αs2-casein f(179-222) or f(164-207) [id=CAA0014]

Synonym: Cr5/Cr6

Producer Organism : Native Protein : Production Method :
Cow αs2-casein Enzymatic hydrolysis and Purification with LC method
Activity : Antibacterial
Target Organisms :

Gram-positive: Bacillus subtilis FSAW 0320 (MIC=4.8 g/ml), Listeria innocua FSAW 2305 (MIC=4.8 g/ml), Listeria monocytogenes FSAW 2310 (MIC=4.8 g/ml).

NOTE: No activity against Escherichia coli NCTC 8196 (>76.2 M) .

Description :
Production method: Chymosin hydrolysis and purification with LC method.

Length : 44 Mass (Da): 5 453.52 Common Amino Acids : K
Isolectric Point : 10.93 Net Charge : 11 Absent Amino Acids : CDEGN
Basic Residues : 11 Acidic Residues : 0 Hydrophobic Residues : 14
Polar Residues : 8 Boman Index : -63.54 Hydropathy Index : -0.7
Aliphatic Index : 86.36 Instability Index : 0 Extinction Coefficient : 12950
Absorbance 280nm : 301.16

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.

Multiple Sequence Alignment (MSA)

 2 CAA0020   100.0%  ---------------------------------VYQHQKAMKPWIQPKTKVIPYVRYL 
 3 CAA0021   100.0%  ---------------------------------VYQHQKAMKPWIQPKTKVIPYVRYL 
 4 CAA0019   100.0%  -------------------------------KTVYQHQKAMKPWIQPKTKVIPYVRYL 
 5 CAA0018   100.0%  ------------------------------LKTVYQHQKAMKPWIQPKTKVIPYVRYL 
 6 CAA0017   100.0%  -------------------------ALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL 
 7 CAA0015   100.0%  ----------------------QKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL 
 9 CAA0009   100.0%  --------KNRLNFLKKISQRYQKFALPQYLKTVYQHQK------------------- 

10 CAA0013   100.0%  --------------LKKISQRYQKFALPQY---------------------------- 

11 CAA0008   100.0%  --------KNRLNFLKKISQRYQ----------------------------------- 




15 CAA0012   100.0%  --------------------RYQKFALPQYLKTVYQHQK------------------- 

16 CAA0016   100.0%  ------------------------FALPQYLK-------------------------- 

Citation: 1

Isolation and characterisation of antibacterial peptides derived from the f(164-207) region of bovine alphaS2-casein

Cited Entries: LFB0086, CAA0014, CAA0015, CAA0017, CAA0018, CAA0019

Authors:McCann, K.B., Shiell, B.J., Michalski, W.P., Lee, A., Wan, J., Roginski, H., Coventry, M.J.
Journal: International Dairy Journal 2005, 15(2).
CrossRef External Link
Abstract: A chymosin digest of sodium caseinate, which showed antibacterial activity against Listeria innocua, was fractionated using reverse phase high performance liquid chromatography and the purified antibacterial peptides were characterised by mass spectrometry, N-terminal amino acid sequencing and comparison to peptide masses of theoretical enzymic digests of milk proteins. Five antibacterial peptides, Cr1, Cr3, Cr4, Cr5 and Cr7 corresponding to amino acid residues 181207, 180207, 175207, 164207 and 172207 of bovine αS2-casein, respectively, were isolated. The minimal inhibitory concentration of peptides Cr1, Cr4 and Cr5 was determined against a range of Gram-positive and Gram-negative bacteria and showed similar activities to those of the bacteriocin peptide, nisin and the antibacterial peptide, lactoferricin B against certain Gram-positive bacteria. A partially purified chymosin digest of sodium caseinate (CrMIX) was prepared and observed to be heat stable for up to 15 min on exposure to 121 C. Although CrMIX showed bactericidal activity against Salmonella Typhimurium in 0.1% (w/v) peptone medium, no antibacterial activity was observed when tested in skim milk at the same concentration.
Keywords: Antibacterial; Peptide; [alpha]s2-Casein

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