Open AccessSpecificity of a cell wall proteinase from Streptococcus lactis NCDO763 towards bovine β‐casein
Author(s) -
Monnet Véronique,
Bars Dominique,
Gripon JeanClaude
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01681.x
Subject(s) - casein , residue (chemistry) , enzyme , biochemistry , peptide , chemistry , cell wall , peptide hydrolases , substrate (aquarium) , biology , protease , ecology
A cell wall proteinase from Streptococcus lactis liberated, with a molar ratio of enzyme over substrate of approx. 10 −5 , at least 5 peptides from the C‐terminal part of β‐casein. The substrate specificity of the enzyme appears to be low. The occurrence of a hydrophobic residue at position P3 seems to be the only feature common to 4 of the 5 susceptible peptide bonds. The released fragments have features found in peptides producing a bitter taste.