S.C. § 103(a) as being obvious
over Reppas2 (Ans. 2—3); and
(2) Claims 1 and 9-11, under 35 U.S.C. § 103(a) as being obvious
over Schirmer3 (Ans. 3 4).
Claim 1 is representative and reads as follows:
Claim 1: A method for producing alkane, comprising
culturing recombinant yeast capable of synthesizing alkane, in
which an alkane synthase gene, a ferredoxin gene, and a
ferredoxin NADPH reductase gene have been introduced, in a
medium and then producing alkane in the medium.
Appeal Br. 13.
DISCUSSION
Because both of the Examiner’s rejections involve the same issues, we
consider them together.
As to Reppas, the Examiner found that the reference discloses
producing alkanes using a recombinant yeast into which certain alkane
synthase genes were introduced, as required by Appellant’s claim 1. Ans. 2—
3. The Examiner found that Reppas differs from claim 1 in not expressly
teaching that the recombinant yeast additionally possessed the ferredoxin
and ferredoxin reductase genes also required by claim 1. Id. at 3.
The Examiner concluded, however, that it would have been obvious to
introduce those additional genes into Reppas’s recombinant yeast in view of
Reppas’s teaching of a “requirement of the ferredoxin/ferredoxin reductase
2 US 2011/0117618 A1 (published May 19, 2011).
3 WO 2009/140695 A1 (published Nov. 19, 2009).
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Application 14/235,833
genes to regenerate the active form of the monooxygenase [alkane synthase]
and enable a yeast host cell transformed with alkane synthase, ferredoxin
and ferredoxin reductase.” Id.
As to Schirmer, the Examiner found that the reference discloses
producing alkanes using a recombinant yeast into which certain alkane
synthase genes were introduced, as required by Appellant’s claim 1. Ans. 3.
The Examiner found that Schirmer differs from claim 1 in not expressly
teaching that the recombinant yeast also possessed the ferredoxin and
ferredoxin reductase genes also required by claim 1. Id. at 4.
The Examiner concluded, however, that it would have been obvious to
introduce those additional genes into Schirmer’s recombinant yeast in view
of Schirmer’s teaching that its “decarbonylase [alkane synthase] requires
ferredoxin/ferredoxin NADPH reductase and NADPH for its activity. See,
in particular, paragraphs 332 and 333.” Id. at 3.
As stated in In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir. 1992):
[T]he examiner bears the initial burden ... of presenting a
prima facie case of unpatentability. . . .
After evidence or argument is submitted by the applicant
in response, patentability is determined on the totality of the
record, by a preponderance of evidence with due consideration
to persuasiveness of argument.
In the present appeal, Appellant does not persuade us that the
Examiner failed to show, by a preponderance of the evidence, that the
process recited in claim 1 would have been obvious over either Reppas or
Schirmer.
Contrary to Appellant’s contention that neither reference teaches or
suggests using a yeast cell as a host for the three genes required by claim 1
(Appeal Br. 6—7), both references state expressly that yeasts may be used as
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Application 14/235,833
the host cell in the disclosed alkane-producing processes. See, e.g., Reppas
1226 (Example 10, entitled “Production of Hydrocarbons in Yeast”); see
also Schirmer 132 (“In any of the aspects described herein, the host cell can
be selected from the group consisting of a mammalian cell, plant cell, insect
cell, yeast cell, fungus cell, filamentous fungi cell, and bacterial cell.”)
(emphasis added).
As the Examiner found, moreover, in addition to the alkane-producing
genes introduced into the host cells, both references teach that reduced
ferredoxin is a required cofactor for the alkane-producing enzymes. See
Reppas Fig. 1; id. at 1205 (disclosing in exemplified strain
“ferredoxin/ferredoxin-NADPH reductase system that can regenerate the di­
iron active site of ADM [alkane synthase], thereby preventing the
accumulation of hexadecanal and octadecanal that could in turn be non-
specifically dehydrogenated to the corresponding 1-alkanols”); see also
Schirmer 1334 ([I]n-vilro conversion of octadecanal to heptadecane was
observed in the presence of [recombinant host strain] Npun02004178. The
enzymatic decarbonylation of octadecanal by Npun02004178 was dependent
on the addition of spinach ferredoxin reducatase, ferredoxin and NA DP I IT)
(emphasis added).
Appellant does not persuade us therefore, that the Examiner erred in
concluding that it would have been prima facie obvious to include, in a yeast
host cell, not only the alkane synthase genes described the references, but
also a ferredoxin gene and a ferredoxin NADPH reductase gene, as required
by claim 1, and to use that recombinant yeast cell to producing alkane in a
medium, as claim 1 also requires.
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Application 14/235,833
As Appellant contends, nonetheless, it is well settled that “a patent
applicant [may] rebut a prima facie case of obviousness [by] mak[ing] a
showing of ‘unexpected results,’ i.e., to show that the claimed invention
exhibits some superior property or advantage that a person of ordinary skill
in the relevant art would have found surprising or unexpected.” In re
Geisler, 116 F.3d 1465, 1469 (Fed. Cir. 1997) (quoting In re Soni, 54 F.3d
746, 750 (Fed. Cir. 1995)).
Appellant does not persuade us, however (see Appeal Br. 8—12; Reply
Br. 4—7), that evidence of unexpected results, sufficient to outweigh the
evidence of prima facie obviousness as to Appellant’s claim 1, has been
advanced on this record.
