αs1-casein f(114-124) [id=CAA0005]

Synonym: Cp1

Producer Organism : Native Protein : Production Method :
Cow αs1-casein Enzymatic hydrolysis and Purification with LC method/Synthetic
Activity : Antibacterial
Target Organisms :

Gram-positive: Bacillus subtilis FSAW 0320 (MIC=125 g/ml), Listeria innocua FSAW 2305 (MIC=125 g/ml), Listeria monocytogenes FSAW 2310 (MIC=125 g/ml), Listeria monocytogenes NCTC 11994 (MIC=125 g/ml).

Gram-negative: Citrobacter freundii FSAW 0801 (MIC=500 g/ml), Escherichia coli NCTC 8196 (MIC=250 g/ml), Salmonella enteritidis FSAW 3420 (MIC=250 g/ml), Salmonella typhimurium FSAW 3412 (MIC=125 g/ml).

NOTE: No activity against Enterobacter aerogenes NCTC 10006 (>1000 g/ml) .

Description :
Production method: Pepsin hydrolysis and purification with LC method/Synthetic.

Length : 11 Mass (Da): 1 386.12 Common Amino Acids : KL
Isolectric Point : 11.13 Net Charge : 4 Absent Amino Acids : ACDEFGHIMNSTW
Basic Residues : 4 Acidic Residues : 0 Hydrophobic Residues : 4
Polar Residues : 1 Boman Index : -18.45 Hydropathy Index : -0.636
Aliphatic Index : 132.73 Instability Index : 0 Extinction Coefficient : 1490
Absorbance 280nm : 149

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

Isolation and characterisation of a novel antibacterial peptide from bovine alphaS1-casein

Cited Entries: CAA0005, CAA0020, CAA0039, CAA0040, CAA0041

Authors:McCann, K.B., Shiell, B.J., Michalski, W.P., Lee, A., Wan, J., Roginski, H., Coventry, M.J.
Journal: International Dairy Journal 2006, 16(4).
CrossRef External Link
Abstract: Bovine casein was hydrolysed with a range of proteolytic enzymes including pepsin, trypsin, α-chymotrypsin and β-chymotrypsin, and assessed for antibacterial activity. The pepsin digest of bovine casein, which showed antibacterial activity, was fractionated using reverse phase high performance liquid chromatography and the antibacterial peptides isolated were characterised using electrospray ionisation mass spectrometry. Two antibacterial peptides were identified, a novel peptide (Cp1) which corresponded to residues 99109 of bovine αS1-casein and a previously reported peptide (Cp2) which corresponded to residues 183207 of bovine αS2-casein. The minimum inhibitory concentration (MIC) of Cp1 and Cp2 were determined against a range of bacterial cultures. Cp1 exhibited an MIC of 125 μg mL−1 against all Gram-positive bacteria tested, and MIC ranging between 125 and >1000 μg mL−1 against the Gram-negative bacteria tested. Cp2 was generally far more potent against the Gram-positive bacteria, exhibiting an MIC of 21 μg mL−1, compared to MICs ranging from 332 to >664 μg mL−1 against most of the Gram-negative bacteria tested.
Keywords: Antibacterial peptides; Bovine casein

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