Antioxidant, tyrosinase inhibitory and urease inhibitory activities of camel αS-casein and its hydrolysate fractions
2019
Addar, Lydia | Bensouici, Chawki | Si Ahmed Zennia, Saliha | Haroun, Saliha Boudjenah | Mati, Abderrahmane
Camel milk casein-derived peptides display various bioactivities. The aim of this study was to investigate the effect of pancreatic enzymes hydrolysis of camel αS-casein on their antioxidant, tyrosinase inhibitory and urease inhibitory activities. Isolated αS-casein was hydrolyzed, fractionated and assayed for their antioxidant properties by using four complementary tests; namely, ABTS•+ scavenging, hydroxyl radical scavenging, ferrous ion chelating and β-carotene-linoleic acid assays. The in vitro enzymatic inhibitory activity was determined using L-DOPA as a substrate and indophenol method for tyrosinase inhibitory and urease inhibitory activity, respectively. After enzymatic hydrolysis; the activities were significantly increased whereas chymotryptic hydrolysis released peptides with higher activity than trypsin. The obtained fraction with low molecular weight (<10KDa) exhibited the highest antioxidant and enzymatic inhibitory activities. Results suggested that antioxidant properties of peptides affect their tyrosinase inhibitory activity. This study revealed that camel milk αS-casein as a great candidate for incorporation into functional foods to help in preventing disorder's caused by oxidative reactions in food and human body's.
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