ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K

Mahmood Rahimi , Seyed Mahmood Ghaffari , Maryam Salami , Seyed Jafar Mousavy , Amir Niasari-Naslaji , Raheleh Jahanbani , Saeed Yousefinejad , Mohammadreza Khalesi , Ali Akbar Moosavi-Movahedi

AbstractThe aim of this study was to evaluate the effects of enzymatic hydrolysis of camel whole casein on their antioxidant and angiotensin-converting enzyme (ACE)-inhibitory properties. Whole camel casein was hydrolyzed by proteinase K (PK), and the hydrolysates were fractionized by ultrafiltration membranes into three fractions. Semi-preparative reversed-phase high-performance liquid chromatography (RP-HPLC) was used to differentiate the mixture of peptides in the 3 kDa permeate fractions. A fraction (F4) with potentials of ACE-inhibitory activity (IC50 = 73 μg.mL−1) and radical scavenging activity (IC50 = 6.8 μg.mL−1) was selected for further purification and fractionation. The fraction F4C obtained from a second step purification of F4 showed strong ACE-inhibitory activity (IC50 = 36 μg.mL−1) as well as radical scavenging activity (IC50 = 3.3 μg.mL−1). The results of this study suggest that whole camel casein can be considered as a promising source for the production of peptides with potential of ACE-inhibitory and antioxidant activities.

Mots clés: Camel milk; Casein; Peptide; Protease; Angiotensin-converting enzyme

Domaines: Sciences du Vivant [q-bio]

Mahmood Rahimi, Seyed Mahmood Ghaffari, Maryam Salami, Seyed Jafar Mousavy, Amir Niasari-Naslaji, et al.. ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K. Dairy Science & Technology, 2016, 96 (4), pp.489-499. ⟨10.1007/s13594-016-0283-4⟩. ⟨hal-01532469⟩