Ex Parte Arnaut et al

Patent Trial and Appeal Board

Dec 21, 2015

10510401 (P.T.A.B. Dec. 21, 2015)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
10/510,401 05/12/2005
321 7590 12/23/2015
SENNIGER POWERS LLP
100 NORTH BROADWAY
17THFLOOR
ST LOUIS, MO 63102
FIRST NAMED INVENTOR
Filip Arnaut
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
ATTORNEY DOCKET NO. CONFIRMATION NO.
PRTO 6832 6305
EXAMINER
BADR, HAMID R
ART UNIT PAPER NUMBER
1791
NOTIFICATION DATE DELIVERY MODE
12/23/2015 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):
uspatents@senniger.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Exparte FILIP ARNAUT, FABIENNE VERTE,
and NICOLE VEKEMANS
Appeal2013-002091
Application 10/510,401 1
Technology Center 1700
Before ADRIENE LEPIANE HANLON, BEYERL YA. FRANKLIN, and
JEFFREY W. ABRAHAM, Administrative Patent Judges.
HANLON, Administrative Patent Judge.
uECISION ON APPEAL
A. STATEMENT OF THE CASE
The Appellants filed an appeal under 35 U.S.C. § 134 from a rejection of
claims 1, 3-9, 24--27, and 32--41. We have jurisdiction under 35 U.S.C. § 6(b).
We REVERSE.
The claims on appeal are directed to a method for preventing or retarding the
staling of bakery products comprising, inter alia, the step of adding an antistaling
composition to a dough wherein the antistaling composition comprises at least one
1 According to the Appellants, the real party in interest is Puratos Naamloze
Vennootschap. Appeal Brief dated July 20, 2012 ("App. Br.") 1.
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Application 10/510,401
intermediate thermostable and/or thermostable serine protease such as keratinase,
Taq polymerase, or thermitase. Spec. i-fi-120-22.
The Appellants disclose:
The proteases may be obtained from the respective micro-
organisms by use of any suitable technique. For instance, the protease
preparation may be obtained by fermentation of a micro-organism and
subsequent isolation of the protease containing preparation from the
resulting broth by methods known in the art such as centrifugation and
ultrafiltration.
Spec. i139.
Claims 1, 40, and 41 are the independent claims on appeal. Claim 1 is
reproduced below from the Claims Appendix of the Appeal Brief dated July 20,
2012 ("App. Br."). The limitations at issue are italicized.
1. A method for the prevention or retarding of staling during the
baking process of bakery products comprising:
forming a dough with the addition of an antistaling composition
comprising an amount of at least one intermediate thermostable and/or
thermostable serine protease; and
baking said dough, wherein:
said intermediate thermostable and/or thermostable serine
protease comprised in said antistaling composition has a temperature
activity optimum between 60QC and 95QC;
the ratio between the protease activity in said antistaling
composition at optimum temperature and the protease activity at 2 5QC
is higher than 1 O;
said protease is active during baking; and
said amount is effective to prevent or retard staling in said
bakery products.
App. Br. 37 (emphasis added).
Similarly, claim 40 recites "[a] method for the prevention or retarding
of staling during the baking process of bakery products" comprising the
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steps recited in claim 1. However, claim 40 recites that the intermediate
thermostable and/or thermostable serine protease has a temperature activity
optimum between 70QC and 95QC. App. Br. 40-41.
Claim 41 recites that the serine protease in the antistaling composition is
"selected from the group consisting of a Taq protease and a keratinase" wherein
"the ratio between the protease activity in said antistaling composition at optimum
temperature and the protease activity at 25QC is higher than 10." App. Br. 41
(emphasis added).
The Appellants seek review of the following rejections on appeal:
(1) claims 1, 3-9, 24--27, and 32--40 under 35 U.S.C. § 112, second
paragraph, as being indefinite;
(2) claims 1, 3-7, 9, 24, 26, and 40 under 35 U.S.C. § 102(b) as
anticipated by Klingenberg et al.;2
(3) claims 8, 24--27, and 32 under 35 U.S.C. § 103(a) as unpatentable
over Klingenberg in view of Kauppinen et al.; 3 and
(4) claims 7, 33-39, and 41under35 U.S.C. § 103(a) as unpatentable
over Klingenberg in view ofKauppinen, and further in view of Terada et al., 4
Chemoglazov et al., 5 and Matsuzawa. 6
2 DD 156,714 A, issued September 15, 1982 ("Klingenberg"). We refer to the
English translation of Klingenberg which was filed in the instant application on
February 16, 2009.
