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β-casein f(184-210) [id=CAB0001]

Producer Organism : Native Protein : Production Method :
Human β-casein Enzymatic hydrolysis and Purification with LC method
Activity : Antibacterial
Target Organisms :

Gram-positive: Active against Lactobacillus delbrueckii subsp. bulgaricus B15, Lactobacillus casei subsp. casei 2047, Lactobacillus sanfranciscensis CB1, Lactococcus lactis subsp. cremoris ST7, Bacillus megaterium F6, Listeria innocua DSM 20649, Staphylococcus aureus ATCC 25923 at 100 g/ml.

Gram-negative: Active against Enterococcus faecium X95, Escherichia coli K-12, Salmonella spp, Yersinia enterocolitica X8 at 100 g/ml, Escherichia coli F19 at 50 g/ml.

NOTE: No activity against Lactobacillus helveticus PR4, Lactobacillus plantarum 20B (>100 g/ml) .

Description :
Production method: Lactobacillus helveticus PR4 proteinase hydrolysis and purification with LC method.

Length : 26 Mass (Da): 2 907.31 Common Amino Acids : P
Isolectric Point : 6.5 Net Charge : 1 Absent Amino Acids : CDFGKMRW
Basic Residues : 2 Acidic Residues : 1 Hydrophobic Residues : 9
Polar Residues : 6 Boman Index : -16.18 Hydropathy Index : -0.185
Aliphatic Index : 112.31 Instability Index : 0 Extinction Coefficient : 1490
Absorbance 280nm : 59.6

Wheel representation

Hydrophobicity plot

Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Citation: 1

Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species

Cited Entries: CAB0001

Authors:Minervini, F., Algaron, F., Rizzello, C.G., Fox, P.F., Monnet, V., Gobbetti, M.
Journal: Applied and Environmental Microbiology 2003, 69(9).
Abstract: Sodium caseinates prepared from bovine, sheep, goat, pig, buffalo or human milk were hydrolyzed by a partially purified proteinase of Lactobacillus helveticus PR4. Peptides in each hydrolysate were fractionated by reversed-phase fast-protein liquid chromatography. The fractions which showed the highest angiotensin I-converting-enzyme (ACE)-inhibitory or antibacterial activity were sequenced by mass spectrum and Edman degradation analyses. Various ACE-inhibitory peptides were found in the hydrolysates: the bovine {alpha}S1-casein ({alpha}S1-CN) 24-47 fragment (f24-47), f169-193, and {beta}-CN f58-76; ovine {alpha}S1-CN f1-6 and {alpha}S2-CN f182-185 and f186-188; caprine {beta}-CN f58-65 and {alpha}S

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