α-La f(108-113) [id=ALA0008]

Producer Organism : Native Protein : Production Method :
Cow α-lactalbumin Not produced
Activity : Not determined
Target Organisms :

Unavailable data

Description :
Predicted as antimicrobial
Length : 6 Mass (Da): 649.79 Common Amino Acids : ASKLCE
Isolectric Point : 6.23 Net Charge : Absent Amino Acids : DFGHIMNPQRTVWY
Basic Residues : 1 Acidic Residues : 1 Hydrophobic Residues : 2
Polar Residues : 2 Boman Index : -7.75 Hydropathy Index : -0.017
Aliphatic Index : 81.67 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

Milk proteins as precursors of bioactive peptides

Cited Entries: LFB0004, LFB0005, LFB0007, LFB0094, LFB0121, ALA0003, ALA0007, ALA0008

Authors:Dziuba, M., Dziuba, B., Iwaniak, A.
Journal: ACTA Scientiarum Polonorum, Technologia Alimentaria 2009, 8(1).
Abstract: Milk proteins, a source of bioactive peptides, are the subject of numerous research studies aiming to, among others, evaluate their properties as precursors of biologically active peptides. Physiologically active peptides released from their precursors may interact with selected receptors and affect the overall condition and health of humans. By relying on the BIOPEP database of proteins and bioactive peptides, developed by the Department of Food Biochemistry at the University of Warmia and Mazury in Olsztyn (www.uwm.edu.pl/biochemia), the profiles of potential activity of milk proteins were determined and the function of those proteins as bioactive peptide precursors was evaluated based on a quantitative criterion, i.e. the occurrence frequency of bioactive fragments (A). The study revealed that milk proteins are mainly a source of peptides with the following types of activity: antihypertensive (Amax = 0.225), immunomodulating (0.024), smooth muscle contracting (0.011), antioxidative (0.029), dipeptidyl peptidase IV inhibitors (0.148), opioid (0.073), opioid antagonistic (0.053), bonding and transporting metals and metal ions (0.024), antibacterial and antiviral (0.024), and antithrombotic (0.029). The enzymes capable of releasing bioactive peptides from precursor proteins were determined for every type of activity. The results of the experiment indicate that milk proteins such as lactoferrin, α-lactalbumin, β-casein and κ-casein hydrolysed by trypsin can be a relatively abundant source of biologically active peptides.

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