3 US 5,994,113, issued November 30, 1999 ("Kauppinen").
4 US 5,124,261, issued June 23, 1992 ("Terada").
5 RU 2, 177,994 published Jan. 10, 2002 ("Chemoglazov").
6 Hiroshi Matsuzawa et al., Purification and Characterization of Aqualysin I (A
Thermophilic Alkaline Protease) Produced by Thermus Aquaticus YT-1, 171 Eur.
J. Biochem. 441-47 (1988) ("Matsuzawa").
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Application 10/510,401
B. DISCUSSION
1. Rejection (1)
The Examiner concludes that the phrase "said amount is effective to prevent
or retard staling in said bakery products" recited in claims 1 and 40 renders the
claims indefinite. More specifically, the Examiner finds "there is no clear
condition for testing the anti-staling effect during baking," "there is no clear
indication of storage conditions under which staling is prevented or retarded," and
"it is not clear how long the staling will be prevented or retarded or to what
degree." Ans. 2 (emphasis added).
The Appellants argue that the Examiner construes the phrase "'during the
baking process'" in the preamble of claims 1 and 40 "to mean that the claimed
method is for preventing or retarding staling that occurs during baking." Reply Br.
5 (emphasis added). 7 The Appellants, however, contend that one of ordinary skill
in the art would understand the preamble of claims 1 and 40 "to mean that the
essential step of the method for preventing or retarding staling is performed during
the baking process." Reply Br. 6 (emphasis added). For support, the Appellants
direct our attention to the "terms of claims 1 and 40 which require that the protease
of the antistaling composition be active during baking and that the optimum
proteolytic activity correspond to temperatures typically encountered during
baking." Id. The Appellants also contend that "those skilled in the art understand
that staling occurs with time and begins after the product is baked." Id.; see also
Ans. 8 ("staling as known in the art takes place (or at least evaluated) during the
storage time of baked products").
7 Reply Brief dated November 26, 2012.
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As for testing the antistaling effect after baking, the Appellants direct our
attention to paragraphs 71-87 of their Specification (Examples 1-3) which disclose
that the antistaling effect may be tested by measuring crumb softness and/or
elasticity. App. Br. 6; Reply Br. 7. The Appellants argue that testing is relative to
a control sample "tested under the same conditions as the sample containing the
antistaling composition and serves as the basis for ... determining the antistaling
effect." App. Br. 7. Thus, according to the Appellants, no recitation of storage
conditions, absolute rates of staling, or time periods for preventing or retarding
staling are required in the claims for an understanding of their scope. Id.
"[T]he definiteness of the language employed [in a claim] must be
analyzed-not in a vacuum, but always in light of the teachings of the prior art and
of the particular application disclosure as it would be interpreted by one possessing
the ordinary level of skill in the pertinent art." In re Moore, 439 F.2d 1232, 1235
(CCP A 1971 ). The preamble of claims 1 and 40 recites "[a] method for the
prevention or retarding of staling during the baking process of bakery products."
It is clear from the Appellants' Specification that the method for preventing or
retarding the staling of a bakery product is carried out during the baking process by
adding "at least one intermediate thermostable and/or thermostable serine
protease" to unbaked dough but testing for the antistaling effect occurs when
baking is complete. See, e.g., Spec. i-fi-1 71-7 5 (disclosing that softness and
elasticity of a bread are measured after the bread has been baked).
The Appellants disclose that the antistaling effect is measured by at least the
softness of the baked bread. See, e.g., id. i1 3 (bread staling includes a hardening of
the crumb). To measure the softness of a bakery product prepared according to the
claimed method, the Appellants provide a basic bread recipe and a bread making
process and measure the loss in softness between day 1 and day 6 after baking.
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See, e.g., id. i-fi-165, 66, 73. The Appellants compare the softness of bread made
with and without the addition of one of the disclosed serine proteases. Id. i-fi-1 71,
76, 81 and Tables 1---6. The Appellants disclose that loss of softness is "a relative
measure" and "absolute values have no meaning as such but should be compared to
a reference for interpretation." Id. i168.
Based on the foregoing, we find that one of ordinary skill in the art would
have understood that the amount of "at least one intermediate thermostable and/or
thermostable serine protease ... effective to prevent or retard staling in said bakery
products" as recited in claims 1 and 40 is any measurable amount of the claimed
serine protease that prevents or retards staling of the claimed bakery products over
time compared to a control. We further find that one of ordinary skill in the art
would have understood the control to be a bakery product that has the same recipe,
is prepared using the same process, and is held under the same testing conditions as
the claimed bakery product but does not contain intermediate thermostable and
thermostable serine proteases as recited in claims 1 and 40. Based on these
findings, we conclude that claims 1 and 40 are definite under 35 U.S.C. § 112,
second paragraph.
