Ex Parte Baur et al

Board of Patent Appeals and Interferences

Aug 24, 2011

11194333 (B.P.A.I. Aug. 24, 2011)

UNITED STATES PATENT AND TRADEMARKOFFICE
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.
11/194,333 08/01/2005 Dieter Baur H 05724 US 9652
79525 7590 08/24/2011
Henkel Corporation
10 Finderne Avenue, Suite B
Bridgewater, NJ 08807
EXAMINER
GOUGH, TIFFANY MAUREEN
ART UNIT PAPER NUMBER
1651
MAIL DATE DELIVERY MODE
08/24/2011 PAPER
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.
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte DIETER BAUR, WERNER PICHLER,
WILFRIED RAEHSE, and JENS VAN HOLT
__________

Appeal 2010-011532
Application 11/194,333
Technology Center 1600
__________

Before ERIC GRIMES, MELANIE L. McCOLLUM, and STEPHEN
WALSH, Administrative Patent Judges.

McCOLLUM, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to a process
for refining concentrated enzyme solutions. The Examiner has rejected the
claims as obvious. We have jurisdiction under 35 U.S.C. § 6(b). We affirm.
Appeal 2010-011532
Application 11/194,333

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STATEMENT OF THE CASE
Claims 1-7, 9-14, 16, 18-34, 36, and 37 are on appeal (App. Br. 5).1
The claims subject to each rejection have not been argued separately and
therefore stand or fall together. 37 C.F.R. § 41.37(c)(1)(vii). Claim 1 is
representative and reads as follows:
1. A process for refining concentrated enzyme solutions comprising
the steps of: (a) providing a concentrated enzyme solution comprised of
insoluble solids; (b) separating the insoluble solids to produce a supernatant
solution having a solids content of no more than 1% by volume and
(c) contacting the supernatant solution with a strongly basic anion exchanger
having an effective pore size of from 0.2 to 0.7 mm carried out with a bed
volume ratio of from 2 to 5 and a residence time of from 0.01 to 0.2 g of
enzyme per g of carrier material per minute to remove a portion of colorless
impurities whereby the enzymes remain in solution to produce an eluate
comprising a decolorized protein solution comprising colorless impurities
having a stabilizing effect on the protein solution.
Claims 1-7, 9-14, 16, 18-34, 36, and 37 stand rejected under 35 U.S.C.
§ 103(a) as obvious over Shetty2 in view of Scopes,3 Mitsubishi,4 Diaion,5
and Paatz US6 (Ans. 4).
Claims 1-7, 9-14, 16, and 20-25 stand rejected under 35 U.S.C.
§ 103(a) as obvious over Shetty in view of Scopes, Mitsubishi, Diaion, and
Boyer7 (Ans. 8).

1 Claims 35 and 38-42 are also pending but have been withdrawn from
consideration (App. Br. 5).
2 Shetty et al., US 5,405,767, Apr. 11, 1995.
3 Scopes, Protein Purification: Principles and Practice 5-8 & 15-16 (2d ed.
1987).
4 Mitsubishi Chemical Corp., Manual of Ion Exchange Resins and Synthetic
Adsorbent, 1 HANDBOOK DIAION 104-108 (2d ed. 1995).
5 Diaion Product Line Brochure 4-6 (2001).
6 Paatz et al., US 6,350,728 B1, Feb. 26, 2002.
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Claims 1, 18, and 19 stand rejected under 35 U.S.C. § 103(a) as
obvious over Shetty in view of Scopes, Mitsubishi, Diaion, Paatz WO,8 and
Sova9 (Ans. 12).
The Examiner relies on Shetty for disclosing “a purified concentrated
enzyme product and method of producing such enzyme” (Ans. 4). In
particular, the Examiner finds that “Shetty disclose[s] that enzyme
concentrates are traditionally prepared by ultrafiltration and evaporation . . .
and disclose[s] removing polysaccharides and polymers,[ ]i.e, solids” (id.).
The Examiner also finds that “Shetty teach[es] the purification of an alkaline
protease,” but that “enzymes such as amylases, cellulases, hemicellulases,
lipases and oxidases may be used” (id. at 4-5). In addition, the Examiner
finds:
After fermentation, the enzyme solution is formed by separating
the enzyme from microbial cells, solids and fermentation
materials by using conventional separation techniques such as
centrifugation. . . . The protease solution is then concentrated
using ultrafiltration until the desired enzyme activity is
obtained, although concentration of the enzyme may be
practiced by any conventional concentration method.
(Id. at 5.)
The Examiner relies on Scopes for disclosing “successful enzyme
concentration methods such as ion exchange, i.e, anion exchanger and
ultrafiltration, along with centrifugation” (id.).

