Comparison of cell wall proteinases from Lactococcus lactis subsp. cremoris AC1 and Lactococcus lactis subsp. lactis NCDO 763.1. Purification and action of the enzymes on caseins
1989
Bockelmann, W. | Monnet, V. | Geis, A. | Teuber, M. | Gripon, J.C. | Federal Dairy Research Centre ; Partenaires INRAE | Institut francilien recherche, innovation et société (IFRIS) ; Institut National de la Recherche Agronomique (INRA)-École des hautes études en sciences sociales (EHESS)-OST-Université Paris-Est Marne-la-Vallée (UPEM)-Ministère de l'Education nationale, de l’Enseignement supérieur et de la Recherche (M.E.N.E.S.R.)-ESIEE Paris-Centre National de la Recherche Scientifique (CNRS)
International audience
Afficher plus [+] Moins [-]anglais. 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 agrs1-, agrs2-, beta-, and K-caseins indicated that both proteinases had a similar specificity. The enzyme of L. lactis subsp. lactis split agrs1- and agrs2-caseins more extensively than that of L. lactis subsp. cremoris.
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