The rejection of claims 1, 3-9, 24--27, and 32--40 under§ 112, second
paragraph, is not sustained.
2. Rejection (2)
Independent claims 1 and 40 recite "[a] method for the prevention or
retarding of staling during the baking process of bakery products comprising,"
inter alia, the step of "forming a dough with the addition of an antistaling
composition comprising an amount of at least one intermediate thermostable
and/or thermostable serine protease" wherein "the ratio between the protease
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activity in said antistaling composition at optimum temperature and the protease
activity at 25QC is higher than 10." App. Br. 37, 40-41.
The invention disclosed in Klingenberg:
relates to a method for producing a thennophilic protease from
Thermoactinomyces vulgaris with special properties for the partial
hydrolysis of animal and vegetable proteins. The enzyme thermitase
being produced is suitable for use in various processes in the food
industry as crude preparation or in partially purified form, and in
highly purified form as fine biochemical. Fields of application are
gluten breakdown in the production of processed foodstuff, waffles,
and bakery products, the preparation of protein partial hydrolysates
for certain target groups, for example for diet purposes or the
nourishment of sick people and convalescent patients. The method
for producing thermitase is suitable for the large-scale production of
the enzyme in agitated fermenters.
Klingenberg 2 (emphasis added).
The Examiner finds Klingenberg discloses that the optimum temperature of
thermitase is "between 60-70C." Ans. 3. The Examiner also finds that thermitase,
as described in Klingenberg, includes a "highly pure form of this enzyme" and "is
one of the claimed enzymes from the same source organism." Ans. 9, 12. Thus,
the Examiner finds that "all characteristics described in instant claims are inherent
in the enzyme of [Klingenberg]."8 Ans. 9; see also Ans. 11.
At the outset, we note Klingenberg discloses that in the food industry
thermitase is used "as crude preparation or in partially purified form," not in highly
8 Klingenberg does not expressly disclose using thermitase to prevent or retard
staling of bakery products as recited in the claims on appeal. Nonetheless, the
Examiner finds that gluten breakdown, as disclosed in Klingenberg, "means the
partial hydrolysis of gluten network in bakery products which inherently leads to
retardation of staling to the extent the gluten network is involved in staling." Ans.
4.
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purified form as found by the Examiner. Klingenberg 2. Focusing on the crude
preparation of thermitase disclosed in Klingenberg, the Appellants argue:
Though not recognized in [Klingenberg], T. vulgaris produces several
proteases resulting in an extract containing a mixture of proteases.
See, for example, page 18, paragraph [0057], lines 9-15 of applicants'
specification as filed. [9J The temperature optimum of the proteolytic
activity obtained in [Klingenberg] is, as mentioned by the Office,
60QC-70QC, while the temperature optimum of the purified thermitase
described in the present patent application is about 85QC in the
comparable measurements on ( azo) casein substrate ... Y OJ This
important difference of about 20QC (i.e. about 25%) may be due to the
presence of non-thermoactive contaminant proteases other than
thermitase in the enzyme preparation of [Klingenberg], the use of a
different T. vulgaris strain, or other factors.
App. Br. 13.
In this regard, the Appellants argue that "[t]he presence of contaminant
proteases [in Klingenberg] is ... reflected by the fact that the cleavage obtained by
the crude extract of [Klingenberg] containing proteases is 'largely non-specific."'
App. Br. 13-14; see also Klingenberg 3 (disclosing that "by cultivating
Thermoactinomyces vulgaris on suitable nutrient substrates, a thermophilic
9 Paragraph 57 of the Appellants' Specification discloses:
In the case of the thermophilic microorganism,
Thermoactinomyces vulgaris, it is known that during the logarithmic
phase of multiplication several proteolytic enzymes are secreted into
the surrounding medium. Among the up to five proteolytic
components of the culture filtrate one protease dominates amounting
70 to 80% of the total activity, termed thermitase.
10 Paragraph 58 of the Appellants' Specification discloses:
Depending on the size of the substrate, thermitase shows maximum
activity at temperatures ranging from 65QC (gelatin), 70QC (protamine)
to 85QC (azocasein). The temperature optimum is most pronounced
with the biggest substrate (azocasein): activity at 85QC is 12 times
over the activity shown at 25QC.
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Application 10/510,401
protease can be produced, the optimum temperature of which is 60- 70 QC and
which causes a largely non-specific and for this reason extensive cleavage of
animal and vegetable proteins").
Moreover, the Appellants argue that:
[T]he activity ratio of 12 as disclosed in paragraph [0058] of the
application is associated with a different strain of T. vulgaris (NRRL
b-161 7) [than disclosed in Klingenberg (IME T 9 512 and IME T
9515)] and to conditions for having a composition whose proteolytic
activity is developed for thermoactive properties (see paragraphs
[0057]-[0059] applicants' specification as filed).
