Physicochemical and biological properties of eel by-products protein hydrolysates: Potential application to meat product preservation
European eel by-products have been hydrolysed in order to produce novel bioactive peptides with antibacterial and antioxidant activity. Protein hydrolysates from Anguilla by-products obtained by treatment with Savinase® (PHAB-s) have high protein content than that produced with Protamex® (PHAB-p). F...
Published in: | Waste and Biomass Valorization |
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Main Authors: | , , , , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Springer Nature
2020
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Subjects: | |
Online Access: | http://hdl.handle.net/10261/175137 https://doi.org/10.1007/s12649-018-0424-5 https://doi.org/10.13039/501100010198 |
Summary: | European eel by-products have been hydrolysed in order to produce novel bioactive peptides with antibacterial and antioxidant activity. Protein hydrolysates from Anguilla by-products obtained by treatment with Savinase® (PHAB-s) have high protein content than that produced with Protamex® (PHAB-p). Furthemore, both protein hydrolysates had a high percentage of essential amino acids. In addition, results indicated that PHAB-s and PHAB-p exhibited different degrees of antioxidant activities, evaluated by several antioxidant assays. Thus, PHAB-s displayed high antioxidant activity, in terms of DPPH-radical scavenging effect (IC50 = 5.2 mg/ml), β-carotene bleaching inhibitory effect (CI50 = 4.4 mg/ml) and metal chelating activity. At 10 mg/ml, PHAB-p showed the highest reducing power. Antibacterial activities of PHAB-s and PHAB-p were also evaluated. PHAB-s showed the most important inhibitory effects against seven bacterial species. The application of PHAB-s and PHAB-p on minced meat as preservative reduced the lipid oxidation and inhibited the microbial growth during chilled storage for 11 days. This work was funded by the Ministry of Higher Education and Scientific Research, Tunisia and the Spanish Ministry of Economy, Industry and Competitiveness under project AGL2014-52825-R. Peer reviewed |
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