Comparison of cell wall proteinases from Lactococcus lactis subsp. cremoris AC1 and Lactococcus lactis subsp. lactis NCDO 763 |
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Authors: | V Monnet W Bockelmann J C Gripon M Teuber |
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Institution: | (1) Station de Recherches Laitières, I.N.R.A., F-78350 Jouy en Josas, France;(2) Institut für Mikrobiologie, Bundesanstalt für Milchforschung, D-2300 Kiel, Germany |
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Abstract: | Summary The cell wall proteinases of Lactococcus lactis subsp. lactis NCDO 763 and L. lactis subsp. cremoris AC1 hydrolyse -casein with a similar specificity even though some quantitative differences can be observed for a few degradation products analysed by reverse phase HPLC and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The main peptides soluble in 1.1% trifluoroacetic acid and liberated by the two proteinases were identified and have been found to be the same for the two enzymes. They are located in two areas of the -casein sequence (53–93 and the C-terminal part: 129–209) and they include bitter tasting or physiologically active fragments. No narrow specificity was observed for these proteinases. However, glutamine and serine residues are more frequently encountered in position P1 and P 1 of the sensitive peptide bond and the close environment (position P2 to P4 and P 2 to P 4) of the cleaved bond is mainly hydrophobic. |
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