Action of a cell wall proteinase from Lactococcus lactis subsp. cremoris SK11 on bovine ? s1-casein

1991 ◽  
Vol 35 (2) ◽  
Author(s):  
JulianR. Reid ◽  
ChristopherH. Moore ◽  
GraemeG. Midwinter ◽  
GrahamG. Pritchard
Keyword(s):  
Cell Wall ◽  
Lactococcus Lactis ◽  
Lactococcus Lactis Subsp ◽  
A Cell

scholarly journals Monoclonal Antibodies to the Cell-Wall-Associated Proteinase of Lactococcus lactis subsp. cremoris Wg2

1988 ◽  
Vol 54 (9) ◽  
pp. 2250-2256 ◽  
Author(s):  
Harry Laan ◽  
Eddy J. Smid ◽  
Loe de Leij ◽  
Edwin Schwander ◽  
Wil N. Konings
Keyword(s):  
Cell Wall ◽  
Monoclonal Antibodies ◽  
Lactococcus Lactis ◽  
Lactococcus Lactis Subsp

Action of a cell-envelope proteinase (CEPIII-type) from Lactococcus lactis subsp. cremoris AM1 on bovine κ-casein

1994 ◽  
Vol 41 (6) ◽  
pp. 644-651 ◽  
Author(s):  
S. Visser ◽  
C. J. Slangen ◽  
A. J. P. M. Robben ◽  
W. D. van Dongen ◽  
W. Heerma ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Cell Envelope ◽  
Lactococcus Lactis Subsp ◽  
A Cell

Action of a cell-envelope proteinase (CEPIII-type) from Lactococcus lactis subsp. cremoris AM1 bovine ?-casein

1994 ◽  
Vol 41 (6) ◽  
pp. 644-651 ◽  
Author(s):  
S. Visser ◽  
C. J. Slangen ◽  
A. J. P. M. Robben ◽  
W. D. van Dongen ◽  
W. Heerma ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Cell Envelope ◽  
Lactococcus Lactis Subsp ◽  
A Cell

scholarly journals Autolysis of Lactococcus lactis Is Influenced by Proteolysis

1998 ◽  
Vol 180 (22) ◽  
pp. 5947-5953 ◽  
Author(s):  
Girbe Buist ◽  
Gerard Venema ◽  
Jan Kok
Keyword(s):  
Cell Wall ◽  
Stationary Phase ◽  
Lactococcus Lactis ◽  
Deletion Mutant ◽  
Stationary Phase Culture ◽  
Intracellular Proteins ◽  
Phase Culture ◽  
A Cell ◽  
Zymographic Analysis ◽  
High Level

ABSTRACT The autolysin AcmA of Lactococcus lactis was shown to be degraded by the extracellular lactococcal proteinase PrtP. Autolysis, as evidenced by reduction in optical density of a stationary-phase culture and concomitant release of intracellular proteins, was greatly reduced when L. lactis MG1363 cells expressed the cell wall-anchored lactococcal proteinase PrtP of the PI-type caseinolytic specificity (PI). On the other hand, lactococcal strains that did not produce the proteinase showed a high level of autolysis, which was also observed when the cells produced the secreted form of PI or a cell wall-anchored proteinase with PIII-type specificity. Autolysis was also increased when MG1363 expressed the cell wall-anchored hybrid PI/PIII-type proteinase PIac. Zymographic analysis of AcmA activity during stationary phase showed that AcmA was quickly degraded by PI and much more slowly by PrtP proteinases with PIII-type and intermediate specificities. Autolysis of L. lactis by AcmA was influenced by the specificity, amount, and location of the lactococcal proteinase. No autolysis was observed when the various proteinases were expressed in an L. lactis acmAdeletion mutant, indicating that PrtP itself did not cause lysis of cells. The chain length of a strain was significantly shortened when the strain expressed a cell wall-anchored active proteinase.

Sign in / Sign up

Export Citation Format

Share Document