Functional properties and biological activities of peptides from zebra blenny protein hydrolysates fractionated using ultrafiltration
2020
Ktari, Naourez | Ben Slama-Ben Salem, Rabab | Bkhairia, Intidhar | Ben Slima, Sirine | Nasri, Rim | Ben Salah, Riadh | Nasri, Moncef
Zebra blenny (Salaria basilisca) protein hydrolysates (ZBPH-Z) were prepared by treating zebra blenny muscles with crude alkaline protease extract from the same species. Hydrolysates were separated according to molecular weight (MW), using ultra-filtration membranes, into 5 fractions (MW > 30, 10 < MW < 30, 5 < MW < 10, 1 < MW < 5, and MW < 1 kDa, referred as F1, F2, F3, F4, and F5, respectively). Peptide fractions were analysed using reversed-phase high-performance liquid chromatography (RP-HPLC). They contained high amount of peptides with hydrophilic character. All peptide fractions had good solubility and had interfacial properties, which were correlated with concentrations and peptide lengths. Peptide fractions showed, to a variable extent, high concentration-dependent antioxidant activity in vitro. F2 showed the highest antioxidant activities. Furthermore, F1 showed the most α-amylase inhibitory activity with IC₅₀ of 71 μg/ml. F1 had the highest prolongation of both the prothrombin time and the activated partial thromboplastin time.
Show more [+] Less [-]AGROVOC Keywords
Bibliographic information
This bibliographic record has been provided by National Agricultural Library