Summary
Cell wall-associated proteinases were isolated from Lactococcus lactis subsp. cremoris AC1 and subsp. lactis NCDO 763 in order to compare their specificities towards different caseins. Two purification strategies were applied. Cells grown in casein-free M17 medium were a suitable starting material for purification, since electrophoretic purity could be achieved after one chromatographic step. Both enzymes has an apparent molecular mass of about 145000 daltons as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Electrophoresis and reversed phase HPLC patterns of hydrolysates of αs1-, αs2-, β-, and K-caseins indicated that both proteinases had a similar specificity. The enzyme of L. lactis subsp. lactis split αs1- and αs2-caseins more extensively than that of L. lactis subsp. cremoris.
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Bockelmann, W., Monnet, V., Geis, A. et al. Comparison of cell wall proteinases from Lactococcus lactis subsp. cremoris AC1 and Lactococcus lactis subsp. lactis NCDO 763. Appl Microbiol Biotechnol 31, 278–282 (1989). https://doi.org/10.1007/BF00258409
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DOI: https://doi.org/10.1007/BF00258409