We acknowledge, as shown in Appellant’s Figure 5, that recombinant
Saccharomyces cerevisiae cells including the ferredoxin and ferredoxin
NADPH reductase genes, along with an alkane synthase gene, have an
improved alkane yield, compared to S. cerevisiae cells having only the
alkane synthase gene. See Fig. 5 (showing relative alkane yield of 100% for
S. cerevisiae strain having only the alkane synthase gene (“YPH499 alkS”),
and relative alkane yield of 3 89% for S. cerevisiae strain having alkane
synthase gene, ferredoxin gene, and ferredoxin NADPH reductase genes
(“YPH 499 alkS YfdxYfdr”); see also Spec. 1 85 (YPH499 and
transformants are S. cerevisiae strains).
We acknowledge that, in contrast, as shown in Appellant’s Figure 10,
recombinant E. coli cells including the ferredoxin and ferredoxin NADPH
reductase genes, along with an alkane synthase gene, have a reduced alkane
yield, compared to E. coli cells having only the alkane synthase gene. See
Fig. 10 (showing relative alkane yield of 100% for E. coli strain having only
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Application 14/235,833
the alkane synthase gene (“BL21(DE3) alkS”), and relative alkane yield of
26% for E. coli strain having alkane synthase gene, ferredoxin gene, and
ferredoxin NADPH reductase genes (“BL21 (DE3) alkS EfdxEfdr”)); see
also Spec. Tflf 105, 109 (BL21 (DE3) and transformants are E. coli strains).
Appellant, in the Specification, does not characterize these results as
being unexpected, however. Rather, the Specification states only that “from
the results shown in Fig. 10, all transformants prepared by introducing the
alkS gene had the ability to synthesize alkane (Tridecane). However, as
shown in Fig. 10, further introduction of the ferredoxin gene and the
ferredoxin NADPH reductase gene did not result in improved ability to
synthesize alkane.” Spec. 1109. Appellant, moreover, does not direct us to
any non-attorney assertions that it would have been unexpected that the
ferredoxin/ferredoxin NADPH reductase gene combination would improve
alkane yield in S. cerevisiae, but not in E. coli.
Rather, Appellant’s briefs contain the sole assertions of record that it
would have been unexpected that the ferredoxin/ferredoxin NADPH
reductase gene combination would improve alkane yield in S. cerevisiae, but
not in E. coli. As explained in In re Geisler, however, such an “assertion of
what seems to follow from common experience is just attorney argument
and not the kind of factual evidence that is required to rebut a prima facie
case of obviousness.” 116 F.3d at 1470.
Thus, in the present appeal, similar to the situation in Geisler,
Appellant “did not offer evidence of unexpected results in the form of a
statement to that effect from the inventors or any third party, or any
objective evidence from a respected source—the kind of evidence that we
have previously required to rebut a prima facie case.” Id.
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It is well settled, moreover, that “any superior property must be
unexpected to be considered as evidence of non-obviousness.” Pfizer, Inc. v.
Apotex, Inc., 480 F.3d 1348, 1371 (Fed. Cir. 2007) (emphasis in original).
In the present case, as noted above, both Reppas and Schirmer
disclose that reduced ferredoxin, which would be generated by the
ferredoxin/ferredoxin NADPH reductase gene combination, is a critical
cofactor for the enzymes encoded by the alkane synthase genes used in both
references. We, therefore, discern no error in the Examiner’s finding that
“the result presented in Figure 5 of the instant application for the
transformed yeast cell is expected . . . .” Ans. 6.
Lastly, we also note that it is well settled that any showing of
unexpected results must be commensurate in scope with the claimed subject
matter. See In re Peterson, 315 F.3d 1325, 1330 (Fed. Cir. 2003)
(“[Ajpplicanf s showing of unexpected results must be commensurate in
scope with the claimed range.”).
As seen above, the evidence advanced by Appellant to show
unexpectedness is limited to experiments in S. cerevisiae. In contrast,
Appellant’s claim 1 encompasses the use of any yeast in the claimed
process. See Appeal Br. 13 (claim 1). Because Appellant does not identify
any specific evidence suggesting that the results shown in S. cerevisiae are
representative of the results that would occur in the full range of yeast
species encompassed by claim 1, we are not persuaded that Appellant’s
alleged evidence of unexpectedness is sufficiently commensurate in scope
with the claimed subject matter to outweigh the evidence of prima facie
obviousness advanced by the Examiner.
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In sum, for the reasons discussed, as to both rejections, Appellant does
not persuade us that the Examiner failed to advance sufficient evidence to
establish a prima facie case of obviousness as to claim 1. For the reasons
discussed, we are not persuaded that Appellant has advanced evidence of
unexpected results sufficient to outweigh the evidence of prima obviousness.
We, therefore, affirm both of the Examiner’s obviousness rejections of claim
1. Claims 9-11 fall with claim 1. 37 C.F.R. § 41.37(c)(l)(iv).
SUMMARY
For the reasons discussed, we affirm the Examiner’s rejection of
claims 1 and 9—11, under 35 U.S.C. § 103(a), for obviousness over Reppas.
For the reasons discussed, we affirm the Examiner’s rejection of
claims 1 and 9—11, under 35 U.S.C. § 103(a), for obviousness over
Schirmer.
TIME PERIOD
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a)(l)(iv).
AFFIRMED
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