Free radical scavenging and antiproliferation of protein hydrolysate from chicken feather meal prepared by alkaline protease

Abstract

This research was aimed to determine the optimal conditions of enzymatic hydrolysis for the preparation of protein hydrolysates from chicken feather meal that possessed antioxidant and antiproliferative inhibition activity. Chicken feather meal hydrolysate was prepared by Protease G6 digestion and separated into five fractions by membrane ultrafiltration. Antioxidant peptide activities were analyzed using three techniques DPPH, ABTS, and NO. The low-molecular-weight fraction MW < 3 kDa showed the best antioxidant activity. In the study of the five malignant cell lines, the protein hydrolysate MW <3 kDa exhibited strongest antiproliferative activity for human malignant cell line BT474 (breast) cancer. The peptides were identified by mass spectrometry techniques, and amino acid sequences were characterized into eleven peptide chains. The search for more potent antioxidant properties of protein hydrolysates continues for ingredients in the formulation of functional food and also for nutraceutical uses in controlling of oxidative stress in the body.