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αs2-casein f(196-222) or f(181-207) [id=CAA0019]

Synonym: Cr1

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=21 g/ml), Listeria innocua FSAW 2305 (MIC=21 g/ml), Listeria monocytogenes FSAW 2310 (MIC=21 g/ml).

Gram-negative: Salmonella typhimurium FSAW 3412 (MIC=21 g/ml).

NOTE: No activity against Bacillus cereus FSAW 0303, Salmonella enteritidis FSAW 3420 (>64 g/ml), Escherichia coli NCTC 8196 (>128 g/ml) .

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

Length : 27 Mass (Da): 3 346.05 Common Amino Acids : K
Isolectric Point : 10.8 Net Charge : 7 Absent Amino Acids : CDEFGNS
Basic Residues : 7 Acidic Residues : 0 Hydrophobic Residues : 8
Polar Residues : 5 Boman Index : -36.14 Hydropathy Index : -0.726
Aliphatic Index : 79.26 Instability Index : 0 Extinction Coefficient : 9970
Absorbance 280nm : 383.46

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)


 1 CAANATIVE 100.0%  KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL 
 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 
 8 CAA0014   100.0%  --------------LKKISQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL 
 9 CAA0009   100.0%  --------KNRLNFLKKISQRYQKFALPQYLKTVYQHQK------------------- 

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

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

12 CAA0010   100.0%  KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK------------------- 

13 CAA0011   100.0%  KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK------------------- 

14 CAA0007    97.4%  -TKITEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK------------------- 

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

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

Citation: 1

Identification of two distinct antibacterial domains within the sequence of bovine alphas2-casein

Cited Entries: CAA0013, CAA0019, CAA0020

Authors:Recio, I., Visser, S.
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects 1999, 1428(2-3).
CrossRef External Link
Abstract: Two distinct domains with antibacterial activity were isolated from a peptic hydrolysate of bovine αs2-casein. The digested αs2-casein was fractionated by cation-exchange chromatography, after which the peptides in the two active fractions obtained were separated by high-performance liquid chromatography and sequenced by electrospray-ionization tandem mass spectrometry. The major component in each active fraction, f(183207) and f(164179), was further purified and the antibacterial activity of these components was tested against several microorganisms. Depending on the target bacterial strain, these peptides exhibited minimum inhibitory concentrations between 8 and 99 μM. Peptide f(183207) exhibited a consistently higher antibacterial activity than f(164179), although both peptides showed a comparable hemolytic effect. A method of in situ enzymatic hydrolysis on a cation-exchange membrane to obtain a fraction enriched in the most active antibacterial domain is presented. The antibacterial and hemolytic activities are discussed in relation to the structure and hydrophobicity of the peptides.
Keywords: Antibacterial peptide; [alpha]s2-Casein; Electrospray mass spectrometry; Hydrolysis of membrane-bound protein
Citation: 2

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
Citation: 3

Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin: In situ enzymatic hydrolysis on an ion-exchange membrane

Cited Entries: LFB0006, LFB0010, LFB0085, LFB0092, LFB0147, LFB0148, LFB0151, CAA0013, CAA0019, CAA0020

Authors:Recio, I., Visser, S.
Journal: Journal of Chromatography A 1999, 831(2).
CrossRef External Link
Abstract: Two ion-exchange chromatographic methods are reported for the rapid isolation of antibacterial peptides from lactoferrin (LF). Using the first method, a pepsin hydrolysate of LF was fractionated by bead-based cation-exchange chromatography. After removal of weakly bound material by washing with ammonia, highly purified lactoferricin-B (LFcin-B) was obtained in a single step by elution with 2 M NaCl. Some other cationic peptides, copurified as minor components, were also characterised by N-terminal sequencing, mass spectrometry and antibacterial activity determination. With the second method, cheese whey was filtered through a cation-exchange membrane, and the selectively bound LF was directly hydrolysed in situ with pepsin. Inactive LF fragments were washed off the membrane with ammonia, and a fraction enriched in LFcin-B was obtained by further elution with 2 M NaCl. The membrane method is more rapid and offers several economic advantages.
Keywords: peptides; ANTIBACTERIAL agents; Lactoferrin

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