Summary
The cell wall proteinases of Lactococcus lactis subsp. lactis NCDO 763 and L. lactis subsp. cremoris AC1 hydrolyse β-casein with a similar specificity even though some quantitative differences can be observed for a few degradation products analysed by reverse phase HPLC and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The main peptides soluble in 1.1% trifluoroacetic acid and liberated by the two proteinases were identified and have been found to be the same for the two enzymes. They are located in two areas of the β-casein sequence (53–93 and the C-terminal part: 129–209) and they include bitter tasting or physiologically active fragments. No narrow specificity was observed for these proteinases. However, glutamine and serine residues are more frequently encountered in position P1 and P′1 of the sensitive peptide bond and the close environment (position P2 to P4 and P′2 to P′4) of the cleaved bond is mainly hydrophobic.
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Monnet, V., Bockelmann, W., Gripon, J.C. et al. Comparison of cell wall proteinases from Lactococcus lactis subsp. cremoris AC1 and Lactococcus lactis subsp. lactis NCDO 763. Appl Microbiol Biotechnol 31, 112–118 (1989). https://doi.org/10.1007/BF00262446
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DOI: https://doi.org/10.1007/BF00262446