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Summary - Growth rates and acid production of the most common dairy-related bifidobacteria (Bifidobacterium infantis, B breve and B longum) were determined in the presence of casein hydrolyzates produced by the action of three proteolytic enzymes (alcalase, chymotrypsin and trypsin). Casein hydrolyzates were fractionated with a two-step ultrafiltration process to study the effect of molecular mass of peptides on bifidobacterial growth. The retentate of the second ultrafiltration (nominal molecular eut-off of membranes was 1000 Da) was called mixture of polypeptides (MP) and the permeate fraction which was mainly composed of free amino acids and small peptides was called AA. These hydrolyzate fractions were characterized by a very different concentration of some amino acids (glu, tyr, phe). Among MP and AA casein fractions, trypsin MP fraction at a final concentration of 2% in synthetic medium (Garches medium) exhibited a higher growth-promoting activity on the three bifidobacterial species tested. However, addition of alcalase AA fraction at a final concentration of 1 or 2% repressed the growth and acid production of B breve and B longum.

Comparison of bifidobacterial growth-promoting activity of ultrafiltered casein hydrolyzate fractions