Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation.

Four roe protein isolates (RPIs) from skipjack tuna were prepared using isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) (ISP) at different pH points to evaluate their physicochemical and functional properties and in vitro bioactivities. Moisture (<6.3%) and protein (71%-77%) content were maintained. Sulfur, sodium, phosphorus, and potassium were the major elements, and glutamic acid and leucine were the prevalent amino acids (12.2-12.8 and 9.6-9.8 g/100 g protein, respectively) in RPIs. RPI-1 showed the highest buffering capacity at pH 7-12. RPIs and casein showed similar water-holding capacities. At pH 12, RPI-1(pH 11/4.5) showed the highest solubility, followed by RPI-3(pH 12/4.5), RPI-2(pH 11/5.5), and RPI-4(pH 12/5.5) (p < .05). Oil-in-water emulsifying activity indices of RPI-1 and RPI-3 significantly differed. At pH 2 and 7-12, pH-shift treatment improved the food functionality of RPIs, which was superior to positive controls (casein and hemoglobin). RPI-1 showed ABTS+ radical scavenging (102.7 μg/ml) and angiotensin-converting enzyme inhibitory activities (44.0%).