Ex Parte Omura et al

Patent Trial and Appeal Board

Jul 26, 2017

12851668 (P.T.A.B. Jul. 26, 2017)

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.
12/851,668 08/06/2010 Hironori Omura 11769.0002-02000 2178
22852 7590 07/28/2017
FINNEGAN, HENDERSON, FARABOW, GARRETT & DUNNER
LLP
901 NEW YORK AVENUE, NW
WASHINGTON, DC 20001-4413
EXAMINER
LIU, SAMUEL W
ART UNIT PAPER NUMBER
1656
NOTIFICATION DATE DELIVERY MODE
07/28/2017 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
following e-mail address(es):
regional-desk @ finnegan. com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte HIRONORI OMURA, HIROKAZU SANADA, TAKAKO YADA,
TETSUNARI MORITA, MIKA KUYAMA, TOKUJI IKED A,
KENJI KANO, and SEIYA TSUJIMURA
Appeal 2015-002637
Application 12/851,66s1
Technology Center 1600
Before RACHEL H. TOWNSEND, DEVON ZASTROW NEWMAN, and
DAVID COTTA, Administrative Patent Judges.
COTTA, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to a
biosensor for measuring glucose. The Examiner rejected the claims on
appeal under 35 U.S.C. § 103(a) as obvious.
We affirm.
1 According to Appellants, the real party in interest is Ikeda Food Research
Co. Ltd. App. Br. iii.
Appeal 2015-002637
Application 12/851,668
STATEMENT OF THE CASE
The Specification teaches that the presence of glucose in blood is “an
important marker for diabetes.” Spec. 1. The Specification further teaches
that “a method for measuring a blood sugar and a means for controlling the
blood sugar level are desired which can be utilized not only in a hospital but
also at home and which is convenient.” Id. at 2. In response to this need,
“an objective of the invention is to provide a novel glucose dehydrogenase
which exhibits an excellent substrate-recognizing ability toward glucose and
which has low activity on maltose, and also to provide a method for
producing the same and a microorganism having an ability of producing the
same.” Id. at 4. “Another objective of the invention is to provide excellent
glucose measuring method, measuring reagent and biosensor which employ
the novel glucose dehydrogenase and which are capable of quantifying
glucose rapidly and conveniently at a high accuracy, as well as a glucose-
eliminating reagent.” Id.
The Specification explains that “[t]he inventors . . . made an effort in
characterizing various microorganisms producing the coenzyme-binding
glucose dehydrogenase, and finally discovered a coenzyme-binding glucose
dehydrogenase-producing microorganism and a coenzyme-binding glucose
dehydrogenase.” Id. at 4—5. “The coenzyme-binding glucose
dehydrogenase has a physicochemical ability of catalyzing a reaction for
oxidizing glucose, especially a hydroxyl group in the lst-position of glucose,
in the presence of an electron acceptor.” Id. “The invention provides a
biosensor employing the novel soluble coenzyme-binding glucose
dehydrogenase and a biosensor capable of quantifying and/or qualifying a
particular component in a sample.” Id. at 7.
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Application 12/851,668
Claims 22—33 are on appeal. Claim 22, the only independent claim, is
illustrative and reads as follows:
22. A biosensor for measuring glucose, comprising:
an electrode system comprising an action electrode and a
counter electrode; and
an enzymatic reaction layer in contact with the action
electrode and/or the counter electrode, the enzymatic reaction
layer comprising an electron acceptor and a soluble flavin
compound-binding glucose dehydrogenase, which has
enzymatic activity to glucose comprising catalyzing a reaction
for oxidizing glucose in the presence of the electron acceptor,
wherein enzymatic activity to maltose in the enzymatic
reaction layer is 5% or less relative to the enzymatic activity to
glucose;
wherein the biosensor can quantify glucose
concentrations ranging from 4.5 mM to 30 mM.
App. Br. 27.
The claims stand rejected as follows:
Claims 22, 25—28, and 31—33 were rejected under 35 U.S.C. § 103(a)
as obvious over the combination of Senior,2 Yugawa A,3 Yugawa B,4 and
Georgieff5 (“The First Rejection”).
2 Senior et al., EP 0 094 161, published Nov. 16, 1983 (“Senior”).
3 Yugawa et al., US Patent No. 6,656,702 Bl, issued Dec. 2, 2003 (“Yugawa
A”).