7 Boyer et al., US 5,565,348, Oct. 15, 1996.
8 Paatz et al., WO 01/37628 A2, May 31, 2001.
9 Sova, US 5,256,269, Oct. 26, 1993.
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The Examiner relies on Mitsubishi for teaching “strongly basic anion
exchange resins” (id.). The Examiner finds that the “highly porous strongly
basic anion resins are used for treating substances with large molecules,
specifically useful in enzyme purification, making insoluble enzymes and
particularly for decolorization of solutions” (id. at 5-6).
The Examiner relies on Diaion for teaching strongly basic anion
exchange resins (id. at 6). In particular, the Examiner finds that Diaion
discloses “gel-type strongly basic anion exchange resins . . . , which are
mainly used for decolorization of solutions and purification” and have an
“exchange capacity to range from 0.8 to 1.3 meq/ml” and “an effective poor
[sic, pore] size of 0.4 mm (minimum)” (id.). In addition, the Examiner finds
that Diaion discloses “porous-type strongly basic anion exchange resins . . . ,
which have been applied in many separation processes including
decolorization” and have an “exchange capacity to range from 0.9 to 1.3
meq/ml” and “an effective poor [sic] size of 0.4 mm” (id.).
The Examiner concludes that it would have been obvious “to have
produced a decolorized protein solution by contacting the concentrated
enzyme solution with a strongly basic anion exchanger such as those
disclosed by Mitsubishi and Diaion because they both teach the exchangers
to be particularly useful for decolorizing solutions” (id.). The Examiner
finds that, “[a]lthough, Mitsubishi and Diaion do not disclose a specific
amount of time a solution should be in contact with the exchanger, it would
be obvious to optimize th[is] result effective variable[] by routine
experimentation” (id.). The Examiner also finds “that the limitation of
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having a bed volume ratio of from 2 to 5 would be simple routine
optimization of a result effective variable” (id. at 15).
Appellants argue that “the Examiner failed to show that the claim
limitation that the bed to volume ratio of from 2 to 5 occurs in the prior art
of record or in the general knowledge in the art” (App. Br. 9 & 12).
ISSUE
With regard to each ground of rejection, the issue is: Does the
evidence support the Examiner’s conclusion that it would have been obvious
to contact the solution with a strongly basic anion exchanger with a bed
volume ratio of from 2 to 5?
FINDINGS OF FACT
We rely on the Examiner’s findings of fact as set forth in the
Examiner’s Answer. However, we also rely on the following recitations in
the Specification:
1. The Specification states: “The chromatography step (C) is
advantageously carried out under certain conditions. These include in
particular a certain bed volume, which is the ratio by volume of the
substance applied to that of the column.” (Spec. ¶ [0059].)
2. The Specification also states:
It has proved to be particularly advantageous and characterizes
correspondingly preferred embodiments to carry out step (C)
with a bed volume of 1 to 10, preferably 1.5 to 7 and more
preferably 2 to 4. These bed volumes represent the optimum
experimentally determined in the EXAMPLES for keeping the
filtrate as clean and at the same time as concentrated as
possible.
(Id. at ¶ [0060].)
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3. In addition, the Specification states:
The decoloring quality and hence the stability of the enzyme
were controlled through the bed volume ratio (BV - ratio by
volume of the enzyme concentrate to the resin) and the
residence time. A ratio of 2 to 5 BV and a dosage of 0.05 kg
enzyme solution per kg resin per min. were adjusted.
(Id. at ¶ 0095].)
PRINCIPLES OF LAW
“[W]here the general conditions of a claim are disclosed in the prior
art, it is not inventive to discover the optimum or workable ranges by routine
experimentation.” In re Aller, 220 F.2d 454, 456 (CCPA 1955). “Only if
the ‘results of optimizing a variable’ are ‘unexpectedly good’ can a patent be
obtained for the claimed critical range.” In re Geisler, 116 F.3d 1465, 1469
(Fed. Cir. 1997) (quoting In re Antonie, 559 F.2d 618, 620 (CCPA 1977)).
ANALYSIS
We conclude that the Examiner has the better position. It is
undisputed that the applied references suggest contacting an enzyme solution
with a strongly basic anion exchanger (Ans. 5-6). Although the Examiner
has not pointed to a particular teaching of the bed volume ratio to be used,
we agree with the Examiner that it would have been obvious to determine
the optimum or workable ranges (id. at 15).
In addition, Appellants have not presented evidence that the claimed
range is critical. Although Appellants argue that they “discovered the
criticality of the claimed value range of bed volume ratio” (Reply Br. 6),
they point to no evidence showing that a bed volume ratio of 2 to 5 is
critical. As noted above, the Specification discloses that “preferred
embodiments” include those using bed volume ratios between 1 and 10,
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which is evidence that the range recited in claim 1, while more preferred, is
not critical.
CONCLUSION
The evidence supports the Examiner’s conclusion that it would have
been obvious to contact the solution with a strongly basic anion exchanger
with a bed volume ratio of from 2 to 5. We therefore affirm the obviousness
rejections.
TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).

AFFIRMED

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