3.4.21.96: Lactocepin

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For detailed information about Lactocepin, go to the full flat file.

Reaction

Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain =

Synonyms

cell envelope associated proteinase, cell envelope proteinase, cell wall anchored proteinase, Cell wall-associated serine proteinase, cell-bound cell envelope proteinase, Cell-envelope proteinase, Cell-envelope-located serine proteinase, Cell-wall-bound proteinase, CEP, Extracellular lactococcal proteinase, Lactocepin, Lactocepin I, lactococcal cell envelope proteinase, Lactococcal cell envelope-associated proteinase, Lactococcal cell wall-associated proteinase, Lactococcal PI-type proteinase, Lactococcal PIII-type poteinase, Lactococcal proteinase, Lactococcal proteinase PI, LP151, PrtH, PrtH2, PrtP, PrtP proteinase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.96 Lactocepin

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Results	in table
373	AA Sequence
10	Application
1	CAS Registry Number
6	Cloned(Commentary)
1	Crystallization (Commentary)
1	General Information
29	Inhibitors
28	Localization
8	Metals/Ions
14	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
76	Organism
7	pH Optimum
3	pH Range
8	Protein Variants
6	Purification (Commentary)
1	Reaction
1	Reaction Type
50	Reference
2	Specific Activity [micromol/min/mg]
1	Storage Stability
155	Substrates and Products (Substrate)
16	Subunits
41	Synonyms
5	Temperature Optimum [°C]
1	Temperature Range [°C]
5	Temperature Stability [°C]

Application

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Application on EC 3.4.21.96 - Lactocepin

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

biotechnology

Lactococcus lactis

Q49SG9, Q49SH0

conversion of lactocepin substrate binding regions by allele exchange can effectively alter lactocepin specificity in industrial strains of Lactococcus lactis without significantly affecting other important strain properties. The methodology can be used to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect

665338

food industry

2 entries

industry

2 entries

nutrition

Lactococcus lactis

-

cheese making, cheese starter organism, dairy industry

29890, 649355

synthesis

2 entries

additional information

Lactococcus lactis subsp. cremoris MG1363

-

exposure of PrtP, and not its proteolytic activity, is responsible for greater cell hydrophobicity and adhesion. The increased bacterial affinity to polar and apolar solvents indicates that exposure of PrtP on lactococcal cell surface can enhance the capacity to exchange attractive van der Waals interactions, and consequently increase their adhesion to different types of solid surfaces and solvents. PrtP or its derivatives may be used as a tool to construct strains with increased adhesion that form protective biofilms

685827

food industry

Lactobacillus helveticus

-

CEP isolated from Mongolian fermented mare's milk strain SBT11087 is distinct from those from previously reported Lactobacillus helveticus strains in terms of its optimal temperature and its degradation of beta-casein

753888

food industry

Lactobacillus helveticus SBT11087

-

CEP isolated from Mongolian fermented mare's milk strain SBT11087 is distinct from those from previously reported Lactobacillus helveticus strains in terms of its optimal temperature and its degradation of beta-casein

-

industry

Lactococcus lactis

Q49SG9, Q49SH0

method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate

665338

industry

Lactococcus lactis s4

-

method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate

-

synthesis

Lactobacillus acidophilus

-

optimisation of enzymatic hydrolysis of beta-casein to produce the angiotensin-I-converting enzyme (ACE) inhibitory peptides. Under optimal conditions (enzyme-to-substrate ([E]/[S]) ratio (w/w) of 0.132 and pH of 8.00 at 38.8°C), the ACE inhibitory activity of hydrolysates is 72.06% and the total peptides is 11.75 mg/ml. The resulting hydrolysates have higher thermal stability than beta-casein and show an increase in the free sulfhydryl content compared with raw beta-casein

753892

synthesis

Lactobacillus acidophilus JQ-1

-

optimisation of enzymatic hydrolysis of beta-casein to produce the angiotensin-I-converting enzyme (ACE) inhibitory peptides. Under optimal conditions (enzyme-to-substrate ([E]/[S]) ratio (w/w) of 0.132 and pH of 8.00 at 38.8°C), the ACE inhibitory activity of hydrolysates is 72.06% and the total peptides is 11.75 mg/ml. The resulting hydrolysates have higher thermal stability than beta-casein and show an increase in the free sulfhydryl content compared with raw beta-casein

-