Appeal No. 2005-1745
Application No. 09/161,680
We have carefully reviewed the sections of the specification relied upon by the
appellants and find that page 4, lines 7-13, as originally filed, state, in relevant part, that
It is possible in principle for the substrate specificity of all enzymes to be altered,
and preferably the substrate specificity of hydrolases is altered in the novel
method. Hydrolases form the 3rd class of enzyme (= 3 . . ) in the IUB
nomenclature system. Hydrolases are preferred in the novel method because, as
a rule, a simple detection reaction for them exists and, in many cases they are
used in industrial syntheses.
We further find that Example 2, on pages 11-12, describes the assay used to
determine esterase activity. In this regard, the specification simply states that “[t]he
esterase activity has been reported in units, where one unit (= U) is defined as the
amount of enzyme which produces 1 :mol of acetic acid per minute under the assay
conditions.” Specification, p. 11, line 46- p. 12, line 2. Contrary to the appellants’
argument, we do not find that either of the aforementioned sections of the specification,
as originally filed, describe a method of generating an enzyme having new catalytic
activity which “is within the same International Union of Biochemistry class as the
enzyme’s original catalytic activity.” Thus, we agree with the examiner that the addition
of this phrase to claims 24-27 constitutes new matter.
Accordingly, Rejection IV is affirmed.
V. New Ground of Rejection
Pursuant to 37 C.F.R. § 41.50(b), we set forth the following new grounds of
rejection.
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