Involvement of enzyme-substrate charge interactions in the caseinolytic specificity of lactococcal cell envelope-associated proteinases

The nature of interaction between lactococcal cell envelope-associated proteinase (CEP) and caseins during hydrolysis of kappa-casein is complex. Oligopeptides with amino acid sequences similar to the sequence from residue 98 to 111 and from 153 to 169 of kappa-resin exhibited different susceptibilities to P(sub I) and P(sub III) lactococcal proteinases.