Abstract
Protein hydrolysates from fishery by-products, have resulted to be nutraceutical ingredients with potential to be applied in human nutrition; however, critical quality attributes are dependent of some process parameters such as enzyme source and degree of hydrolysis. This study reports the biochemical properties and antioxidant activity of protein hydrolysates at 10, 20 and 30% degree of hydrolysis (DH), prepared from sea catfish muscle and casein by treatment with alcalase (ALC) and a semi-purified protease extract (SPE) from intestinal tissues of sea catfish (Bagre panamensis). With SPE, the DH was reached faster than ALC regardless the protein substrate used. Sea catfish muscle (MUSC) hydrolysate made with SPE at 30% DH showed the highest antioxidant activity (DPPH: 118.8 µmoles TE/mg; ABTS: EC50 of 1.5 mg/mL). In FRAP assay, the MUSC hydrolysates produced with SPE or ALC at 20% DH showed the higher activity (0.38 and 0.40 µmoles TE/mg, respectively). MUSC hydrolysates made with SPE, contained the highest proportion of peptides with MW < 1.35 kDa, high protein content (72 to 78%,) and almost 50% of amino acids were essential. These results, suggest that intestinal proteases and muscle of marine catfish represents a potential source to elaborate antioxidant protein hydrolysates. Our results promote the full utilization of this fish species and offering a biotechnological strategy to the management and valorization of its byproducts.