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Subject:
From:
"Valerie W. McClain" <[log in to unmask]>
Reply To:
Lactation Information and Discussion <[log in to unmask]>
Date:
Tue, 19 Aug 2003 16:40:10 EDT
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In search of more information on comfort proteins I ran across this patent
from Nestec SA (Nestle) called "Purified proteolytic enzyme and method of
purification," with the inventor being Braun et al. and filed in 1998. Note the
mention of toxic side effects of the inflammatory type in breastfeeding infants.
What does that mean? Does Nestle breakdown products in infant formula
particularly effect breastfeeding infants?  Is this situation resolved?
Valerie W. McClain, IBCLC

patent # 6420156

"Trypsin is commonly used in the manufacture of protein hydrolysates intended
in particular to enter into the composition of infant products. To
incorporate the protein portion into a finished product, for example an infant milk, any
residual lipolytic enzymatic activity resulting from the protein hydrolysate
must be removed. This is necessary in order to avoid the appearance of
products of degradation of lecithin which is added to the final formula for
technological reasons, for example to enhance the wettability of powders, into
lysolecithin, in particular during storage. Such breakdown products may manifest
themselves both in liquid products and in powders by the appearance of stability or
organoleptic defects, for example spots, poor taste, or by their toxicity
leading to side effects, for example of an inflammatory type in breastfeeding
infants.

However, it is the case that the complete removal of phospholipases in
particular is difficult to achieve. The complete purification of proteases generally
requires various precipitation steps, chromatographic separations, heat
treatments under well-defined conditions or chemical inactivations. The complete
removal of phospholipase A.sub.2, which is very heat-resistant, requires a
prolonged heat treatment which unfortunately also affects the protease."

The aim of the invention is the preparation of a purified protease whose
proteolytic activity is quantitatively and qualitatively preserved, but which is
free of lipolytic activity, in particular of phospholipase A.sub.2, by a simple
and inexpensive method.

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