Angiotensin-Converting Enzyme Inhibition In Vitro by Protein Hydrolysates and Peptide Fractions from Mojarra of Nile Tilapia (Oreochromis niloticus) Skeleton.

Mojarra of Nile tilapia (Oreochromis niloticus) skeleton was used as protein source for the preparation of protein hydrolysates and peptide fractions with angiotensin-converting enzyme (ACE) inhibitory activity. The flour presented a content of 34.92% protein and a brightness (luminosity, L*) of 82.29. Protein hydrolysates were obtained from the protein-rich flour with the enzymes Flavourzyme® and Alcalase® reaching degree of hydrolysis (%DH) of 52% and 67% at 100 min of reaction, respectively. Both hydrolysates showed low-molecular-weight (MW) peptides estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The hydrolysates obtained with Flavourzyme at 60 min and at 80 min with Alcalase showed greater ACE inhibitory activity with IC50 values of 0.238 and 0.344 mg/mL, respectively. The peptide fraction A (MW >10 kDa) with Flavourzyme and fraction B (MW = 10-5 kDa) with Alcalase obtained by ultrafiltration of hydrolysates with higher DH presented IC50 of 0.728 and 0.354 mg/mL, respectively, whereas peptide fraction C (MW = 5-3 kDa) with both enzymes hydrolysates with greater ACE inhibitory activity showed IC50 values of 0.470 and 0.634 mg/mL. The components obtained in this study could be used as functional ingredients in the design and development of functional foods.

Influence of extrusion on the bioactive compounds and the antioxidant capacity of the bean/corn mixtures.

The aim of this investigation was to examine the influence of extrusion on the bioactive compounds and the antioxidant capacity of bean/corn mixtures. Whole bean flour and nixtamalized corn were mixed in a 60:40 proportion and extrusion was performed in different moisture (14.5%, 15.4%, 17.1% and 18.0%) and temperature (150°C, 160°C, 170°C, 180°C and 190°C) conditions in order to find the optimal extrusion conditions. According to their functional properties and antioxidant status, the mixtures 142°C/16.3% H, 170°C/16.3% H and 198°C/16.3% H were defined as optimal, moderate and bad, respectively. Total polyphenols and flavonoids in the mixture of 142°C/16.3% H (15.09±1.7 mg gallic acid equivalent [GAE]/g dry weight [DW] and 1.57±0.2 mg catechin equivalent [CE]/g DW) were significantly higher (P<0.05) than in the sample 170°C/16.3% H (9.42±1.1 mg GAE/g DW and 1.4±0.1 mg CE/g DW) and the mixture 198°C/16.3% H (6.46±0.8 mg GAE/g DW and 0.78±0.1 mg CE/g DW). The antioxidant activity (37.02±3.8 and 25.01±2.5 µM Trolox equivalent [TE]/g DW) of mixture 142°C/16.3% H, determined by the cupric reducing antioxidant capacity with Trolox equivalent antioxidant capacity and ß-carotene-linoleic acid (ß-carotene,% of inhibition) assays, was significantly higher (P<0.05) than in 170°C/16.3% H (25.69±2.8 and 17.02±1.8 µM TE/g DW) and in mixture 198°C/16.3% H (13.93±1.5 and 8.94±0.9 µM TE/g DW), respectively. The free polyphenols, flavonoids and the antioxidant activities showed lower results than the hydrolyzed ones. The correlation coefficients between polyphenols, flavonoids, and cupric reducing antioxidant capacity capacities were between 0.93 and 0.99. In cereal proteins extracted and separated by electrophoresis, some differences were found in the sodium dodecyl sulfate-protein bands in the region from 36 to 45 kDa for 142°C/16.3% H, in comparison with other samples. Therefore, there is a need to find such conditions for the extrusion procedures that would take into consideration the contents of the bioactive compounds and the antioxidant capacity in the end product.