Ex Parte Bergeron

Patent Trial and Appeal Board

Sep 24, 2012

11281009 (P.T.A.B. Sep. 24, 2012)

UNITED STATES PATENT AND TRADEMARK OFFICE
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BEFORE THE PATENT TRIAL AND APPEAL BOARD

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Ex parte CHANTAL BERGERON
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Appeal 2012-000138
Application 11/281,009
Technology Center 1600
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Before ERIC GRIMES, LORA M. GREEN, and
MELANIE L. McCOLLUM, Administrative Patent Judges.

GRIMES, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to methods
for whitening teeth. The Examiner has rejected the claims as obvious. We
have jurisdiction under 35 U.S.C. § 6(b). We affirm.
STATEMENT OF THE CASE
The Specification discloses “methods for the whitening of natural and
manufactured teeth without the use of peroxides or abrasives” (Spec. 2,
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¶ 0004). “The active ingredient in the present invention is ‘actinidin’ … and
is produced from kiwifruit” (id.).
Claims 1-5 and 7 are on appeal. Claim 1 is representative and reads
as follows:
1. A method for whitening natural or manufactured teeth, the method
comprising:
a) providing a peroxide-free actinidin-containing preparation;
b) formulating the actinidin-containing preparation of step a) for
application to natural or manufactured teeth, wherein the formulation thus
obtained is also peroxide-free; and
c) contacting the peroxide-free formulation of step b) with natural or
manufactured teeth in an amount and for a period of time sufficient to effect
whitening of the natural or manufactured teeth.

The claims stand rejected under 35 U.S.C. § 103(a) as follows:
• Claims 1-3, 5, and 7 in view of Browning1 and Carne;2 and
• Claim 4 in view of Browning, Carne, and Glace.3
I.
Issue
The Examiner has rejected claims 1-3, 5, and 7 under 35 U.S.C.
§ 103(a) as obvious in view of Browning and Carne. Claims 2, 3, 5, and 7
have not been argued separately and therefore stand or fall with claim 1. 37
C.F.R. § 41.37(c)(1)(vii).

