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264 IV.Resultados y discusión. Capítulo III
presented in Table 2. As can be observed, the main soluble peptides in the
fermented milks were constituted by peptides with Mw lower than 400 Da
(Table 1) together with the highest Mw fraction (from 15 to 8 kDa).
Scarce differences were found between the peptide profiles of the labmade
and commercial samples. Nevertheless, the amount of peptides with
Mw < 400 Da was significantly greater (p < 0.05) in the almond commercial
milks (Table 2). All fermented samples presented similar proteolytic
patterns as reported by Papadimitriou et al. (2007), when working with goat
yoghurts obtained with different starters. However, the use of the different
strains in the fermentation process led to the generation of quantitative
differences in the almond protein fractions as can be seen in Table 2; major
differences were found when using the R strain, which produced a greater
release of small peptides (Mw < 400 Da), but only when the commercial
milk was used as a fermentative matrix. These results suggest that R strain is
able to produce a larger amount of peptides with Mw lower than 400 Da
than G strain, which is coherent with their more intense proteolytic activity
(Table 1).
The percentage of water-soluble peptides found in the fermented
almond milks after the in vitro SGID as a function of their molecular weight
(Mw) is presented in Table 3. For comparison purposes, the SGID nonfermented
almond milk (AM) was also analysed. The in vitro digestion
process of fermented samples led to the disappearance of the major part of
the high Mw peptide fraction (from 15 to 8 kDa) and to the generation of
greater amount of low Mw peptides (< 2.5 kDa), which capability to exert
inflammatory effect has never been evaluated.