App. Br. 14--15; Klingenberg 3.
Finally, the Appellants argue:
In view of the fact that the optimal temperature of the composition
comprising proteases as in [Klingenberg] is about 20QC (i.e. 25%)
lower than the optimal temperature in the composition of the present
patent application (yet both comprising thermitase ), [Klingenberg]
cannot implicitly disclose an activity ratio of at least 10 as in claims 1
and 40.
App. Br. 15.
For an anticipation rejection to be proper, the prior art "must clearly and
unequivocally" describe the claimed invention or direct one of ordinary skill in the
art to the claimed invention "without any need for picking, choosing, and
combining various disclosures." In re Arkley, 455 F.2d 586, 587-88 (CCPA
1972).
We find the Examiner has failed to show, in the first instance, that the
thermitase employed by Klingenberg to break down gluten is identical or
substantially identical to the Appellants' thermitase. See In re Oetiker, 977 F.2d
1443, 1445 (Fed. Cir. 1992) (the examiner bears the initial burden of presenting a
prima facie case of unpatentability). Thus, the Examiner's finding that "all
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characteristics described in instant claims are inherent in the enzyme of
[Klingenberg]" is not supported by the record. Ans. 9.
Regarding the claimed ratio of protease activity recited in claims 1 and 40,
the Examiner also finds that "a thennophilic/thermoactive enzyme with a high
optimum temperature for activity will be much more active at high temperatures
(high optimum temperature) than the same enzyme at much lower temperature e.g.
25C." Ans. 3. Therefore, the Examiner finds "the ratio of the two activities (70C
vs 25C) [of the enzyme disclosed and characterized by Klingenberg] will be in the
range as presently claimed." Id. at 10.
The Appellants argue that the Examiner does not cite any disclosure in
Klingenberg to support the assumption that "a thermostable enzyme with a high
optimum temperature for activity will be much more active at high temperatures
than the same enzyme at much lower temperature." App. Br. 1 O; see also Reply
Br. 8-9 (arguing the Examiner makes assumptions as to the activity of
Klingenberg's enzyme at 25QC). ivforeover, "even though a thermostable protease
may have a high optimum temperature for activity," the Appellants argue that "it
does not necessarily follow that the thermostable protease can match the very high
activity ratios of 10 or 15 as claimed." App. Br. 10.
Significantly, the Examiner does not direct us to any portion of Klingenberg
disclosing the activity of thermitase as a crude preparation or in partially purified
form at optimum temperature or at 25QC. The mere fact that the enzyme may be
much more active at high temperatures than at a much lower temperature does not
establish that the activity ratio of thermitase, described in Klingenberg as a crude
preparation or in partially purified form, is higher than 10 as recited in claims 1
and 40.
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For the reasons set forth above, the § 102 (b) rejection of claims 1, 3-7, 9,
24, 26, and 40 is not sustained.
3. Rejection (3)
Claims 8, 24-27, and 32 ultimately depend from claim 1 or claim 40. The
Examiner's factual findings and legal conclusions based on Klingenberg and
Kauppinen in rejection (3) do not cure the deficiencies of Klingenberg discussed
above in connection with the§ 102(b) rejection. Therefore, the§ 103(a) rejection
of claims 8, 24-27, and 32 is not sustained.
4. Rejection (4)
The Examiner finds that Klingenberg is silent regarding protease of Thermus
aquaticus and Keratinase of Bacillus licheniformis. The Examiner finds Terada
discloses a process for producing aqualysin I by cultivating Thermus aquaticus and
Matsuzawa discloses that Thermus aquaticus produces both aqualysin I and II
which have optimum temperatures around 75QC and 95QC, respectively. The
Examiner also finds Chemoglazov discloses a new keratinase from Bacillus
licheniformis that can be used in the food industry. Ans. 6-7.
The Examiner concludes that incorporating other thermoactive proteases,
such as the thermoactive proteases disclosed in Terada, Chemoglazov, and
Matsuzawa, in the process of Klingenberg would have been obvious to one of
ordinary skill in the art. Id. at 7, 18.
Significantly, the Examiner has not directed us to any disclosure in Terada,
Chemoglazov, or Matsuzawa that describes, either expressly or inherently, or
renders obvious a Taq protease or a keratinase having an activity ratio within the
range recited in claim 41. See App. Br. 32. For this reason, the§ 103(a) rejection
of claims 7, 33-39, and 41 is not sustained.
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C. DECISION
The decision of the Examiner is reversed.
REVERSED
bar
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