Abstract
The specificity of a cell wall proteinase (PI) from Streptococcus cremoris strain HP in its action on bovine β-casein was determined. To this end an enzymic digest (pH 6.2; 15° C) of β-casein was brought to pH 4.6 and the soluble fraction separated by semi-preparative reversed-phase HPLC. Purified peptides were analyzed by amino acid and end-group analysis. Ten chromatographic components were identified, which together accounted for at least seven cleavage sites all being located in the C-terminal fifty-residue part of β-casein. In five cases it concerned a Gln-X or X-Gln peptide linkage. The specificity of this proteinase from S. cremoris HP shows similarity to that reported for a cell wall proteinase from S. lactis NCDO 763 in its action on β-casein.
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