Techno-functional, antioxidant, and amino acid characterization of hydrolyzed bioactive peptides from coconut (Cocos nucifera L.) meal protein

In this study, the techno-functional characteristics and nutritional value of coconut meal protein (CMP) and the obtained polypeptides by alcalase (H-Alc), trypsin (H-Try), pancreatin (H-Pan), and pepsin (H-pep) were investigated. The degree of hydrolysis was influenced by the enzyme type, where an order of H-Pan (37.5%) > H-Alc (33.2%) > H-Try (29.9%) > H-Pep (23.4%) was observed. Hydrolysates' solubility, emulsifying properties, foaming capacity, water-holding capacity (WHC), and oil-binding capacity (OHC) were substantially improved after hydrolysis. The techno-functional properties of CMP were affected by pH and the enzyme type. H-Pan and H-Pep samples exhibited the highest WHC (6.5 g water per g) and oil-holding capacity (OHC, 7.1 g oil per g). Different groups of functional amino acids, including essential (EAAs), antioxidant (AAAs), hydrophobic (HAAs), negatively-charged (NCAAs), and positively-charged (PCAAs), and the protein efficiency ratio (PER) in hydrolysates were influenced by the type of protease. H-Pan showed the highest antioxidant amino acids (AAAs = 125.3 mg g^-1; NCAAs = 261.0 mg g^-1) and nutritional value (with EAAs of 295.1 mg g^-1; an EAA to total amino acid (TAA) ratio of 35.3% and a PER value of 2.4). Enzymatic hydrolysis, in general, led to a considerable enhancement in the antioxidant activity of hydrolysates compared to that of the primary proteins. Regardless of the type of antioxidant assay, the most enhanced antioxidant capacity was attributed to H-Pan hydrolysates with DPPH, hydroxyl (OH), ABTS⁺, and nitric oxide (NO) radical scavenging activities of 82.0%, 71.8%, 82.9%, and 49.8%, respectively. However, other hydrolysates did not show significantly different antioxidant activities (P > 0.05).