Determination of ace inhibitory activity, antioxidant and some functional properties of protein hydrolysates obtained from different kinds of poultry egg whites

In this study, the dry matter and protein content, degree of hydrolysis (%), foaming and emulsion properties, and antioxidant properties (ABTS and DPPH radical scavenging activities) of different of types poultry (chicken, quail, duck, turkey, and goose) egg white hydrolysates prepared with alkalase enzyme were investigated. Furthermore, in vitro Angiotensin I-Converting Enzyme (ACE) and Lipoxygenase (LOX) enzyme inhibitory effects were investigated. Additionally, Differential Scanning Calorimetry (DSC) analyses were performed to determine the thermal properties of the hydrolysates, Fourier Transform Infrared Spectroscopy (FTIR) to investigate structural changes, and Scanning Electron Microscopy (SEM) to observe surface morphology. The protein amount of the hydrolysate groups (18.72-19.66 mg/mL) was found to be higher compared to the control groups (8.34- 13.88 mg/mL). The degree of hydrolysis increased with enzyme hydrolysis. In egg species, the hydrolyzation process had a significant effect on DPPH radical scavenging activity (p<0.01). Goose egg white hydrolysate exhibited the highest DPPH radical scavenging activity (78.22%). ABTS radical scavenging capacity of all samples was determined between 21.20-87.54% and the highest radical scavenging capacity belonged to chicken egg white hydrolysate (87.54%). ADE enzyme and LOX enzyme inhibition activities increased with the hydrolyzation process (p<0.01). Among all hydrolysates, chicken egg white hydrolysate exhibited the highest ACE inhibitory activity (68.64%), whereas goose egg white hydrolysate was found to have the highest LOX enzyme inhibitory activity (72.96%).