Casein hydrolysis
If standard enzymes are used to cleave the
milk protein casein, then this creates dissolvable oligopeptides with a bitter
taste. Exoproteases detach the first amino acids from a peptide chain, one at
a time. Also, these free amino acids are bitter and, what is more, unstable.
Endopeptidases
DSM used only endopeptidases and a new patented
endoprotease with a ‘preference’ for the amino acid proline. This specifically
cuts the bitter peptides into pieces which are not bitter anymore. The
resulting di- and tripeptides are constructed from two or three amino acids,
are water soluble and no longer bitter. In this way the unique PeptoPro®
production process ensures that no single amino acids are formed and,
equally important, that the bitter
peptides are removed! In addition, di- and tripeptides do not cause any
allergic reactions.
Di-& tripeptides
Beside all their practical advantages, di-
and tripeptides can be used much faster by the organism. The proteins are,
after all, already split up and can be absorbed by the body without further
ado. Also they do not lie in your stomach like a brick, which means that
PeptoPro® can also be taken before or during a
sports performance.