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Comparison of cell wall proteinases from lactococcus lactis ssp cremoris ac1 and lactococcus lactis ssp lactis ncdo 763 i. purification and action of the enzymes on caseins


Comparison of cell wall proteinases from lactococcus lactis ssp cremoris ac1 and lactococcus lactis ssp lactis ncdo 763 i. purification and action of the enzymes on caseins



Applied Microbiology and Biotechnology 31(3): 278-282



ISSN/ISBN: 0175-7598

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 had an apparent molecular mass of about 145 000 daltons as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Electrophoresis and reversed phase HPLC patterns of hydrolysates of .alpha.s1-, .alpha.s2-, .beta.-, and K-caseins indicated that both proteinases had a similar specificity. The enzyme of L. lactis subsp. lactis split .alpha.s1- and .alpha.s2-caseins more extensively than that of L. lactis subsp. cremoris.

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Accession: 007139118

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