4 Yugawa et al., US Patent No. 6,059,946, issued May 9, 2000 (“Yugawa
B”).
5 Georgieff et al., US Patent No. 4,767,785, issued Aug. 30, 1988
(“Georgieff’).
3
Appeal 2015-002637
Application 12/851,668
Claims 23, 24, 29, and 30 were rejected under 35 U.S.C. § 103(a) as
obvious over the combination of Senior, Yugawa A, Yugawa B, Georgieff,
and Matsumoto6 (“the Second Rejection”).
Claims 22—27 and 29-33 were rejected on the ground of non-statutory
obviousness-type double patenting over claims 1, 6, 21, and 24 of US Patent
Application No. 12/396,724 (“the ‘724 Application”). However, the ‘724
Application has been abandoned, rendering this rejection moot. See, Aug. 4,
2016 Notice of Abandonment.
FINDINGS OF FACT
1. Yugawa A discloses:
A biosensor that enables rapid and simple quantitation of a
substrate with high accuracy and demonstrates an excellent
preservation characteristic by best retaining enzyme activity is
disclosed. The biosensor comprises an electrically insulating
base plate, an electrode system including at least a working
electrode and a counter electrode formed on the base plate, and a
reaction layer containing at least an enzyme and a sugar. The
reaction layer may be formed on the electrode system. The
enzyme may be selected from glucose oxidase, glucose
dehydrogenase, and fructose dehydrogenase.
Yugawa A Abstract.
2. Yugawa A discloses that an “object of the present invention is
to provide a biosensor with high stability against preservation.” Id. at col. 1,
11. 63-65.
3. Yugawa A discloses that “the present invention provides a
compact disposable biosensor of low cost.” Id. at col. 2,11. 1—2.
6 Matsumoto et al., Development of a Micro-Planar Ag/AgCl Quasi-
Reference Electrode with Long-Term Stability for an Amperometric Glucose
Sensor, 462 Analytica Chimica Acta 253-259 (2002).
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Application 12/851,668
4. Yugawa B discloses “a stable and cost-effective biosensor”
comprising “an electrode system that includes at least a working electrode
and counter electrode formed on the base plate, a reaction layer containing at
least an enzyme, an electron acceptor that is formed on, or in the vicinity of,
the electrode system, and a divalent water-soluble metallic salt provided in,
or in the vicinity of, the reaction layer.” Yugawa B Abstract.
5. Yugawa B discloses “The object of the present invention is to
provide a cost-effective biosensor with high stability after preservation by
causing the enzyme carried on the sensor to exert its maximal activity
thereby reducing the amount of enzyme carried per sensor.” Id. at col. 1,1.
66-col. 2,1.3.
6. Senior discloses: “A method for determining glucose present in
a fluid wherein a sample of a glucose-containing fluid is contacted with an
assay mixture comprising . . . flavin-dependent glucose dehydrogenase
enzyme E.C. (Enzyme Commission) No. 1.1.99.10 [derived from a strain of
Aspergillus! and a reducible compound, reduction of which can produce
changes in electro-magnetic radiation absorbance characteristics and/or
electrical changes, in an appropriate buffered medium.” Senior p. 10, claim
7.
7. Senior discloses:
The constant for glucose dehydrogenase E.C. 1.1.99.17 from
Acinetobacter is approximately 2 mM. The constant for E.C.
1.1.99.10 from Aspergillus oryzae is approximately 20 mM.
The consequence of this is that the useful range in which the
reaction rate is linearly proportional to substrate concentration
differs by a factor of 10 for these two enzymes. Thus when the
concentrations to be determined are small it is preferred to use
the enzyme having the lower Km, in this instance E.C.
1.1.99.17. Conversely when, as is often the case with serum
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Appeal 2015-002637
Application 12/851,668
samples, the concentrations to be determined may be relatively
high it is preferred to use the enzyme having the higher Km, i.e.
in this instance E.C.1.1.99.10.
Id. at p. 6—7.
8. The Specification discloses: “An inventive coenzyme-binding
glucose dehydrogenase may for example be an enzyme classified as EC 1.1.
99, preferably EC 1.1. 99.10, EC 1.1.99.13 or EC 1.1.99.17, and is a
coenzyme-binding enzyme, preferably a soluble coenzyme-binding
enzyme.” Spec. 3.
