Abstract
A large degree of strain variation was observed in caseinolytic properties of six cheese related Lactobacillus helveticus strains. Activity on intact α s1- and β-casein was observed only after growth in milk and not in MRS. Totally 27 peptides from α s1- and 22 from β-casein were identified from MS/MS fragmentation patterns. All six strains released peptides from the amino end of α s1-casein, and the bonds Ile 6-Lys 7 and Gln 9-Gly 10 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 α s1-casein while L. helveticus LHC2 had the highest activity towards β-casein, and these two strains also produced unique peptides from both α s1- and β-casein.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
