Avaliação de rendimento, capacidade antioxidante e ação inibitória de acetilcolinesterase por hidrolisados de cartilagem esternal de frango

Abstract

During industrial chicken processing, by-products such as cartilage, a source of collagen, are obtained. Among the high-added-value products generated from collagen are the protein hydrolysates (PHs), derived from the hydrolysis of peptide bonds of proteins that result in free amino acids and peptides of different sizes. Due to this characteristic, PHs have demonstrated potential for several bioactive properties, such as antioxidant and enzyme modulation. The inhibition of acetylcholinesterase enzyme (AChE) is related to mitigating dementia symptoms, the incidence of Alzheimer’s disease, and s. Still, there is a lack of information about PHs action for this purpose. Thus, the main objective of this work was to evaluate how cartilage hydrolysates produced by enzymatic hydrolysis could affect the AChE activity. The chicken sternal cartilage was hydrolyzed for 4 hours (i-Alcalase®, pH 8,0, 50°C, 1.8% E:S; ii- Flavourzyme®, pH 7,0, 50°C, 1.8%E:S). After hydrolysis, the solution was submitted to thermal inactivation (90°C/15 min), followed by centrifugation and lyophilization of the supernatant. Results showed hydrolysis yields equal to 97.42% (Alcalase®) and 93.71% (Flavourzyme®), demonstrating greater digestion capacity of the by-product by with Alcalase® . Concerning antioxidant capacity, the following results were obtained: DPPH 55.78 μmolET.g- 1 (Alcalase®) and 53.18 μmolET.g-1 (Flavourzyme®); FRAP 12.20 μmolET.g-1 (Alcalase®) and 11.24 μmolET.g-1 (Flavourzyme®); ABTS 30,91 μmolET.g-1 (Alcalase®) and 31,18 μmolET.g-1 (Flavourzyme®); TBARS 55,89 μmolET.g-1 (Alcalase®) and 74,20 μmolET.g-1 (Flavourzyme®). The AChE inhibition by the PHs was equal to 37.05%, 45.57%, and 60.65% for Alcalase® at 20, 30 and 40 mg.mL-1, respectively, and 28.20%, 29.71%, and 32.47% for Flavourzyme® at the same concentrations. This demonstrates the high potential of Alcalase® in hydrolyzing the chicken sternal cartilage, resulting in higher antioxidant capacity, as well as, resulting in higher antioxidant capacity and AChE inhibition bioactivity. The analysis of the amino acid profile of the hydrolysates was performed by HPLC and 18 amino acids were identified (6 hydrophilic and 12 hydrophobic), and the amino acid content positively corroborated with the greater AChE influence action by the hydrolysate produced whith Alcalase®.