ArticleMarine drugs2025
Production of Protein Hydrolysates from Cod Backbone Using Selected Enzymes: Evaluation of Antioxidative and Antimicrobial Activities of Hydrolysates.
Article in Marine drugs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Identification and In Silico Selection of Novel Antioxidant Peptides from Asian Swamp Eel Bone: Quantum Chemical Calculations, Molecular Docking, and Zebrafish Model Validation.Antioxidants (Basel, Switzerland) · 2026Article
- Sustainability-oriented recovery of antioxidant and ACE-inhibitory low-molecular-weight peptide fractions fromFrontiers in nutrition · 2026Article
- Marine Antimicrobial Peptides: Advances in Discovery, Multifunctional Mechanisms, and Therapeutic Translation Challenges.Marine drugs · 2025Review
- Marine Bioactive Peptides in the Regulation of Inflammatory Responses: Current Trends and Future Directions.Proteomes · 2025Review
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Authors and funding
5 authors.
Funding
Abstract
In the fish industry, up to 70% of all fish end up as side-streams such as backbones, heads, and viscera. To reduce the quantities of side-streams, a higher utilization degree of fish is needed. The aim of this study was to use cod backbone for an enzymatic production of bioactive hydrolysates with antioxidative and/or antimicrobial properties. Three different enzymes were applied (Alcalase, Neutrase, and Protamex), and hydrolyses were carried out within the enzyme's optima for pH and temperature for 0.5-6 h. The efficiency of the enzyme treatment was evaluated based on the protein extraction yield (PEY), the degree of hydrolysis (DH), and antioxidant activity using two different in vitro assays (1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging and iron chelation) and antimicrobial activity determined by minimum inhibitory concentration (MIC) and disk diffusion assays. Selected hydrolysates showing activity were evaluated with respect to amino acid composition and molecular weight. Alcalase-treated samples had the highest PEY (3 h, 63.5 ± 4.5%) followed by Protamex-treated samples (3 and 6 h; 51.9 ± 5.5% and 56.5 ± 4.5%); the lowest PEY was obtained with Neutrase (3 and 6 h; 30.4 ± 1.9% and 34.7 ± 3.4%). No clear relationship was observed between the PEY and DH. All hydrolysates had antioxidant activities. For radical scavenging activity, Protamex-treated hydrolysate showed the lowest IC
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