Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Abstract

Chicken collagen was explored for its possible ACE inhibitory and antioxidant activities. Flavourzyme, Neutrase and Alcalase were employed for hydrolysis of chicken collagen at predetermined times with optimal conditions for corresponding enzymes. Flavourzyme hydrolysate showed the highest antioxidant activity as measured by ORAC-FL assay (20942 μmol TE/100 g) followed by Neutrase (19207 μmol TE/100 g) and Alcalase (14352 μmol TE/100 g). Further purification by size exclusion chromatography showed that lower molecular weight fractions (between 170-776 Dalton) have highest antioxidant capacity (52787 and 44093 μmol TE/100 g for Flavourzyme and Neutrase fractions respectively). The ACE inhibitory activity of collagen hydrolysates also appeared to be higher with low molecular weight fractions (between 1200-450 Dalton) having IC50 value of about 47.2 and 59.7 μg/ml for Flavourzyme and Neutrase respectively. The present study suggests collagen as an effective candidate for both ACE inhibitory and antioxidant activity which can be employed in functional food formulations.