9. Table 1 of the Specification reads as follows:
Substrate
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Id. at 45 (emphasis added).
10. The Examiner finds, and Appellants do not dispute, that Table 1
reports the enzyme activity of GDH classified as EC 1.1.99.10. Final Act.
4.7
11. The Examiner finds, and Appellants do not dispute that “[t]wo
enzymes having [the] identical EC number necessarily possess identical
enzymatic activity including ‘substrate specificity/” Ans. 13. The
Examiner explains that “enzymatic activities are classified by the IUBMB
7 Office Action mailed July 2, 2013 (“Final Act.”).
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Appeal 2015-002637
Application 12/851,668
using Enzyme Commission (EC) number (i.e., EC number) which are
specific numerical identifiers with total four numbers wherein the last
numeral is a serial number for substrate specificity.” Id. (citing Kotera et al.,
126 J. Am. Chem. Soc. 16487-16298 (2004)).
12. The Specification discloses: “By using this culture method, the
coenzyme-binding glucose dehydrogenase can be produced by the
microorganism and accumulated also internal fungus body. Subsequently,
the coenzyme-binding glucose dehydrogenase can be recovered from the
culture by means of an ordinary protein purification method.” Id. at 32.
THE FIRST REJECTION
Appellants argue claims 22, 25—28, and 31—33 together. We
designate claim 22 as representative. 37 C.F.R. § 41.37(c)(l)(iv).
The Examiner finds that Senior discloses “an electrode sensor system
(wherein the sensor is equivalent to instant ‘biosensor’) to measure glucose
concentration; the system (or “glucose biosensor”) comprising glucose
dehydrogenase (GDH); wherein GDH is preferably obtained from
Aspergillus oryzae [of] ‘E.C.l. 1.99.10’.” Ans. 4. The Examiner finds that
Senior teaches that E.C.l. 1.99.10 is preferred “due to its ‘Km’8 being suitable
for measuring glucose . . . concentration in serum blood sample.” Id. at 12.
The Examiner notes that the Specification also identifies E.C.l. 1.99.10 as
“preferred” and teaches that E.C.l. 1.99.10 has “substrate specificity to
8 “The Michaelis Constant Km is that concentration of the substrate for an
enzyme at which the enzyme-catalysed reaction proceeds at half its
theoretical maximum rate at saturating (infinite) substrate concentration.”
Senior 6.
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Appeal 2015-002637
Application 12/851,668
glucose (relative activity of 100%) versus maltose (relative activity of
1.4%).” Id. at 4-5.
The Examiner finds that Yugawa A discloses a glucose biosensor for
measuring glucose concentration comprising an electrically insulated base
plate, an electrode system, and a reaction layer. Id. at 5—6. Yugawa B
discloses “substantially [the] same subject matters” as Yugawa A. Id. at 6.
The Examiner further finds that the Yugawa references teach that their
biosensors have three advantages: providing high stability, providing a
compact low-cost disposable design, and reduced amount of enzyme per
sensor. Id. The Examiner also finds that the Yugawa references teach that
their biosensor can be used with “different enzymes such as glucose
dehydrogenase (GDH) [and] even [the] quite different enzyme ‘fructose
dehydrogenase.’” Id.
Based on the combined teachings of Senior, Yugawa A, and Yugawa
B, the Examiner concludes that “[i]t would have been obvious to one of
ordinary skill in the art at the time the invention was made to design and
make the glucose biosensor comprising the Senior’s GDH of EC 1.1.99.10
based on the Yugawa[ references’] biosensor structure.” Id. The Examiner
finds that Senior would have suggested to the person of ordinary skill to use
E.C.1.1.99.10 because Senior teaches that its Km value is suitable for
measuring glucose in serum blood sample. Ans. 12. The Examiner further
finds that it would have been obvious to use a biosensor comprising an
insulating plate (layer), electrode system, and a reaction layer, as taught by
the Yugawa references, because the Yugawa references teach that such
sensors have high stability, require a reduced amount of enzyme per sensor,
and are compact, low-cost, and disposable. Ans. 7.
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Appeal 2015-002637
Application 12/851,668
We adopt the Examiner’s findings of fact and reasoning regarding the
scope and content of the prior art (Ans. 3—24; Final Act. 3—11) and agree
that the claims are obvious over Senior, Yugawa A, Yugawa B, and
Georgieff. We address Appellants’ arguments below.
