Isolation and identification of antimicrobial peptides derived by peptic cleavage of whey protein isolate |
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Authors: | Jérémie Théolier Riadh Hammami Philip Labelle Ismail Fliss Julie Jean |
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Affiliation: | STELA Dairy Research Centre, Nutraceuticals and Functional Foods Institute, Université Laval, Québec, QC, Canada G1V 0A6 |
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Abstract: | The antimicrobial potential of whey protein isolate hydrolyzed by gastrointestinal enzymes was determined by attempting to identify and characterize the antimicrobial peptides responsible. While tryptic and chymotryptic hydrolysates did not show antibacterial activity, whey proteins hydrolyzed for 45–90 min by pepsin exhibited significant activity. Fractionation of 60-min hydrolysate by reversed-phase high performance liquid chromatography yielded 5 fractions that were antibacterial, with minimum inhibitory concentrations comprised between 20 and 35 μg/mL. These fractions contained short peptides not previously identified as antimicrobial. Fragment 14–18 (KVAGT) of β-lactoglobulin is very close to a sequence previously identified as antibacterial and is found in antimicrobial sequences of diverse origin. Five other peptides derived from β-lactoglobulin, and one fragment from α-lactalbumin (f117–121, KVGIN), were also identified as antibacterial. The identified peptides do not match pepsin action exactly, indicating modified proteolysis of unknown origin. Protein by-products of the dairy industry offer potential for large-scale production of antimicrobial peptides. |
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