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alpha(S1)-casein + H2O
?
-
-
-
?
alpha-lactalbumin + H2O
?
alpha1-casein + H2O
Fragments of alpha1-casein
-
-
-
-
?
alpha1-casein + H2O
fragments of alphas1-casein
-
-
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
beta-Casein + H2O
Fragments of beta-casein
beta-lactoglobulin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
casein + H2O
hydrolyzed casein
Insulin B-chain + H2O
Fragments of insulin B-chain
-
-
-
?
kappa-Casein + H2O
Fragemnts of kappa-casein
-
-
-
-
?
kappa-casein + H2O
fragments of kappa-casein
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
synthetic substrate
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
Suc-Ala-Glu-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
Succinyl-Ala-Glu-Pro-Phe 4-nitroanilide + H2O
?
Succinyl-Ala-Gly-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-His-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ile-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Leu-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Lys-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Phe-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Trp-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
additional information
?
-
alpha-lactalbumin + H2O
?
-
-
-
-
?
alpha-lactalbumin + H2O
?
-
-
-
-
?
alpha1-casein + H2O
?
-
-
-
-
?
alpha1-casein + H2O
?
-
-
-
-
?
alphas1-casein + H2O
?
-
-
-
-
?
alphas1-casein + H2O
?
-
-
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
specificity of the enzyme for the Arg22-Phe23 bond
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
specificity of the enzyme for the Arg22-Phe23 bond
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
-
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
-
the product spectrum depends on water activity and salt concentration
?
alphas1-Casein + H2O
Fragments of alphas1-casein
-
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
specificity of the enzyme for Lys3-His4 bond
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
specificity of the enzyme for Lys3-His4 bond
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the wild-type enzyme of strain SK11, cleaves bonds 16-17 and 17-18, the mutant enzyme lacking the loop 238-388 is highly specific for bond 21-22
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
PI-type proteinase of subsp. cremoris strain HP cleaves the bonds 8-9, 9-10, 13-14, the PIII- type proteinase of subsp. cremoris strain AM1 cleaves bonds 16-17, 17-18, 21-22
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the wild-type enzyme of strain SK11, cleaves bonds 16-17 and 17-18, the mutant enzyme lacking the loop 238-388 is highly specific for bond 21-22
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
preferred substrate
-
-
?
beta-casein + H2O
?
-
preferred substrate
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
shows proteolytic activity only under in vivo conditions
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
-
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
-
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
-
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
-
subsp. lactis MG611, more than 100 different fragments
?
beta-Casein + H2O
Fragments of beta-casein
-
PIII-type proteinase of subsp. cremoris AM1 preferentially cleaves 16 peptide bonds, the cleavage sites are primarily Gln-X or Glu-X, mostly a large hydrophobic residue is part of the cleavable position, a hydrophobic residue is frequently at position P2, sometimes also at P2', one or more side chains in P2-P3 or P2'-P3' are negetively charged
-
-
?
beta-Casein + H2O
Fragments of beta-casein
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
nitrogen nutrition mechanism of lactic streptococci, process in cheese ripening
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
hydrolysis of alpha-s1-, beta- and kappa-casein, alpha-s1-casein which is normally resistant to lactocepin I activity is rapidly hydrolyzed in presence of polyethylene glycol 20000
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
kappa-casein + H2O
fragments of kappa-casein
-
specificity of the enzyme for Phe105-Met106 bond
-
-
?
kappa-casein + H2O
fragments of kappa-casein
-
specificity of the enzyme for Phe105-Met106 bond
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
synthetic substrate
-
-
?
Succinyl-Ala-Glu-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Glu-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Usp 45 + H2O
?
-
a secreted 60 kDa protein of Lactococcus lactis
-
-
?
Usp 45 + H2O
?
-
a secreted 60 kDa protein of Lactococcus lactis
-
-
?
additional information
?
-
-
no substrate: Leu-4-nitroanilide
-
-
?
additional information
?
-
-
no substrate: Leu-4-nitroanilide
-
-
?
additional information
?
-
-
proline is the preferred residue at the cleavage site. No substrate: kappa-casein
-
-
?
additional information
?
-
-
proline is the preferred residue at the cleavage site. No substrate: kappa-casein
-
-
?
additional information
?
-
-
overview, specificity of wild-type SK11 proteinase and its mutants as compared to strain Wg2
-
-
?
additional information
?
