Variation in caseinolytic properties of six cheese related Lactobacillus helveticus strains

A large degree of strain variation was observed in caseinolytic properties of six cheese related Lactobacillus helveticus strains. Activity on intact αs1- and β-casein was observed only after growth in milk and not in MRS. Totally 27 peptides from αs1- and 22 from β-casein were identified from MS/MS fragmentation patterns. All six strains released peptides from the amino end of αs1-casein, and the bonds Ile6-Lys7 and Gln9-Gly10 were identified as primary cleavage sites. Strain variation in the activity on intact β-casein was observed and five of the six strains released peptides from the C-terminal region. The strains had very different activities and some strains had only trace activities. L. helveticus CNRZ 32 had the highest activity towards αs1-casein while L. helveticus LHC2 had the highest activity towards β-casein, and these two strains also produced unique peptides from both αs1- and β-casein.