RESUMEN
Fish by-products are excellent sources of collagen. Acid-soluble collagen (ASC) derived from a mixed by-product of different fish species was hydrolyzed to obtain peptide fractions and evaluate their biological and functional activities. All fractions obtained (F1: ≥30, F2: 10-30, F3: 5-10, F4: 1-5, and F5: ≤1kDa) exhibited antioxidant activity at concentrations of 5, 10, and 15 mg/mL. However, F5 registered the highest reducing power (absorbance 0.366) and hydroxyl-radical-scavenging activity (91%) at 15 mg/mL; whereas the highest DPPH scavenging activity (81%) was also detected in F5 at 5 mg/mL. The solubility of F1, F2, and F3 was ≥ 95% at pH 7. The highest foaming capacity (78%), foaming stability (60%), and emulsion stability index (42 min) were registered for F1. However, the highest emulsifying activity index (130 m2/g) was for F3. These results place collagen obtained from a mixed by-product of different fish species as a potential biotechnological alternative for the industry.
Asunto(s)
Antioxidantes/farmacología , Colágeno/química , Productos Pesqueros , Proteínas de Peces/química , Péptidos/química , Péptidos/farmacología , Aminoácidos/análisis , Animales , Antibacterianos/química , Antibacterianos/farmacología , Antioxidantes/química , Emulsionantes/química , Proteínas de Peces/farmacología , Depuradores de Radicales Libres/química , Concentración de Iones de Hidrógeno , Hidrólisis , Radical Hidroxilo/química , Hidrolisados de Proteína/química , SolubilidadRESUMEN
A Mucuna pruriens protein concentrate was hydrolyzed with a digestive (pepsin-pancreatin) enzymatic system. The soluble portion of the hydrolysate was fractionated by ultrafiltration and the ultrafiltered peptide fraction (PF) with lower molecular weight was purified by reversed-phase high-performance liquid chromatography. The PF obtained were evaluated by testing the biological activity in vitro. Fractions showed that the ability to inhibit the angiotensin-converting enzyme had IC50 values that ranged from 2.7 to 6.2 µg/mL. Trolox equivalent antioxidant capacity values ranged from 132.20 to 507.43 mM/mg. The inhibition of human platelet aggregation ranged from 1.59% to 11.11%, and the inhibition of cholesterol micellar solubility ranged from 0.24% to 0.47%. Hydrophobicity, size, and amino acid sequence could be factors in determining the biological activity of peptides contained in fractions. This is the first report that M. pruriens peptides act as antihypertensives, antioxidants, and inhibitors for human platelet aggregation and cholesterol micellar solubility in vitro.