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β-casein f(80-89) [id=CAB0006]

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

Gram-positive:Active against Listeria monocytogenes ATCC7644, Listeria monocytogenes M, Listeria monocytogenes LMG15139, Listeria monocytogenes LMG16783, Listeria monocytogenes LMG13304, Listeria monocytogenes 2231, Lactococcus lactis subsp. lactis LMG21206, Lactobacillus curvatus-HG.

NOTE: No activity against Staphylococcus aureus-HG, Lactobacillus curvatus CWBI-B28, Lactobacillus curvatus CWBI-B28m, Lactobacillus plantarum-HG, Lactobacillus brevis-H28, Escherichia coli-HG, Pseudomonas sp. 55, Saccharomyces cerevisiae BK24, Penicillium spp. BKS-TAN2, Aspergillus niger BKS-TAN31 .

Description :
Production method: Lactobacillus curvatus enzyme hydrolysis and purification with LC method.

Length : 10 Mass (Da): 1 111.64 Common Amino Acids : P
Isolectric Point : 6.11 Net Charge : Absent Amino Acids : ACDEGHIKMRSWY
Basic Residues : 0 Acidic Residues : 0 Hydrophobic Residues : 4
Polar Residues : 2 Boman Index : 1.23 Hydropathy Index : 0.25
Aliphatic Index : 97 Instability Index : 0 Extinction Coefficient :
Absorbance 280nm : 0

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

Production of three anti-listerial peptides by Lactobacillus curvatus in MRS broth

Cited Entries: CAB0006

Authors:Ghalfi, H., Benkerroum, N., Ongena, M., Bensaid, M., Thonart, P.
Journal: Food Research International 2010, 43(1).
CrossRef External Link
Abstract: Three novel bioactive peptides (BAP13) from Lactobacillus curvatus CWBI-B28 were isolated and purified using de Man, Rogosa and Sharp (MRS) broth by a three-step protein purification protocol including ammonium sulfate precipitation, hydrophobic C18 Sep-Pak column and reverse-phase high performance liquid chromatography (RP-HPLC). This procedure allowed the recovery of chromatographically pure antimicrobial peptides with the yields of 19%, 10% and 15% of BAP1, BAP2 and BAP3, respectively. The respective apparent molecular masses as determined by tricine-SDS-polyacrilamide gel electrophoresis were 6365, 3426 and 3496. N-terminal amino acid sequencing of the BAPs and comparison of their sequences with those of international data bases indicated that BAP1 is more likely to be a casein-derived bioactive protein produced upon hydrolysis of the tryptone present in MRS broth by Lb. curvatus CWBI-B28 during active growth. However, the identity of BAP2 and BAP3 could not be determined with certainty; yet, they would be novel bacteriocins not fitting in any of the known classes of bacteriocins. Therefore, this strain would have the ability to produce intrinsic antimicrobial substances and also release bioprotective peptides from milk-proteins upon cultivation in milk or casein-containing food products due to its proteolytic activity. Thus, Lb. curratus CWBI-B28 possesses a good potential to be used in food preservation and safety.
Keywords: Lactobacillus curvatus; Casein-derived bioprotective peptides; Bacteriocin; Listeria monocytogenes; purification

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