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Isracidin [id=CAA0038]

Synonym: Alphas1-casein f(1-23)

Producer Organism : Native Protein : Production Method :
Bufala αs1-casein Enzymatic hydrolysis and Purification with LC method
Activity : Not determined
Target Organisms :

Unavailable data

Description :
Production method: Natural chymosin hydrolysis and purification with LC method.

Not tested
Length : 23 Mass (Da): 2 652.86 Common Amino Acids : PL
Isolectric Point : 11.65 Net Charge : 4 Absent Amino Acids : ACDMSTWY
Basic Residues : 5 Acidic Residues : 1 Hydrophobic Residues : 7
Polar Residues : 4 Boman Index : -43.27 Hydropathy Index : -0.783
Aliphatic Index : 97.39 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

Characterisation and cytomodulatory properties of peptides from Mozzarella di Bufala Campana cheese whey

Cited Entries: CAA0038

Authors:De Simone, C., Picariello, G., Mamone, G., Stiuso, P., Dicitore, A., Vanacore, D., Chianese, L., Addeo, F., Ferranti, P.
Journal: Journal of Peptide Science 2009, 15(3).
Abstract: Bioactive peptides are present in a latent state, encrypted within the amino acid sequence of milk proteins, requiring enzymatic proteolysis for their release. They can be produced by gastrointestinal digestion or food processing, thus they can be present in fermented milks, cheese and also in the by-products of dairy industry such as waste whey. The spectrum of biological activity covered by milk-derived peptides is extremely wide, including antibacterial, immunostimulating, antihypertensive, antithrombotic and opioid actions. However, the characterisation of milk-derived peptides with classical analytical methodologies is severely challenged by the complexity of the milk protein fraction and by the wide dynamic range of relative peptide abundance in both dairy products and by-products. Here we report the characterisation of the peptide fraction released in the whey during the different production stages of Mozzarella di Bufala Campana cheese. The peptide extracts were separated by RP HPLC and analysed by MS in order to identify the peptides produced and to trace the pathway of formation of potential bioactive peptides. The antioxidant properties and the modulatory effect on the cell cycle exerted by the peptide extracts were also studied in CaCo2 cell line. We found that a significant antiproliferative effect on CaCo2 was exerted by Mozzarella di Bufala waste whey peptides.
Keywords: river buffalo milk; Mozzarella di Bufala Campana cheese; bioactive peptides; cytomodulatory activity; Ms; cheese whey

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