Appellants argue that the Examiner improperly construed the claim
limitation requiring an “enzyme activity to maltose” of “5% or less” relative
to that of glucose to read on the activity of just GDH, rather than on the
activity of the entire reactive layer. Reply Br. 4—5. Appellants contend that
“multiple enzymes are necessarily present in the preparation of Senior” and
that Senior’s purification process “would only reduce the concentration of
protein impurities, not eliminate them.” App. Br. 6. These impurities could,
Appellants argue, affect the maltose activity of the preparation. Id. at 5—6.
As support, Appellants cite Tsuju9 as providing an example in which
purification of GDH from the same microorganism used in Senior —
Aspergillus oryzae — did not remove maltose activity. Id. at 6—7. Appellants
thus argue that the “possible presence of contaminants and the low degree of
purification make it impossible to conclude that the GDH preparation
discussed in Senior necessarily would have less than 5% activity toward
maltose relative to the activity of glucose.” Id. at 7 (citing Turner Deck 1
21).10 We are not persuaded.
Where the Examiner establishes a reasonable belief that the property
or characteristic recited in the claims would have been inherent to the
product or process, the burden of proof shifts to Appellants to show that this
9 Tsuji et al., US Patent No. 7,655,130 B2, issued Feb. 2, 2010 (“Tsuji”).
10 December 11, 2013 Declaration of Anthony Turner Under 37 C.F.R. §
1.132 (“Turner Decl.”).
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Application 12/851,668
characteristic or property is not possessed by the prior art. See In re Best,
562 F.2d 1252, 1254-55 (CCPA 1977); In re Spada, 911 F.2d 705, 708 (Fed.
Cir. 1990). Here, the enzyme disclosed in Senior — EC 1.1.99.10 — is
identified as preferred in the Specification. FF8. Enzymes that share the
same EC number necessarily possess identical enzymatic activity including
substrate specificity. FF11. Table 1 of the Specification reflects that the
activity of GDH EC 1.1.99.10 with respect to maltose is 1.4% of its activity
with respect to glucose. FF9&FF10. In view of these facts, the Examiner
has provided a reasonable basis for expecting Senior’s GDXT to have the
same properties as the claimed GDH, thus shifting the burden to Appellants
to disprove this fact.3 3
While we agree with the Appellants that the claims are directed to the
activity of the enzyme layer and not just of GDH, see Reply Br. 2-4, we do
not agree that the “possible presence of contaminants” in Senior’s enzyme
preparation renders the claimed biosensor non-obvious. As an initial matter.
Appellants’ speculation about the possibility that Senior’s preparation may
contain contaminants does not establish that the Senior’s preparation in fact
had such contaminants. Nor does Tsuji’s example of a contaminated
preparation establish the presence of such contaminants in Senior, at least
11 Appellants argue that the Examiner cannot rely on identity in structure
because “the structure at issue is the enzymatic reaction layer, which Senior
did not disclose.” Reply Br. 8. This argument is not persuasive because the
Examiner relied not on identity of reaction layers, but on the identity of
GDH E.C.1.1.99.10 derived from Aspergillus oryzae (as disclosed in Senior)
to the GDH E.C. 1.1.99.10 disclosed in the Specification with respect to
substrate specificity. The Examiner found that it would have been obvious
to incorporate Senior’s GDH E.C.1.1.99.10 in a biosensor having a reaction
layer as disclosed in the Yugawa references. Ans. 6—7.
10
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Application 12/851,668
because Tsuji relied on a different purification method than was used in
Senior. Moreover, we agree with the Examiner that to the extent Senior’s
preparation includes contaminants, it would have been “obvious for one of
ordinary skill in the art to modify . . . Senior’s chromatographic purification
to obtain better purity/yield of GDH since various protein purification means
have been commercially available and known in the art.” Advisory Act. at
2.12 As the Examiner explains, “one skilled in the art would be aware of the
drawback of having an impure enzyme (i.e., contaminated with enzyme
preparation that hydrolyze maltose) leading to false glucose readings and
would appropriately make every effort to use only a purified GDH enzyme
taught by Senior.” Ans. 12.
