Antioxidant and α-Amylase Inhibitory Properties Generated from Chicken Head Proteins by Dual-Enzyme Hydrolysis

Abstract

The aim of this work was to examine the effect of different concentrations of the combination of bromelain and papain enzymes in hydrolyzing chicken head protein in terms of the physicochemical characteristics and bioactivity of the hydrolysate. A laboratory experimental method using a completely randomized design (CRD) was used in this research. In this study, chicken head protein was hydrolyzed using different combinations of bromelain (b) and papain (p), namely CHP (without hydrolysis); CHP1 (0.25% b and 0.75% p); CHP2 (0.5% b and 0.5% p); and CHP3 (0.75% b and 0.25% p). The data were analyzed using one-way analysis of variance followed by Duncan's multiple range test. The results showed that different concentrations of the combination of bromelain and papain had a significant effect (P<0.01) on pH, soluble protein concentration, peptide concentration, degree of hydrolysis, IC 50 of DPPH, reducing power, iron and copper chelating ability, and α-amylase inhibitory activity. CHP1 showed the best bioactivity with a DPPH IC 50 value of 4.62 mg/ml, iron chelating ability of 81.07%, copper chelating ability of 35.97%, and α-amylase inhibitory activity of 32.67%. While the best reducing power was at CHP2. As a result, it can be concluded that the use of a combination of bromelain and papain enzymes in chicken head protein hydrolysate has the potential to produce good bioactivity.