Appeal No. 1997-3537
Application No. 08/395,867
explicitly states that trypsin "leaves much of the ABBOS sequence intact" (p. 306, c. 2).
Second, Thibault explicitly states that albumin is "hydrolysable with the most difficulty by the
enzyme system adopted," and explicitly states that serum albumin and immunoglobulins
are the principal "residual proteins" left by the described trypsin/chymotrypsin enzyme
system (c. 7, ll. 23-26). Similarly, Martinez describes an "optional preliminary step prior to
hydrolysis ... [of] preheating of the protein solution to insure denaturation of whey protein
fractions, e.g., serum albumin (BSA) and immunoglobulins (particularly IgG)" (c. 3, ll. 25-
28). Thus, Martinez also suggests that the disclosed trypsin/chymotrypsin enzyme system
may not be effective to hydrolyze BSA. Third, while Martinez states that its hydrolysate "is
preferably devoid of detectable intact milk protein" (c. 4, ll. 18-20), the examiner has not
established on this record that the loss of "detectable intact milk protein" necessarily
means that the milk proteins have been hydrolyzed, i.e., cleaved, as opposed to denatured
such that their quaternary structure is simply unfolded somewhat. Thus, it is unclear on this
record that the enzymatic hydrolysis steps of Thibault or Martinez will inherently result in the
claimed invention. In other words, the examiner has not established a factual basis upon
which to conclude that the trypsin/chymotrypsin hydrolysis method and resulting hydrolysate
of Thibault or Martinez would reasonably be expected to hydrolyze BSA, in particular its
ABBOS sequence so as to result necessarily in the claimed invention.
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