Abstract
Cell wall proteinases from 5 strains of Streptococcus lactis including one S. lactis subsp. diacetylactis were compared and partially characterized. They shared sorne common enzymatic features: only one activity optimum at 30-40°C, at pH 5.5-6 on casein and 4-4.5 on haemoglobin. Crude cell wall extracts from the S. lactis strains were fully inhibited by DFP, but this inhibition was only partial for the S. lactis subsp. diacetylactis strain. Electrophoregrams of as!, {3 and K-casein hydrolysates obtained with the cell-wall extracts of these strains were quite similar for each protein substrate. {3-caseinwas preferentially broken down; as! and K-caseins were hydrolysed to a lesser extent.
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