Protein Characteristics and Bioactivity of Fish Protein Hydrolysates from Tra Catfish (Pangasius hypophthalmus) Side Stream Isolates

Funding Information: This research was supported by the UNESCO GRÓ−Fisheries Training Programme and The Icelandic Food Research Fund in Iceland (Matvælasjóður). Publisher Copyright: © 2022 by the authors.Enzymatic hydrolysis is a novel method to recover highly potent bioactive fish protein hydrolysates (FPHs) from fish processing side-streams. The common way of producing FPHs directly from fish side-streams may be inappropriate due to the excess of lipids and pro-oxidants, especially in lipid-rich streams, as obtained from Tra catfish. This study aimed to optimise the hydrolysis conditions for a commercial enzyme (Alcalase® 2.4 L) (enzyme concentrate, temperature, and time) in FPH production from the fish protein isolate obtained from Tra catfish dark muscle (DM-FPI) using the pH-shift method. The degree of hydrolysis (DH), protein recovery (PR), and antioxidant properties, including DPPH radical scavenging activity (DPPH-RSA) and total reducing power capacity (TRPC), were measured to evaluate the effects of the hydrolysis conditions on the FPHs. Optimal hydrolysis was obtained at an enzyme/substrate protein ratio of 3% (v/w) and a hydrolysis temperature of 50 °C for 3 h. The FPHs obtained from different substrates, including DM-FPI, abdominal cut-off (ACO) FPI, and head and backbone blend (HBB) FPI, had similar DHs under these optimum conditions, ranging from 22.5% to 24.0%. However, the FPH obtained from abdominal cut-off isolate (ACO-FPH) showed the highest PR of 81.5 ± 4.3% and the highest antioxidant properties, with a DPPH-RSA of 86.1 ± 1.6% and a TRPC of 6.4 ± 0.4 equivalent mg vitamin C/g protein. The resulting FPHs present a natural source of antioxidants with great potential for food applications, especially the ACO-FPH. In addition, all FPHs had excellent amino acid profiles, indicating strong potential for their use as supplements. Tra catfish protein-rich side-streams can thus be processed into high-value bioactive FPHs using Alcalase for human consumption.Peer reviewe