Production of Protein Hydrolysate Containing Antioxidant and Angiotensin -I-Converting Enzyme (ACE) Inhibitory Activities from Tuna (Katsuwonus pelamis) Blood

Tuna blood (TB) was subjected to enzymatic hydrolysis. The effects of the relationship of hydrolysis time (30–180 min) and enzyme concentration (0.5–3.0% w/w protein) on the degree of hydrolysis (DH), yield, antioxidant and angiotensin-I-converting enzyme (ACE) inhibitory activities were determined. The response surface methodology (RSM) showed that TB hydrolysis’s optimum conditions were hydrolysis for 180 min and Alcalase, Neutrase or Flavourzyme at 2.81%, 2.89% or 2.87% w/w protein, respectively. The hydrolysates with good DH (40–46%), yield (3.5–4.6%), the IC50 of DPPH (0.8–1.6 mg/mL) and ABTS (1.0–1.4 mg/mL) radical scavenging activity, ferric reducing antioxidant power (FRAP) value (0.28–0.65 mmol FeSO4/g) and IC50 of ACE inhibitory activity (0.15–0.28 mg/mL) were obtained with those conditions. The TB hydrolysate using Neutrase (TBHN) was selected for characterization in terms of amino acid composition, peptide fractions and sensory properties. The essential, hydrophobic and hydrophilic amino acids in TBHN were ~40%, 60% and 20% of total amino acids, respectively. The fraction of molecular weight <1 kDa showed the highest antioxidant and ACE inhibitory activities. Fishiness and bitterness were the main sensory properties of TBHN. Fortification of TBHN in mango jelly at ≤ 0.5% (w/w) was accepted by consumers as like moderately to like slightly, while mango jelly showed strong antioxidant and ACE inhibitory activities. TBHN could be developed for natural antioxidants and antihypertensive peptides in food and functional products.