1 J. Browning et al., Comparison of Oxidizing Agents and Proteolytic
Enzymes on Whitening Teeth, 73 JOURNAL OF DENTAL RESEARCH (1
SUPPL)323 (abstract 1774) (1994).
2 Alan Carne et al., The Amino Acid Sequence of the Tryptic Peptides from
Actinidin, a Proteolytic Enzyme from the Fruit of Actinidia chinensis, 173
BIOCHEM J. 73-83 (1978).
3 Glace et al., US 4,986,981, Jan. 22, 1991.
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The Examiner finds that Browning compared the “tooth whitening
effect of proteolytic enzymes with 35% hydrogen peroxide or 35% hydrogen
peroxide/sodium hypochlorite” and found that “whitening was highly
significant for both oxidizing agents and proteolytic enzymes. The
proteolytic enzymes tested were papain, bromelain, and ficin.” (Answer 5.)
The Examiner finds that Carne identifies actinidin as a proteolytic enzyme
from Chinese gooseberry or Kiwi fruit (id.). The Examiner finds that Carne
discloses that actinidin is “grouped in the class of plant thiol proteinases,
which includes papain, ficin and bromelain.… Carne teaches that these
enzymes share substantial similarities in chemical and physical properties.”
(Id. at 5-6.)
The Examiner concludes that “it would have been obvious to use
actinidin in a method for whitening teeth since it is a proteolytic enzyme
having substantially similar chemical and physical properties with other
proteolytic enzymes used to whiten teeth” (id. at 6). The Examiner reasons
that the “artisan would have reasonably expected a proteolytic enzyme of the
same class to also be useful for the same purpose” (id.).
Appellant contends that it would not have been obvious to substitute
Carne’s actinidin for the proteases in Browning’s tooth whitening method
because actinidin has a different isoelectric point from the plant thiol
proteases used by Browning, and Carne does not sufficiently characterize the
protease activity of actinidin (Appeal Br. 8-10).
The issue with respect to this rejection is: Does the evidence of
record support the Examiner’s conclusion that it would have been obvious to
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substitute Carne’s actinidin for the plant thiol proteases used in Browning’s
tooth whitening method?
Findings of Fact
1. Browning discloses that “[c]oncern over the potential side effects
of H2O2 tooth whiteners on soft tissues and pulp has led to exploration of
other potential tooth whitening agents, including proteolytic enzymes”
(Browning 1).
2. Browning “compare[s] the tooth whitening effectiveness of 35%
H2O2, or 35% H2O2 + NaClO, 5%, with the proteolytic enzymes papain,
bromelain, and ficin” (id.)
3. Browning discloses that human teeth were “exposed to an
oxidizing agent or a proteolytic enzyme for 30 minutes” (id.)
4. Browning discloses that the “Before/After differences in whiteness
… were highly significant for both oxidizing agents and proteolytic
enzymes” (id.).
5. Browning concludes that its data “suggest that the proteolytic
enzymes tested as whitening agents were statistically no less effective than
the H2O2/NaClO and only slightly less effective than conc. H2O2” (id.).
6. Carne discloses that “[a]ctinidin is a proteolytic enzyme from the
fruit of Actinidia chinensis, the Chinese gooseberry… and is grouped in the
class of plant thiol proteinases.” (Carne 73, right col.)
7. Carne discloses that the class of plant thiol proteinases “includes
papain, ficin and stem bromelain.… There are substantial similarities in the
chemical and physical properties of these enzymes. Papain, ficin and stem
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bromelain have similar sequences about the active site cysteine and histidine
residues, and kinetic studies indicate similar modes of action.” (Id.)
8. Carne discloses that, for this class of proteins, “variations are
found in the amino acid compositions, molecular weights, isoelectric points
and carbohydrate contents.… [A]ctinidin has a mol.wt. of 23 500, compared
with 23 400, 25 500 and 33 500 for papain, ficin and stem bromelain
respectively.” (Id.)
9. Carne discloses that the “isoelectric point of actinidin is 3.1, which
is very different from the values for papain (8.75), ficin (>9) and stem
bromelain (9.55)” (id.).
10. Carne discloses that it “has been suggested that the plant
proteinases form a family of homologous proteins because of their structural
and kinetic similarities” (id.).
Analysis
Claim 1 is directed to a method for whitening teeth by contacting
them with a peroxide-free formulation of actinidin. Browning discloses that
the proteolytic enzymes papain, bromelain, and ficin were effective as tooth
whitening agents. Carne discloses that actinidin is grouped in the same class
of plant thiol proteinases as papain, ficin and stem bromelain. Carne
discloses that these enzymes have substantial similarities in chemical and
physical properties, and that the plant thiol proteinases are thought to form a
family of homologous proteins because of their structural and kinetic
similarities. In view of these disclosures, it would have been obvious to one
of ordinary skill in the art to substitute Carne’s actinidin for the plant thiol
proteases used in Browning’s tooth whitening method because Browning
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discloses that papain, ficin and bromelain are all useful for tooth whitening,
