Summary
A cell wall-associated, β-casein specific protease and a peptidase were purified simulta-neously fromStreptococcus cremoris AC1. The molecular weights are 145,000 daltons for the pro-tease and 36,000 for the peptidase. The protease has a pH optimum at 5.5-6 and a temperature optimum at 40° C. It is activated by 1 mM of Ca++ but severely inhibited by higher Ca++ concentrations. Further inhibitor studies indicate that the protease is probably a serin protease. The peptidase shows aminopeptidase activity and most effectively hydrolyses L-lysyl-p-nitroanilide, and to a lesser extent IMeucyl-, L-alanyl- and L-alanyl-L-alanyl-p-nitroanilide. No endopeptidase activity could be detected. The peptidase is irreversibly inhibited by EDTA.
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Geis, A., Bockelmann, W. & Teuber, M. Simultaneous extraction and purification of a cell wall-associated peptidase and β-casein specific proteas fromStreptococcus cremoris AC1. Appl Microbiol Biotechnol 23, 79–84 (1985). https://doi.org/10.1007/BF02660123
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DOI: https://doi.org/10.1007/BF02660123