-
-
subsp. lactis NCDO 763 prefers hydrophilic amino acids in P4, proline in P2 and hydrophilic amino acids in P1
-
-
?
additional information
?
-
-
subsp. lactis NCDO 763 prefers hydrophilic amino acids in P4, proline in P2 and hydrophilic amino acids in P1
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
PI-type proteinase hydrolyzes beta- casein and kappa-casein, PIII-type proteinase hydrolyzes beta-casein and kappa-caein with different bond-specificities and alpahs1-casein
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
overview, specificity of wild-type SK11 proteinase and its mutants as compared to strain Wg2
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
?
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions
-
-
?
additional information
?
-
-
the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
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Monnet, V.; Ley, J.P.; Gonzalez, S.
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Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase
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Structural changes and interactions involved in the Ca(2+)-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11
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66
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Reid, J.R.; Coolbear, T.
Lactocepin: the cell envelope-associated endopeptidase of lactococci
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2
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Broadbent, J.R.; Rodriguez, B.T.; Joseph, P.; Smith, E.A.; Steele, J.L.
Conversion of Lactococcus lactis cell envelope proteinase specificity by partial allele exchange
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100
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Lactococcus lactis, Lactococcus lactis (Q49SG9), Lactococcus lactis (Q49SH0), Lactococcus lactis s4
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Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci
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7
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Lactococcus lactis subsp. cremoris MG1363
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Pastar, I.; Fira, D.; Strahinic, I.; Krstic, K.; Begovic, J.; Topisirovic, L.; Jovanovic, G.
Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus
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51
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Lacticaseibacillus rhamnosus
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Scolari, G.; Vescovo, M.; Zacconi, C.; Vescovi, F.
Extraction and partial characterization of proteolytic activities from the cell surface of Lactobacillus helveticus Zuc2
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Hebert, E.M.; Mamone, G.; Picariello, G.; Raya, R.R.; Savoy, G.; Ferranti, P.; Addeo, F.
Characterization of the pattern of alphas1- and beta-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581
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Lactobacillus delbrueckii
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Capone, R.; Wang, H.T.; Ning, Y.; Sweier, D.G.; Lopatin, D.E.; Fenno, J.C.
Human serum antibodies recognize Treponema denticola Msp and PrtP protease complex proteins
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23
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Sadat-Mekmene, L.; Jardin, J.; Corre, C.; Moll, D.; Richoux, R.; Delage, M.; Lortal, S.; Gagnaire, V.
Simultaneous presence of PrtH and PrtH2 proteinases in Lactobacillus helveticus strains improves breakdown of the pure alphas1-casein
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Lactobacillus helveticus
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Vukotic, G.; Mirkovic, N.; Jovcic, B.; Miljkovic, M.; Strahinic, I.; Fira, D.; Radulovic, Z.; Kojic, M.
Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation
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Classification of Lactococcus lactis cell envelope proteinase based on gene sequencing, peptides formed after hydrolysis of milk, and computer modeling
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Lactococcus lactis
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Worsztynowicz, P.; Schmidt, A.O.; Bia?as, W.; Grajek, W.
Identification and partial characterization of proteolytic activity of Enterococcus faecalis relevant to their application in dairy industry
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Enterococcus faecalis, Enterococcus faecalis 2/28
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Miyamoto, M.; Ueno, H.M.; Watanabe, M.; Tatsuma, Y.; Seto, Y.; Miyamoto, T.; Nakajima, H.
Distinctive proteolytic activity of cell envelope proteinase of Lactobacillus helveticus isolated from airag, a traditional Mongolian fermented mares milk
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Lactobacillus helveticus, Lactobacillus helveticus SBT11087
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Ren, X.; Pan, D.; Wu, Z.; Zeng, X.; Sun, Y.; Cao, J.; Guo, Y.
Limited hydrolysis of beta-casein by cell wall proteinase and its effect on hydrolysatess conformational and structural properties
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Lactobacillus acidophilus, Lactobacillus acidophilus JQ-1
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Guo, T.; Ouyang, X.; Xin, Y.; Wang, Y.; Zhang, S.; Kong, J.
Characterization of a new cell envelope proteinase PrtP from Lactobacillus rhamnosus CGMCC11055
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Lacticaseibacillus rhamnosus, Lacticaseibacillus rhamnosus CGMCC11055
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