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Abstract
Fish viscera are usually discarded as waste, causing environmental problems, or as low-value by-products. This study describes a self-sufficient and zero waste approach to obtain enzymes and protein hydrolysates from fish by-products. Firstly, recovery steps of viscera enzymatic extract were applied, and the resulting raw extract was stable at a pH range of 8–9 and at temperatures between 40 and 50 °C. The application of the extracted enzymes and alcalase on fish by-products hydrolysis was also determined. The selected conditions for the enzymatic hydrolysis were 10% (E/S) for 6 h using viscera enzymatic extract and 3% (E/S) for 2 h using alcalase. Fish protein hydrolysates (FPH) proved to have a notable antioxidant capacity with similar activity, ~11 mg ascorbic acid/g dry extract (ABTS assay) and ~150 mg Trolox/g dry extract (ORAC assay). FPH were also able to inhibit the angiotensin-converting enzyme, however, alcalase hydrolysates revealed a higher antihypertensive potential, IC50 of 101 µg of protein/mL. In general, FPH obtained by both enzymes systems maintained these bioactivities after the passage throughout a simulated gastrointestinal tract. The hydrolysates also displayed important technological properties, namely oil absorption capacity (~1 g oil/g sample) and emulsifying property (~40%). Therefore, it will be conceivable to use fish by-products based on a circular economy approach to generate added value compounds for animal and human nutrition
Original language | English |
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Article number | 1155 |
Number of pages | 16 |
Journal | Molecules |
Volume | 28 |
Issue number | 3 |
DOIs | |
Publication status | Published - Feb 2023 |
Keywords
- Bioactive peptides
- Protein hydrolysis
- Technological properties
- Viscera
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Dive into the research topics of 'Fish by-products: a source of enzymes to generate circular bioactive hydrolysates'. Together they form a unique fingerprint.Projects
- 1 Finished
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MOREPEP: Valorização de subprodutos animais com o desenvolvimento de péptidos de valor e sustentáveis
Pintado, M. M. (PI)
1/12/16 → 31/05/20
Project: Research