Appellants argue that “even if there had been a suggestion for further
purification, contrary to Senior’s explicit teaching that it was not necessary,
the cited prior art references are devoid of any teaching that one of ordinary
skill could have purified a flavin-dependent GDH sufficiently to remove
contaminating activity to the extent required by the claims.” App. Br. 7.
We are not persuaded. The Examiner finds that Senior’s enzyme
preparation can be purified using purification means that are “commercially
available and known in the art.” Advisory Act. 2. This finding is supported
by the Specification’s teaching that “glucose dehydrogenase can be
recovered from the culture by means of an ordinary protein purification
method.” FF12; see also, Hearing Tr. 5 (affirming that Appellants do not
12 Advisory Action mailed January 10, 2014 (“Advisory Act.”).
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Appeal 2015-002637
Application 12/851,668
contend that the person of ordinary skill would have been unable to purity
GDH to the levels that are claimed).13
Appellants acknowledge Senior’s teaching that E.C.1.1.99.10 is
preferred, but argue that by the time Yugawa was published the concerns
that led to E.C. 1.1.99.10 being preferred were proven to be unfounded.
Hearing Tr. 8—10; Reply Br. 19—20. Senior explains why E.C.1.1.99.10 is
preferred as follows:
The constant for glucose dehydrogenase E.C. 1.1.99.17 from
Acinetobacter is approximately 2 mM. The constant for E.C.
1.1.99.10 from Aspergillus oryzae is approximately 20 mM.
The consequence of this is that the useful range in which the
reaction rate is linearly proportional to substrate concentration
differs by a factor of 10 for these two enzymes. Thus when the
concentrations to be determined are small it is preferred to use
the enzyme having the lower Km, i.e. in this instance E.C.
1.1.99.17. Conversely when, as is often the case with serum
samples, the concentrations to be determined may be relatively
high it is preferred to use the enzyme having the higher Km, i.e.
in this instance E.C. 1.1.99.10.
FF7. Appellants argue that the concerns expressed in Senior regarding the
use of enzymes other than E.C. 1.1.99.10 are unfounded because Yugawa A
“disclosed that a biosensor using PQQ-GDH can detect glucose
concentration effectively over a broad concentration range.” Reply. Br. 19.
The range of glucose concentrations detected “encompassed the range of
5mM to 40mM that the Examiner alleged to occur in blood samples.” Id.
Thus, Appellants argue, “one of ordinary skill would not have considered
[the] ability to make serum glucose measurements an advantage of Senior’s
13 Transcript May 22, 2017 Oral Hearing, mailed June 20, 2017 (“Hearing
Tr.”).
12
Appeal 2015-002637
Application 12/851,668
EC 1.1.99.10 enzyme relative to the PQQ-GDH.” Id. at 21. We are not
persuaded.
Senior provides a clear teaching that E.C. 1.1.99.10 is preferred for use
with serum samples. FF7. Yugawa A’s disclosure that PQQ-GDH can
detect glucose over a broad concentration range does not diminish this
teaching. Crediting Appellants’ argument (that Yugawa A shows that PQQ-
GDH is useful for making glucose measurements in serum), simply
establishes that PQQ-GDH and E.C. 1.1.99.10 are both useful for the same
purpose — measuring glucose in serum; it does not render the claimed
invention non-obvious. Accordingly, we find the references relied on by the
Examiner support a prima facie case of substituting E.C. 1.1.99.10 for PQQ-
GDH. See In reFout, 675 F.2d 297, 301 (CCPA 1982) (“Because both
[references] teach a method for separating caffeine from oil, it would have
been prima facie obvious to substitute one method for the other.”)
Appellants argue that objective indicia of non-obviousness, including
long-felt need and the failure of others to satisfy that need demonstrate the
non-obviousness of the claimed biosensor. App. Br. 11—18. The need that
Appellants identify as solved by the claimed biosensor is set forth in the
Turner Declaration, which states:
I co-authored the article D’Costa et al., Biosensors 2, 71-87
(1986). ... In that article, we stated that there was an “urgent
need for improved methods of blood glucose monitoring” and
that it would be “ideal” if the dehydrogenase enzymatic action
of a glucose sensor would “have no cofactor requirement” and
be specific to “a single substrate.”
