Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine ?-casein

1991 ◽  
Vol 35 (4) ◽  
Author(s):  
Servaas Visser ◽  
ArjanJ.P.M. Robben ◽  
CharlesJ. Slangen
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 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 Specificity of two genetically related cell-envelope proteinases of Lactococcus lactis subsp. cremoris towards αs1-casein-(1–23)-fragment

1991 ◽  
Vol 273 (1) ◽  
pp. 135-139 ◽  
Author(s):  
F A Exterkate ◽  
A C Alting ◽  
C J Slangen
Keyword(s):  
Lactococcus Lactis ◽  
Hydrophobic Interaction ◽  
Cell Envelope ◽  
Sequence Similarity ◽  
Cleavage Sites ◽  
Hydrogen Bond Formation ◽  
Lactococcus Lactis Subsp ◽  
Related Cell ◽  
Close Sequence ◽  
Low Ionic Strength

The specificity of two genetically related cell-envelope serine proteinases (PI-type and PIII-type) of Lactococcus lactis subsp. cremoris towards the alpha s1-casein-(1-23)-fragment, an important intermediate product of primary chymosin-directed proteolysis in cheese, has been established. Both enzymes showed, at pH 6.5 and under relatively low-ionic-strength conditions, a characteristic, mutually different, cleavage pattern that seems, in the first instance, to be determined by the charge N-terminal to the cleaved bond. With Pi, three cleavage sites were found in the N-terminal positively charged part of the peptide and, with PIII, three sites were found in the C-terminal negatively charged part. Comparison of the specific cleavage sites in this peptide and those in β-casein revealed similarities with respect to the different residues which can occur N-terminally to the cleaved bond. The properties of these substrate residues match with the structural and various interactive features of the respective binding regions of the enzymes predicted on the basis of a close sequence similarity of the lactococcal proteinases with the subtilisin family. A hydrophobic interaction and/or hydrogen-bridge formation seems to govern the binding of the first amino acid residue N-terminal to the scissile bond. The more distantly N-terminally positioned sequence of residues apparently is attracted electrostatically by a negative charge in the binding region of PI and by a positive charge in that of PIII, provided that the opposite charge is is present at the appropriate position in this sequence. Hence a specific electrostatic binding may occur; additionally, hydrophobic interaction and/or hydrogen-bond formation is important.

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
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