and Carne discloses that actinidin is another member of the same plant thiol
protease family of homologous proteins.
Appellant argues that the Examiner ignored Carne’s disclosure that
the isoelectric point of actinidin is “very different” from that of the other
plant thiol proteases (Appeal Br. 8). Appellant argues that the “difference in
isoelectric point would be expected to affect the activity, solubility and
formulation properties of the enzyme at different pH levels” (id.).
This argument is not persuasive. Although Carne discloses that
actinidin does have a significantly different isoelectric point than papain,
ficin and stem bromelain, Appellant has not pointed to any evidence to show
that this difference would lead a skilled worker to expect actinidin to be
unsuitable for use in Browning’s method. “Attorney’s argument in a brief
cannot take the place of evidence.” In re Pearson, 494 F.2d 1399, 1405
(CCPA 1974). We conclude that, since Carne also discloses that the plant
thiol proteinases make up a family of homologous proteins with structural
and kinetic similarities, it would have been obvious to one of skill in the art
to substitute actinidin for the plant thiol proteases of Browning with a
reasonable expectation of success. Obviousness does not require an absolute
predictability of success, only a reasonable expectation of success. In re
O’Farrell, 853 F.2d 894, 903-04 (Fed. Cir. 1988).
Appellant also argues that Carne “does not characterize the enzymatic
activity of actinidin, except to say it is a thiol protease.… There is no basis
in the references cited to assume that the enzymatic activity of actinidin is
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the same in all relevant respects as that of enzymes of Browning, so that it
might be readily substituted.” (Appeal Br. 9.)
This argument is also unpersuasive. Browning describes papain,
bromelain, and ficin as “proteolytic enzymes” (FF 2). Carne describes
actinidin as a proteolytic enzyme in the same family as papain, stem
bromelain, and ficin (FFs 6, 7, 10). Appellant has pointed to no persuasive
evidence to support the position that any further characterization would have
been necessary in order for a person of ordinary skill in the art to reasonably
expect that actinidin would be useful in Browning’s method.
Conclusion of Law
The evidence of record supports the Examiner’s conclusion that it
would have been obvious to substitute Carne’s actinidin for the plant thiol
proteases used in Browning’s tooth whitening method.
II.
The Examiner has rejected claim 4 under 35 U.S.C. § 103(a) as
obvious in view of Browning, Carne, and Glace. Claim 4 is directed to the
“method of Claim 1, wherein the actinidin-containing preparation also
comprises glycerin at a concentration of at least 20 wt. %.”
The Examiner relies on Browning and Carne as discussed above. The
Examiner finds that Glace discloses “a peroxide-free low abrasion toothpaste
comprising papain (protease)” (Answer 6). The Examiner finds that Glace
discloses that “toothpastes are made up of seven major types of ingredients,
and lists a humectant or moistening system as one of the seven” (id.). The
Examiner finds that Glace discloses that glycerin is “one of the most
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frequently used humectants … Humectants are taught to be used in an
amount of 20-30 percent by weight.” (Id. at 6-7.) The Examiner concludes
that “it would have been obvious to use a humectant glycerin in a method for
whitening teeth since it is a suitable for use in dental compositions, and
recognized as one of seven major ingredients for toothpastes, as taught by
Glace” (id. at 7), and that the “humectant would have been employed to
prevent loss of water from the composition when it is exposed to air, as
taught by Glace.” (id.).
We agree with the Examiner’s findings and conclusion that it would
have been obvious, based on Glace’s disclosure, to include at least 20 wt %
glycerin in the composition used in the method suggested by Browning and
Carne (see Answer 6-7).
Appellant argues that “if Glace were properly reviewed for what it
discloses as a whole, one skilled in the art would learn that Glace teaches
away from using enzymes such as papain unless combined with citric
acid/metal citrate. (See, Glace at col. 3, lines 23 to 25).” (Appeal Br. 11.)
This argument is not persuasive. Appellant points to Glace’s
disclosure that “papain, when used without the citric acid combination, has
no effect whatever on the calcium content of calculus” (Glace, col. 3, ll. 22-
24). However, Glace also teaches that “[e]ven when used without the
citrate, papain has a tendency to dissolve and remove plaque.… [T]his
proteolytic enzyme serves to dissolve the proteinaceous matrix of calculus
that is attached to dentin and enamel.” (Id. at col. 3, ll. 18-22.) Thus, we do
not agree that Glace teaches away from using a protease without citric acid.
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In any event, claim 4 does not exclude the presence of citric acid and metal
citrate components in the recited actinidin-containing preparation.
SUMMARY
We affirm the rejection of claims 1-5 and 7 under 35 U.S.C. § 103(a).
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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