Turner Decl. 110. The Turner Declaration further states: “Even though the
need for a dehydrogenase-based glucose sensor with both of those properties
was desired at least as early as 1986,1 was not aware of such a sensor that
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Application 12/851,668
had both of those properties before December 24, 2003.” Id. Dr. Turner
explains that biosensors based on NAD-GDH enzymes do not satisfy this
need because they require a cofactor. Id. at || 14—15. Although Senior does
not require a cofactor, Dr. Turner contends that Senior’s disclosure failed to
satisfy the need for a dehydrogenase-based glucose sensor because of the
“possible presence of contaminants and the low degree of purification.” Id.
at 1118-24.
Appellants argue that 20 years elapsed after the publication of Senior
and 17 years elapsed after the documented recognition of the need during
which no one, to Dr. Turner’s knowledge, carried Senior’s alleged teachings
forward to produce a biosensor that solved the need. App. Br. 14—15 (citing
Turner Decl. 116). Appellants assert that “the persistence of this need is all
the more remarkable because the nature of the biosensor industry indicates
that others very likely tried and failed to solve the need.” Id. at 15.
Appellants have not persuaded us that objective indicia of non­
obviousness demonstrates the non-obviousness of the claimed biosensor
because the scope of the claims is not commensurate with the asserted need.
Claim 22 employs the transitional phrase “comprising,” and thus does not
exclude biosensors that employ a cofactor. The claims thus encompass
biosensors that use cofactors and thus do not satisfy the alleged need for
dehydrogenase-based glucose sensors that do not rely on a cofactor.
Accordingly, Appellants’ evidence of long felt need and of failure to satisfy
that need is not persuasive. See Application of Tiffin, 448 F.2d 791, 792
(CCPA 1971) (finding that “appellants’ evidence of commercial success and
the satisfaction of a long-felt need, both the success and the need being with
respect to ‘cups’ used in vending machines was sufficient to overcome the
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Application 12/851,668
Patent Office’s case of prima facie obviousness” for claims reciting “cups”
but not for claims “reciting ‘containers’ generally”); see also In re
Greenfield, 571 F.2d 1185, 1189 (CCPA 1978) (concluding that evidence of
secondary considerations was not commensurate with the scope of the
claims where that evidence related to a single compound and there was no
adequate basis to conclude that other compounds included within the scope
of the claims would exhibit the same behavior).
Finally, Appellants argue that Yugawa’s teachings regarding the
advantages of PQQ-GDH teach away from the use of use of E.C. 1.1.99.10.
App. Br. 18—22. A reference teaches away from a claimed invention if it
“criticize[s], discredits], or otherwise discourage[s]” modifying the
reference to arrive at the claimed invention. In re Fulton, 391 F.3d 1195,
1201 (Fed. Cir. 2004). The teachings identified by Yugawa regarding the
advantages of PQQ-GDH do not meet this standard. As the statements in
Yugawa regarding the advantages of PQQ-GDH do not include any criticism
of E.C. 1.1.99.10, we find that it does not constitute a teaching away. DyStar
Textilfarben GmbH & Co. Deutschland KG v. C.H. Patrick Co., 464 F.3d
1356, 1364 (Fed. Cir. 2006) (“We will not read into a reference a teaching
away from a process where no such language exists.”). Accordingly, we
affirm the Examiner’s rejection of claims 22, 25—28, and 31—33 as obvious
over the combination of Senior, Yugawa A, Yugawa B, and Georgieff.
THE SECOND REJECTION
Appellants argue that the Second Rejection should be reversed for the
reasons provided in connection with the First Rejection, noting that adding
Matsumoto to the combination of references relied upon in the First
Rejection does not remedy any alleged deficiencies. Accordingly, we affirm
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the Examiner’s rejection of claims 23, 24, 29, and 30 as obvious over the
combination of Senior, Yugawa A, Yugawa B, Georgieff, and Matsumoto
for the reasons discussed in connection with the First Rejection.
SUMMARY
For the reasons set forth herein and those set forth in the Examiner’s
Answer and Final Office Action, we affirm the Examiner’s rejection of
claims 22, 25—28, and 31—33 as obvious over the combination of Senior,
Yugawa A, Yugawa B, and Georgi and the Examiner’s rejection of claims
23, 24, 29 and 30 as obvious over the combination of Senior, Yugawa A,
Yugawa B, Georgieff, and Matsumoto.
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a)(1).
AFFIRMED
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