EVALUATION OF THE BIOACTIVE POTENTIAL OF PEPTIDES FRACTIONS OBTAINED FROM TRIGGERFISH (Balistes capriscus) COPRODUCTS
Name: MONIQUE LOPES RIBEIRO
Publication date: 30/04/2024
Examining board:
Name |
Role |
|---|---|
| ALEXANDRE MARTINS COSTA SANTOS | Presidente |
| BARTOLOMEU WARLENE SILVA DE SOUZA | Examinador Externo |
| JAIRO PINTO DE OLIVEIRA | Examinador Externo |
| MARIA APARECIDA CICILINI | Examinador Externo |
| MARIA GABRIELA BELLO KOBLITZ | Examinador Externo |
Summary: Fish industry generates a significant amount of waste which have high biological value and potential for industrial use. The aim of this study was to evaluate the antioxidant and ACE-inhibitory activities of peptide fractions from triggerfish (Balistes capriscus) processing coproducts. Molecular mass distribution of the proteins extracted from fish viscera was determined by molecular exclusion chromatography presenting fractions with a wide range of molecular mass (<1.2 kDa to > 440 kDa). Soluble Protein Extract (SPE) was hydrolysate using papain (HP), bromelain (HB) and trypsin (HT) (3% p.p-1, 6h). Samples were fractionated (>100 MWCO, 30–100, 10-30 and < 10 MWCO). Antioxidant activity of fractions was evaluated and fraction SPE4 (<10 MWCO) showed the highest value of Trolox Equivalent Antioxidant Capacity - TEAC (10,157.7 mol Trolox. g-1) and Ferric Reducing Antioxidant Power - FRAP (1,588.71 mol FeSO4. g1 ). SPE and hydrolysates (<10MWCO) were separated by ion-exchange chromatography. Fraction F1 showed the highest value for TEAC capacity (8,839.04 mol Trolox. g-1) and FRAP (1,749.94 mol FeSO4. g-1). ACE-inhibitory activity was evaluated for non-hydrolysate and hydrolysate fractions. Fractions F3, F5 and HP3 showed the lowest IC50 value (30.1, 42.7 e 37.7 µg, respectively). Antimicrobial activity was observed in samples SPE (against S. aureus), F1 and F4 (against Pseudomonas sp.) It was identified 20 amino acid sequences that could contribute to the biological activity of the peptide fractions. Proteins extracted from triggerfish viscera demonstrated to be a good source of bioactive peptides that may have food and pharmaceutical applications.
